---
OA_type: closed access
_id: '21762'
abstract:
- lang: eng
text: Bacteria, like eukaryotes, use conserved cytoskeletal systems for intracellular
organization. The plasmid-encoded ParMRC system forms actin-like filaments that
segregate low–copy number plasmids. In multicellular cyanobacteria such as Anabaena
sp., we found that a chromosomally encoded ParMR system has evolved into a cytoskeletal
system named CorMR with a function in cell shape control rather than DNA segregation.
Live-cell imaging, in vitro reconstitution, and cryo–electron microscopy revealed
that CorM formed dynamically unstable, antiparallel double-stranded filaments
that were recruited to the membrane by CorR through an amphipathic helix conserved
in multicellular cyanobacteria. CorMR filaments were regulated by MinC, which
excluded them from the poles and division plane. Comparative genomics indicated
that the repurposing of ParMR and Min systems coevolved with cyanobacterial multicellularity,
highlighting the evolutionary plasticity of cytoskeletal systems in bacteria.
acknowledged_ssus:
- _id: Bio
- _id: ScienComp
- _id: EM-Fac
- _id: LifeSc
acknowledgement: "We thank all members of the Loose lab at ISTA for helpful discussions;
M. Kojic for critical reading of the manuscript; A. Herrero (Sevilla University)
for sharing her extensive BACTH plasmid library and other plasmids, as well as cyanobacterial
strains; T. Dagan and F. Nies (both Kiel University) for sharing cyanobacterial
strains and plasmids and for valuable discussions; N. Sapay and A. Michon for providing
the Amphipaseek code, which enabled us to perform our large-scale amphipathic helix
screen of cyanobacterial CorR proteins; V.-V. Hodirnau for support in cryo-ET data
collection; and J. Hansen for advice about cryo-EM data processing.\r\nThis work
was supported by the Scientific Service Units (SSU) of ISTA through resources provided
by the Imaging & Optics Facility (IOF), the Scientific Computing (SciComp), the
Electron Microscopy Facility (EMF), and the Lab Support Facility (LSF). This work
was funded by the European Union’s Horizon 2020 research and innovation program
(Marie Skłodowska-Curie grant 101034413 to B.L.S.); the European Research Council
(ERC) of the European Union (grant ActinID 101076260 to F.K.M.S.); the Swiss National
Science Foundation (starting grant TMSGI3_226208 to G.L.W.); and the Jean-Jacques
et Letitia Lopez-Loreta Foundation (G.L.W.)."
article_number: eaea6343
article_processing_charge: No
article_type: original
author:
- first_name: Benjamin L
full_name: Springstein, Benjamin L
id: b4eb62ef-ac72-11ed-9503-ed3b4d66c083
last_name: Springstein
orcid: 0000-0002-3461-5391
- first_name: Manjunath
full_name: Javoor, Manjunath
id: 305ab18b-dc7d-11ea-9b2f-b58195228ea2
last_name: Javoor
orcid: 0000-0003-2311-2112
- first_name: Daniela
full_name: Megrian, Daniela
last_name: Megrian
- first_name: Roman
full_name: Hajdu, Roman
id: ffab949d-133f-11ed-8f02-94de21ace503
last_name: Hajdu
- first_name: Dustin M.
full_name: Hanke, Dustin M.
last_name: Hanke
- first_name: Bettina
full_name: Zens, Bettina
id: 45FD126C-F248-11E8-B48F-1D18A9856A87
last_name: Zens
orcid: 0000-0002-9561-1239
- first_name: Gregor L.
full_name: Weiss, Gregor L.
last_name: Weiss
- first_name: Florian Km
full_name: Schur, Florian Km
id: 48AD8942-F248-11E8-B48F-1D18A9856A87
last_name: Schur
orcid: 0000-0003-4790-8078
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
citation:
ama: Springstein BL, Javoor M, Megrian D, et al. Repurposing of a DNA segregation
machinery into a cytoskeletal system controlling cell shape. Science. 2026;392(6795).
doi:10.1126/science.aea6343
apa: Springstein, B. L., Javoor, M., Megrian, D., Hajdu, R., Hanke, D. M., Zens,
B., … Loose, M. (2026). Repurposing of a DNA segregation machinery into a cytoskeletal
system controlling cell shape. Science. AAAS. https://doi.org/10.1126/science.aea6343
chicago: Springstein, Benjamin L, Manjunath Javoor, Daniela Megrian, Roman Hajdu,
Dustin M. Hanke, Bettina Zens, Gregor L. Weiss, Florian KM Schur, and Martin Loose.
“Repurposing of a DNA Segregation Machinery into a Cytoskeletal System Controlling
Cell Shape.” Science. AAAS, 2026. https://doi.org/10.1126/science.aea6343.
ieee: B. L. Springstein et al., “Repurposing of a DNA segregation machinery
into a cytoskeletal system controlling cell shape,” Science, vol. 392,
no. 6795. AAAS, 2026.
ista: Springstein BL, Javoor M, Megrian D, Hajdu R, Hanke DM, Zens B, Weiss GL,
Schur FK, Loose M. 2026. Repurposing of a DNA segregation machinery into a cytoskeletal
system controlling cell shape. Science. 392(6795), eaea6343.
mla: Springstein, Benjamin L., et al. “Repurposing of a DNA Segregation Machinery
into a Cytoskeletal System Controlling Cell Shape.” Science, vol. 392,
no. 6795, eaea6343, AAAS, 2026, doi:10.1126/science.aea6343.
short: B.L. Springstein, M. Javoor, D. Megrian, R. Hajdu, D.M. Hanke, B. Zens, G.L.
Weiss, F.K. Schur, M. Loose, Science 392 (2026).
corr_author: '1'
date_created: 2026-04-26T22:01:46Z
date_published: 2026-04-16T00:00:00Z
date_updated: 2026-04-28T13:29:05Z
day: '16'
department:
- _id: MaLo
- _id: FlSc
- _id: GradSch
- _id: EM-Fac
doi: 10.1126/science.aea6343
ec_funded: 1
external_id:
pmid:
- '41990175'
intvolume: ' 392'
issue: '6795'
language:
- iso: eng
month: '04'
oa_version: None
pmid: 1
project:
- _id: fc2ed2f7-9c52-11eb-aca3-c01059dda49c
call_identifier: H2020
grant_number: '101034413'
name: 'IST-BRIDGE: International postdoctoral program'
- _id: bd980d18-d553-11ed-ba76-ceaa645c97eb
grant_number: '101076260'
name: A molecular atlas of Actin filament IDentities in the cell motility machinery
publication: Science
publication_identifier:
eissn:
- 1095-9203
issn:
- 0036-8075
publication_status: published
publisher: AAAS
quality_controlled: '1'
scopus_import: '1'
status: public
title: Repurposing of a DNA segregation machinery into a cytoskeletal system controlling
cell shape
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 392
year: '2026'
...
---
DOAJ_listed: '1'
OA_place: publisher
OA_type: gold
_id: '19795'
abstract:
- lang: eng
text: Super-resolution microscopy often entails long acquisition times of minutes
to hours. Since drifts during the acquisition adversely affect data quality, active
sample stabilization is commonly used for some of these techniques to reach their
full potential. Although drifts in the lateral plane can often be corrected after
acquisition, this is not always possible or may come with drawbacks. Therefore,
it is appealing to stabilize sample position in three dimensions (3D) during acquisition.
Various schemes for active sample stabilization have been demonstrated previously,
with some reaching sub-nanometer stability in 3D. Here, we present a scheme for
active drift correction that delivers the nanometer-scale 3D stability demanded
by state-of-the-art super-resolution techniques and is straightforward to implement
compared to previous schemes capable of reaching this level of stabilization precision.
Using a refined algorithm that can handle various types of reference structure,
without sparse signal peaks being mandatory, we stabilized sample position to
∼1 nm in 3D using objective lenses both with high and low numerical aperture.
Our implementation requires only the addition of a simple widefield imaging path
and we provide an open-source control software with graphical user interface to
facilitate easy adoption of the module. Finally, we demonstrate how this has the
potential to enhance data collection for diffraction-limited and super-resolution
imaging techniques using single-molecule localization microscopy and cryo-confocal
imaging as showcases.
acknowledged_ssus:
- _id: M-Shop
- _id: EM-Fac
- _id: LifeSc
acknowledgement: 'We acknowledge expert support by ISTA’s scientific service units,
including the Miba Machine Shop, the Electron Microscopy Facility, and the Lab Support
Facility. This work has been made possible in part by CZI grant DAF2021-234754 and
grant DOI: https://doi.org/10.37921/812628ebpcwg from the Chan Zuckerberg Initiative
DAF, an advised fund of Silicon Valley Community Foundation (funder DOI: https://doi.org/10.13039/100014989)
(F.K.M.S. and J.G.D.). We further gratefully acknowledge funding by the following
sources: Austrian Science Fund (FWF) grant DK W1232 (M.R.T. and J.G.D.); Austrian
Academy of Sciences DOC fellowship 26137 (M.R.T.); Marie Skłodowska-Curie Actions
Fellowship GA no. 665385 under the EU Horizon 2020 program (J.L.); ISTA postdoctoral
fellowship IST fellow (A.W.); and Human Frontier Science Program postdoctoral fellowship
LT000557/2018 (W.J.).'
article_number: '100211'
article_processing_charge: Yes
article_type: original
author:
- first_name: Jakob
full_name: Vorlaufer, Jakob
id: 937696FA-C996-11E9-8C7C-CF13E6697425
last_name: Vorlaufer
orcid: 0009-0000-7590-3501
- first_name: Nikolai
full_name: Semenov, Nikolai
id: e64d39c7-72ef-11ef-b75a-ee3046860d1b
last_name: Semenov
- first_name: Caroline
full_name: Kreuzinger, Caroline
id: 382077BA-F248-11E8-B48F-1D18A9856A87
last_name: Kreuzinger
- first_name: Manjunath
full_name: Javoor, Manjunath
id: 305ab18b-dc7d-11ea-9b2f-b58195228ea2
last_name: Javoor
orcid: 0000-0003-2311-2112
- first_name: Bettina
full_name: Zens, Bettina
id: 45FD126C-F248-11E8-B48F-1D18A9856A87
last_name: Zens
orcid: 0000-0002-9561-1239
- first_name: Nathalie
full_name: Agudelo Duenas, Nathalie
id: 40E7F008-F248-11E8-B48F-1D18A9856A87
last_name: Agudelo Duenas
- first_name: Mojtaba
full_name: Tavakoli, Mojtaba
id: 3A0A06F4-F248-11E8-B48F-1D18A9856A87
last_name: Tavakoli
orcid: 0000-0002-7667-6854
- first_name: Marek
full_name: Suplata, Marek
id: EE8452B8-C26A-11E9-B157-E80CE6697425
last_name: Suplata
- first_name: Wiebke
full_name: Jahr, Wiebke
id: 425C1CE8-F248-11E8-B48F-1D18A9856A87
last_name: Jahr
orcid: 0000-0003-0201-2315
- first_name: Julia
full_name: Lyudchik, Julia
id: 46E28B80-F248-11E8-B48F-1D18A9856A87
last_name: Lyudchik
- first_name: Andreas
full_name: Wartak, Andreas
id: 60aaa06c-3de5-11eb-9e53-baa88e955dcb
last_name: Wartak
- first_name: Florian Km
full_name: Schur, Florian Km
id: 48AD8942-F248-11E8-B48F-1D18A9856A87
last_name: Schur
orcid: 0000-0003-4790-8078
- first_name: Johann G
full_name: Danzl, Johann G
id: 42EFD3B6-F248-11E8-B48F-1D18A9856A87
last_name: Danzl
orcid: 0000-0001-8559-3973
citation:
ama: Vorlaufer J, Semenov N, Kreuzinger C, et al. Image-based 3D active sample stabilization
on the nanometer scale for optical microscopy. Biophysical Reports. 2025;5(2).
doi:10.1016/j.bpr.2025.100211
apa: Vorlaufer, J., Semenov, N., Kreuzinger, C., Javoor, M., Zens, B., Agudelo Duenas,
N., … Danzl, J. G. (2025). Image-based 3D active sample stabilization on the nanometer
scale for optical microscopy. Biophysical Reports. Elsevier. https://doi.org/10.1016/j.bpr.2025.100211
chicago: Vorlaufer, Jakob, Nikolai Semenov, Caroline Kreuzinger, Manjunath Javoor,
Bettina Zens, Nathalie Agudelo Duenas, Mojtaba Tavakoli, et al. “Image-Based 3D
Active Sample Stabilization on the Nanometer Scale for Optical Microscopy.” Biophysical
Reports. Elsevier, 2025. https://doi.org/10.1016/j.bpr.2025.100211.
ieee: J. Vorlaufer et al., “Image-based 3D active sample stabilization on
the nanometer scale for optical microscopy,” Biophysical Reports, vol.
5, no. 2. Elsevier, 2025.
ista: Vorlaufer J, Semenov N, Kreuzinger C, Javoor M, Zens B, Agudelo Duenas N,
Tavakoli M, Suplata M, Jahr W, Lyudchik J, Wartak A, Schur FK, Danzl JG. 2025.
Image-based 3D active sample stabilization on the nanometer scale for optical
microscopy. Biophysical Reports. 5(2), 100211.
mla: Vorlaufer, Jakob, et al. “Image-Based 3D Active Sample Stabilization on the
Nanometer Scale for Optical Microscopy.” Biophysical Reports, vol. 5, no.
2, 100211, Elsevier, 2025, doi:10.1016/j.bpr.2025.100211.
short: J. Vorlaufer, N. Semenov, C. Kreuzinger, M. Javoor, B. Zens, N. Agudelo Duenas,
M. Tavakoli, M. Suplata, W. Jahr, J. Lyudchik, A. Wartak, F.K. Schur, J.G. Danzl,
Biophysical Reports 5 (2025).
corr_author: '1'
date_created: 2025-06-08T22:01:22Z
date_published: 2025-06-11T00:00:00Z
date_updated: 2026-04-07T11:48:07Z
day: '11'
ddc:
- '570'
department:
- _id: JoDa
- _id: GradSch
- _id: FlSc
- _id: EM-Fac
doi: 10.1016/j.bpr.2025.100211
ec_funded: 1
file:
- access_level: open_access
checksum: 4018c833f25a3ad3b57e3577fed70334
content_type: application/pdf
creator: dernst
date_created: 2025-06-10T07:24:46Z
date_updated: 2025-06-10T07:24:46Z
file_id: '19802'
file_name: 2025_BiophysicalReports_Vorlaufer.pdf
file_size: 7238179
relation: main_file
success: 1
file_date_updated: 2025-06-10T07:24:46Z
has_accepted_license: '1'
intvolume: ' 5'
issue: '2'
language:
- iso: eng
license: https://creativecommons.org/licenses/by/4.0/
month: '06'
oa: 1
oa_version: Published Version
project:
- _id: 62909c6f-2b32-11ec-9570-e1476aab5308
grant_number: CZI01
name: CryoMinflux-guided in-situ molecular census and structure determination
- _id: 6285a163-2b32-11ec-9570-8e204ca2dba5
grant_number: '26137'
name: Studying Organelle Structure and Function at Nanoscale Resolution with Expansion
Microscopy
- _id: 2564DBCA-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '665385'
name: International IST Doctoral Program
- _id: 26AA4EF2-B435-11E9-9278-68D0E5697425
call_identifier: FWF
grant_number: W1232-B24
name: Molecular Drug Targets
- _id: 2668BFA0-B435-11E9-9278-68D0E5697425
grant_number: LT00057
name: High-speed 3D-nanoscopy to study the role of adhesion during 3D cell migration
publication: Biophysical Reports
publication_identifier:
eissn:
- 2667-0747
publication_status: published
publisher: Elsevier
quality_controlled: '1'
related_material:
record:
- id: '20206'
relation: dissertation_contains
status: public
scopus_import: '1'
status: public
title: Image-based 3D active sample stabilization on the nanometer scale for optical
microscopy
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 5
year: '2025'
...
---
APC_amount: 1395,61 EUR
DOAJ_listed: '1'
OA_place: publisher
OA_type: gold
PlanS_conform: '1'
_id: '20370'
abstract:
- lang: eng
text: The Huntingtin protein (HTT), named for its role in Huntington’s disease,
has been best understood as a scaffolding protein that promotes vesicle transport
by molecular motors along microtubules. Here, we show that HTT also interacts
with the actin cytoskeleton, and its loss of function disturbs the morphology
and function of the axonal growth cone. We demonstrate that HTT organizes F-actin
into bundles. Cryo–electron tomography (cryo-ET) and subtomogram averaging (STA)
structural analyses reveal that HTT’s N-terminal HEAT and Bridge domains wrap
around F-actin, while the C-terminal HEAT domain is displaced; furthermore, HTT
dimerizes via the N-HEAT domain to bridge parallel actin filaments separated by
~20 nanometers. Our study provides the structural basis for understanding how
HTT interacts with and organizes the actin cytoskeleton.
acknowledgement: 'We thank C. Cuveillier, J. Delaroche, T. Ferraro, and A. Zanchi
for help with TIRF experiments, electron microscopy preparation, data analysis,
and cell cultures, respectively; A. Antkowiak, C. Bosc, C. Fassier, A. Fourest-Lieuvin,
and V. Brandt for helpful discussions. We acknowledge the contribution of the Photonic
Imaging Center of Grenoble Institute Neuroscience which is part of the ISdV core
facility and certified by the IBiSA label and ICM.Quant (RRID:SCR_026393) core facility
of the Paris Brain Institute (ICM); the AniRA lentivector production facility from
the CELPHEDIA Infrastructure and SFR Biosciences (UAR3444/CNRS, US8/Inserm, ENS
de Lyon, UCBL); the Scientific Service Units (SSUs) of ISTA through resources provided
by Scientific Computing (SciComp, A. Schloegl and S. Elefante); and the Electron
Microscopy Facility (EMF, V.V. Hodirnau). The software programs used for the processing
were supported by SBGrid (www.sbgrid.org). This work was supported by the Agence
Nationale pour la Recherche (AXYON: ANR-18-CE16-0009-01, S.H.), Austrian Science
Fund (FWF) grants (P33367, F.K.M.S.; E435, J.M.H.), ChanZuckerberg Initiative (CZI)
grant (DAF2021-234754, F.K.M.S.), Hereditary Disease Foundation Research Grant (HDF
990846, M.C.), European Union (ERC: ActinID 101076260, F.K.M.S.), Fondation pour
la Recherche Médicale (FRM: équipe labellisée DEQ202203014675, S.H.; PhD fellowship,
FDT202001010865, R.C.), Korea Health Industry Development Institute (KHIDI) (Korea-Switzerland
global research support grant: RS-2023-00266300, J.-J.S.), National Research Foundation
(NRF) of Korea (Korea-Austria collaborative grant NRF-2019K1A3A1A181160, J.-J.S.
and F.K.M.S.; NRF-2020R1A2B5B03001517 and RS-2024-00333346 and RS-2024-00436173,
J.-J.S.; 2021R1C1C1006700, D.K.).'
article_number: eadw4124
article_processing_charge: Yes
article_type: original
author:
- first_name: Rémi
full_name: Carpentier, Rémi
last_name: Carpentier
- first_name: Jaesung
full_name: Kim, Jaesung
last_name: Kim
- first_name: Mariacristina
full_name: Capizzi, Mariacristina
last_name: Capizzi
- first_name: Hyeongju
full_name: Kim, Hyeongju
last_name: Kim
- first_name: Florian
full_name: Fäßler, Florian
id: 404F5528-F248-11E8-B48F-1D18A9856A87
last_name: Fäßler
orcid: 0000-0001-7149-769X
- first_name: Jesse
full_name: Hansen, Jesse
id: 1063c618-6f9b-11ec-9123-f912fccded63
last_name: Hansen
orcid: 0000-0001-7967-2085
- first_name: Min Jeong
full_name: Kim, Min Jeong
last_name: Kim
- first_name: Eric
full_name: Denarier, Eric
last_name: Denarier
- first_name: Béatrice
full_name: Blot, Béatrice
last_name: Blot
- first_name: Marine
full_name: Degennaro, Marine
last_name: Degennaro
- first_name: Sophia
full_name: Labou, Sophia
last_name: Labou
- first_name: Isabelle
full_name: Arnal, Isabelle
last_name: Arnal
- first_name: Maria J.
full_name: Marcaida, Maria J.
last_name: Marcaida
- first_name: Matteo Dal
full_name: Peraro, Matteo Dal
last_name: Peraro
- first_name: Doory
full_name: Kim, Doory
last_name: Kim
- first_name: Florian KM
full_name: Schur, Florian KM
id: 48AD8942-F248-11E8-B48F-1D18A9856A87
last_name: Schur
orcid: 0000-0003-4790-8078
- first_name: Ji-Joon
full_name: Song, Ji-Joon
last_name: Song
- first_name: Sandrine
full_name: Humbert, Sandrine
last_name: Humbert
citation:
ama: Carpentier R, Kim J, Capizzi M, et al. Structure of the Huntingtin F-actin
complex reveals its role in cytoskeleton organization. Science Advances.
2025;11(38). doi:10.1126/sciadv.adw4124
apa: Carpentier, R., Kim, J., Capizzi, M., Kim, H., Fäßler, F., Hansen, J., … Humbert,
S. (2025). Structure of the Huntingtin F-actin complex reveals its role in cytoskeleton
organization. Science Advances. AAAS. https://doi.org/10.1126/sciadv.adw4124
chicago: Carpentier, Rémi, Jaesung Kim, Mariacristina Capizzi, Hyeongju Kim, Florian
Fäßler, Jesse Hansen, Min Jeong Kim, et al. “Structure of the Huntingtin F-Actin
Complex Reveals Its Role in Cytoskeleton Organization.” Science Advances.
AAAS, 2025. https://doi.org/10.1126/sciadv.adw4124.
ieee: R. Carpentier et al., “Structure of the Huntingtin F-actin complex
reveals its role in cytoskeleton organization,” Science Advances, vol.
11, no. 38. AAAS, 2025.
ista: Carpentier R, Kim J, Capizzi M, Kim H, Fäßler F, Hansen J, Kim MJ, Denarier
E, Blot B, Degennaro M, Labou S, Arnal I, Marcaida MJ, Peraro MD, Kim D, Schur
FK, Song J-J, Humbert S. 2025. Structure of the Huntingtin F-actin complex reveals
its role in cytoskeleton organization. Science Advances. 11(38), eadw4124.
mla: Carpentier, Rémi, et al. “Structure of the Huntingtin F-Actin Complex Reveals
Its Role in Cytoskeleton Organization.” Science Advances, vol. 11, no.
38, eadw4124, AAAS, 2025, doi:10.1126/sciadv.adw4124.
short: R. Carpentier, J. Kim, M. Capizzi, H. Kim, F. Fäßler, J. Hansen, M.J. Kim,
E. Denarier, B. Blot, M. Degennaro, S. Labou, I. Arnal, M.J. Marcaida, M.D. Peraro,
D. Kim, F.K. Schur, J.-J. Song, S. Humbert, Science Advances 11 (2025).
corr_author: '1'
date_created: 2025-09-22T08:00:52Z
date_published: 2025-09-19T00:00:00Z
date_updated: 2026-05-20T08:20:27Z
day: '19'
ddc:
- '570'
department:
- _id: FlSc
doi: 10.1126/sciadv.adw4124
external_id:
isi:
- '001575751700013'
pmid:
- '40971423'
file:
- access_level: open_access
checksum: 4e2407bdabf8d53f399eb8a20d86218e
content_type: application/pdf
creator: dernst
date_created: 2025-09-23T07:57:51Z
date_updated: 2025-09-23T07:57:51Z
file_id: '20372'
file_name: 2025_ScienceAdvance_Carpentier.pdf
file_size: 3599137
relation: main_file
success: 1
file_date_updated: 2025-09-23T07:57:51Z
has_accepted_license: '1'
intvolume: ' 11'
isi: 1
issue: '38'
language:
- iso: eng
month: '09'
oa: 1
oa_version: Published Version
pmid: 1
project:
- _id: 9B954C5C-BA93-11EA-9121-9846C619BF3A
grant_number: P33367
name: Structure and isoform diversity of the Arp2/3 complex
- _id: 7bd318a1-9f16-11ee-852c-cc9217763180
grant_number: E435
name: In Situ Actin Structures via Hybrid Cryo-electron Microscopy
- _id: 62909c6f-2b32-11ec-9570-e1476aab5308
grant_number: CZI01
name: CryoMinflux-guided in-situ molecular census and structure determination
- _id: bd980d18-d553-11ed-ba76-ceaa645c97eb
grant_number: '101076260'
name: A molecular atlas of Actin filament IDentities in the cell motility machinery
- _id: 3AC91DDA-15DF-11EA-824D-93A3E7B544D1
call_identifier: FWF
name: FWF Open Access Fund
publication: Science Advances
publication_identifier:
issn:
- 2375-2548
publication_status: published
publisher: AAAS
quality_controlled: '1'
scopus_import: '1'
status: public
title: Structure of the Huntingtin F-actin complex reveals its role in cytoskeleton
organization
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 11
year: '2025'
...
---
APC_amount: 12348 EUR
OA_place: publisher
OA_type: hybrid
_id: '17884'
abstract:
- lang: eng
text: Human T cell leukemia virus type 1 (HTLV-1) immature particles differ in morphology
from other retroviruses, suggesting a distinct way of assembly. Here we report
the results of cryo-electron tomography studies of HTLV-1 virus-like particles
assembled in vitro, as well as derived from cells. This work shows that HTLV-1
uses a distinct mechanism of Gag–Gag interactions to form the immature viral lattice.
Analysis of high-resolution structural information from immature capsid (CA) tubular
arrays reveals that the primary stabilizing component in HTLV-1 is the N-terminal
domain of CA. Mutagenesis analysis supports this observation. This distinguishes
HTLV-1 from other retroviruses, in which the stabilization is provided primarily
by the C-terminal domain of CA. These results provide structural details of the
quaternary arrangement of Gag for an immature deltaretrovirus and this helps explain
why HTLV-1 particles are morphologically distinct.
acknowledged_ssus:
- _id: ScienComp
- _id: LifeSc
- _id: EM-Fac
acknowledgement: This work was funded by the Institute of Science and Technology Austria
(ISTA) and the Austrian Science Fund (grant P31445 to F.K.M.S.). Access to high-resolution
cryo-ET data acquisition at European Molecular Biology Laboratory (EMBL) Heidelberg
was supported through the EMBL cryo-EM platform. We thank V.-V. Hodirnau at ISTA
and W. Hagen and F. Weis at EMBL Heidelberg for support in cryo-ET data acquisition.
This research was also supported by the scientific service units of ISTA through
resources provided by Scientific Computing, the Life Science Facility, and the EM
Facility. L.M.M. was supported by National Institutes of Health grants R01 GM151775
and R21 DE032878 and by the University of Minnesota Masonic Cancer Center. D.P.
was supported by the DOC doctoral fellowship program of the Austrian Academy of
Sciences. R.A.D was supported by the National Institute of Allergy and Infectious
Diseases (grant R01AI147890). The funders had no role in study design, data collection
and analysis, decision to publish or preparation of the manuscript. Specifically,
we also want to thank A. Schlögl for computational support and J. Hansen and V.
Vogt for critical comments on the manuscript. We also thank the other members of
the Schur lab for helpful discussions and experimental advice.
article_processing_charge: Yes (in subscription journal)
article_type: original
author:
- first_name: Martin
full_name: Obr, Martin
id: 4741CA5A-F248-11E8-B48F-1D18A9856A87
last_name: Obr
orcid: 0000-0003-1756-6564
- first_name: Mathias
full_name: Percipalle, Mathias
id: 4986e21c-eb97-11eb-a6c2-a4ef0b629971
last_name: Percipalle
- first_name: Darya
full_name: Chernikova, Darya
id: 7dbaf460-fa9e-11eb-b0ca-bc7c7ff21ad0
last_name: Chernikova
- first_name: Huixin
full_name: Yang, Huixin
last_name: Yang
- first_name: Andreas
full_name: Thader, Andreas
id: 3A18A7B8-F248-11E8-B48F-1D18A9856A87
last_name: Thader
- first_name: Gergely
full_name: Pinke, Gergely
id: 4D5303E6-F248-11E8-B48F-1D18A9856A87
last_name: Pinke
- first_name: Dario J
full_name: Porley, Dario J
id: 2FD6EA6C-F248-11E8-B48F-1D18A9856A87
last_name: Porley
- first_name: Louis M.
full_name: Mansky, Louis M.
last_name: Mansky
- first_name: Robert A.
full_name: Dick, Robert A.
last_name: Dick
- first_name: Florian KM
full_name: Schur, Florian KM
id: 48AD8942-F248-11E8-B48F-1D18A9856A87
last_name: Schur
orcid: 0000-0003-4790-8078
citation:
ama: Obr M, Percipalle M, Chernikova D, et al. Distinct stabilization of the human
T cell leukemia virus type 1 immature Gag lattice. Nature Structural &
Molecular Biology. 2025;32:268-276. doi:10.1038/s41594-024-01390-8
apa: Obr, M., Percipalle, M., Chernikova, D., Yang, H., Thader, A., Pinke, G., …
Schur, F. K. (2025). Distinct stabilization of the human T cell leukemia virus
type 1 immature Gag lattice. Nature Structural & Molecular Biology.
Springer Nature. https://doi.org/10.1038/s41594-024-01390-8
chicago: Obr, Martin, Mathias Percipalle, Darya Chernikova, Huixin Yang, Andreas
Thader, Gergely Pinke, Darío Porley Esteves, Louis M. Mansky, Robert A. Dick,
and Florian KM Schur. “Distinct Stabilization of the Human T Cell Leukemia Virus
Type 1 Immature Gag Lattice.” Nature Structural & Molecular Biology.
Springer Nature, 2025. https://doi.org/10.1038/s41594-024-01390-8.
ieee: M. Obr et al., “Distinct stabilization of the human T cell leukemia
virus type 1 immature Gag lattice,” Nature Structural & Molecular Biology,
vol. 32. Springer Nature, pp. 268–276, 2025.
ista: Obr M, Percipalle M, Chernikova D, Yang H, Thader A, Pinke G, Porley Esteves
D, Mansky LM, Dick RA, Schur FK. 2025. Distinct stabilization of the human T cell
leukemia virus type 1 immature Gag lattice. Nature Structural & Molecular
Biology. 32, 268–276.
mla: Obr, Martin, et al. “Distinct Stabilization of the Human T Cell Leukemia Virus
Type 1 Immature Gag Lattice.” Nature Structural & Molecular Biology,
vol. 32, Springer Nature, 2025, pp. 268–76, doi:10.1038/s41594-024-01390-8.
short: M. Obr, M. Percipalle, D. Chernikova, H. Yang, A. Thader, G. Pinke, D. Porley
Esteves, L.M. Mansky, R.A. Dick, F.K. Schur, Nature Structural & Molecular
Biology 32 (2025) 268–276.
corr_author: '1'
date_created: 2024-09-08T10:29:06Z
date_published: 2025-02-01T00:00:00Z
date_updated: 2026-03-16T12:55:18Z
day: '01'
ddc:
- '570'
department:
- _id: FlSc
- _id: LeSa
doi: 10.1038/s41594-024-01390-8
external_id:
isi:
- '001306564000001'
oaworkid:
- W4402316284
pmid:
- '39242978'
file:
- access_level: open_access
checksum: c641ad94afb28917b20425db676fc3ee
content_type: application/pdf
creator: dernst
date_created: 2025-04-23T07:02:33Z
date_updated: 2025-04-23T07:02:33Z
file_id: '19608'
file_name: 2025_NatureStrucBio_Obr.pdf
file_size: 13724041
relation: main_file
success: 1
file_date_updated: 2025-04-23T07:02:33Z
has_accepted_license: '1'
intvolume: ' 32'
isi: 1
language:
- iso: eng
month: '02'
oa: 1
oa_version: Published Version
oaworkid: 1
page: 268-276
pmid: 1
project:
- _id: 26736D6A-B435-11E9-9278-68D0E5697425
call_identifier: FWF
grant_number: P31445
name: Structural conservation and diversity in retroviral capsid
- _id: 9B9C98E0-BA93-11EA-9121-9846C619BF3A
grant_number: '25762'
name: Structural characterization of spumavirus capsid assemblies to understand
conserved Ortervirales assembly mechanisms
publication: Nature Structural & Molecular Biology
publication_identifier:
eissn:
- 1545-9985
issn:
- 1545-9993
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
scopus_import: '1'
status: public
title: Distinct stabilization of the human T cell leukemia virus type 1 immature Gag
lattice
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 32
year: '2025'
...
---
APC_amount: 11700 EUR
OA_place: publisher
OA_type: hybrid
_id: '14979'
abstract:
- lang: eng
text: Poxviruses are among the largest double-stranded DNA viruses, with members
such as variola virus, monkeypox virus and the vaccination strain vaccinia virus
(VACV). Knowledge about the structural proteins that form the viral core has remained
sparse. While major core proteins have been annotated via indirect experimental
evidence, their structures have remained elusive and they could not be assigned
to individual core features. Hence, which proteins constitute which layers of
the core, such as the palisade layer and the inner core wall, has remained enigmatic.
Here we show, using a multi-modal cryo-electron microscopy (cryo-EM) approach
in combination with AlphaFold molecular modeling, that trimers formed by the cleavage
product of VACV protein A10 are the key component of the palisade layer. This
allows us to place previously obtained descriptions of protein interactions within
the core wall into perspective and to provide a detailed model of poxvirus core
architecture. Importantly, we show that interactions within A10 trimers are likely
generalizable over members of orthopox- and parapoxviruses.
acknowledged_ssus:
- _id: ScienComp
- _id: LifeSc
- _id: EM-Fac
acknowledgement: "We thank A. Bergthaler (Research Center for Molecular Medicine of
the Austrian Academy of Sciences) for providing VACV WR. We thank A. Nicholas and
his team at the ISTA proteomics facility, and S. Elefante at the ISTA Scientific
Computing facility for their support. We also thank F. Fäßler, D. Porley, T. Muthspiel
and other members of the Schur group for support and helpful discussions. We also
thank D. Castaño-Díez for support with Dynamo. We thank D. Farrell for his help
optimizing the Rosetta protocol to refine the atomic model into the cryo-EM map
with symmetry.\r\n\r\nF.K.M.S. acknowledges support from ISTA and EMBO. F.K.M.S.
also received support from the Austrian Science Fund (FWF) grant P31445. This publication
has been made possible in part by CZI grant DAF2021-234754 and grant https://doi.org/10.37921/812628ebpcwg
from the Chan Zuckerberg Initiative DAF, an advised fund of Silicon Valley Community
Foundation (funder https://doi.org/10.13039/100014989) awarded to F.K.M.S.\r\n\r\nThis
research was also supported by the Scientific Service Units (SSUs) of ISTA through
resources provided by Scientific Computing (SciComp), the Life Science Facility
(LSF), and the Electron Microscopy Facility (EMF). We also acknowledge the use of
COSMIC45 and Colabfold46."
article_processing_charge: Yes (in subscription journal)
article_type: original
author:
- first_name: Julia
full_name: Datler, Julia
id: 3B12E2E6-F248-11E8-B48F-1D18A9856A87
last_name: Datler
orcid: 0000-0002-3616-8580
- first_name: Jesse
full_name: Hansen, Jesse
id: 1063c618-6f9b-11ec-9123-f912fccded63
last_name: Hansen
orcid: 0000-0001-7967-2085
- first_name: Andreas
full_name: Thader, Andreas
id: 3A18A7B8-F248-11E8-B48F-1D18A9856A87
last_name: Thader
- first_name: Alois
full_name: Schlögl, Alois
id: 45BF87EE-F248-11E8-B48F-1D18A9856A87
last_name: Schlögl
orcid: 0000-0002-5621-8100
- first_name: Lukas W
full_name: Bauer, Lukas W
id: 0c894dcf-897b-11ed-a09c-8186353224b0
last_name: Bauer
- first_name: Victor-Valentin
full_name: Hodirnau, Victor-Valentin
id: 3661B498-F248-11E8-B48F-1D18A9856A87
last_name: Hodirnau
orcid: 0000-0003-3904-947X
- first_name: Florian KM
full_name: Schur, Florian KM
id: 48AD8942-F248-11E8-B48F-1D18A9856A87
last_name: Schur
orcid: 0000-0003-4790-8078
citation:
ama: Datler J, Hansen J, Thader A, et al. Multi-modal cryo-EM reveals trimers of
protein A10 to form the palisade layer in poxvirus cores. Nature Structural
& Molecular Biology. 2024;31:1114-1123. doi:10.1038/s41594-023-01201-6
apa: Datler, J., Hansen, J., Thader, A., Schlögl, A., Bauer, L. W., Hodirnau, V.-V.,
& Schur, F. K. (2024). Multi-modal cryo-EM reveals trimers of protein A10
to form the palisade layer in poxvirus cores. Nature Structural & Molecular
Biology. Springer Nature. https://doi.org/10.1038/s41594-023-01201-6
chicago: Datler, Julia, Jesse Hansen, Andreas Thader, Alois Schlögl, Lukas W Bauer,
Victor-Valentin Hodirnau, and Florian KM Schur. “Multi-Modal Cryo-EM Reveals Trimers
of Protein A10 to Form the Palisade Layer in Poxvirus Cores.” Nature Structural
& Molecular Biology. Springer Nature, 2024. https://doi.org/10.1038/s41594-023-01201-6.
ieee: J. Datler et al., “Multi-modal cryo-EM reveals trimers of protein A10
to form the palisade layer in poxvirus cores,” Nature Structural & Molecular
Biology, vol. 31. Springer Nature, pp. 1114–1123, 2024.
ista: Datler J, Hansen J, Thader A, Schlögl A, Bauer LW, Hodirnau V-V, Schur FK.
2024. Multi-modal cryo-EM reveals trimers of protein A10 to form the palisade
layer in poxvirus cores. Nature Structural & Molecular Biology. 31, 1114–1123.
mla: Datler, Julia, et al. “Multi-Modal Cryo-EM Reveals Trimers of Protein A10 to
Form the Palisade Layer in Poxvirus Cores.” Nature Structural & Molecular
Biology, vol. 31, Springer Nature, 2024, pp. 1114–23, doi:10.1038/s41594-023-01201-6.
short: J. Datler, J. Hansen, A. Thader, A. Schlögl, L.W. Bauer, V.-V. Hodirnau,
F.K. Schur, Nature Structural & Molecular Biology 31 (2024) 1114–1123.
corr_author: '1'
date_created: 2024-02-12T09:59:45Z
date_published: 2024-07-01T00:00:00Z
date_updated: 2026-04-07T12:59:44Z
day: '01'
ddc:
- '570'
department:
- _id: FlSc
- _id: ScienComp
- _id: EM-Fac
doi: 10.1038/s41594-023-01201-6
external_id:
isi:
- '001158144600002'
pmid:
- '38316877'
file:
- access_level: open_access
checksum: bda7bf65d81455480efaed8ca293b0db
content_type: application/pdf
creator: dernst
date_created: 2024-07-22T11:27:22Z
date_updated: 2024-07-22T11:27:22Z
file_id: '17307'
file_name: 2024_NatureStrucBio_Datler.pdf
file_size: 17485494
relation: main_file
success: 1
file_date_updated: 2024-07-22T11:27:22Z
has_accepted_license: '1'
intvolume: ' 31'
isi: 1
keyword:
- Molecular Biology
- Structural Biology
language:
- iso: eng
month: '07'
oa: 1
oa_version: Published Version
page: 1114-1123
pmid: 1
project:
- _id: 26736D6A-B435-11E9-9278-68D0E5697425
call_identifier: FWF
grant_number: P31445
name: Structural conservation and diversity in retroviral capsid
publication: Nature Structural & Molecular Biology
publication_identifier:
eissn:
- 1545-9985
issn:
- 1545-9993
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
related_material:
link:
- description: News on ISTA Website
relation: press_release
url: https://ista.ac.at/en/news/down-to-the-core-of-poxviruses/
record:
- id: '18766'
relation: dissertation_contains
status: public
scopus_import: '1'
status: public
title: Multi-modal cryo-EM reveals trimers of protein A10 to form the palisade layer
in poxvirus cores
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345
volume: 31
year: '2024'
...
---
_id: '15146'
abstract:
- lang: eng
text: The extracellular matrix (ECM) serves as a scaffold for cells and plays an
essential role in regulating numerous cellular processes, including cell migration
and proliferation. Due to limitations in specimen preparation for conventional
room-temperature electron microscopy, we lack structural knowledge on how ECM
components are secreted, remodeled, and interact with surrounding cells. We have
developed a 3D-ECM platform compatible with sample thinning by cryo-focused ion
beam milling, the lift-out extraction procedure, and cryo-electron tomography.
Our workflow implements cell-derived matrices (CDMs) grown on EM grids, resulting
in a versatile tool closely mimicking ECM environments. This allows us to visualize
ECM for the first time in its hydrated, native context. Our data reveal an intricate
network of extracellular fibers, their positioning relative to matrix-secreting
cells, and previously unresolved structural entities. Our workflow and results
add to the structural atlas of the ECM, providing novel insights into its secretion
and assembly.
acknowledged_ssus:
- _id: LifeSc
- _id: ScienComp
- _id: EM-Fac
- _id: M-Shop
acknowledgement: "Open Access funding provided by IST Austria. We thank Armel Nicolas
and his team at the ISTA proteomics facility, Alois Schloegl, Stefano Elefante,
and colleagues at the ISTA Scientific Computing facility, Tommaso Constanzo and
Ludek Lovicar at the Electron Microsocpy Facility (EMF), and Thomas Menner at the
Miba Machine shop for their support. We also thank Wanda Kukulski (University of
Bern) as well as Darío Porley, Andreas Thader, and other members of the Schur group
for helpful discussions. Matt Swulius and Jessica Heebner provided great support
in using Dragonfly. We thank Dorotea Fracciolla (Art & Science) for support in figure
illustration.\r\n\r\nThis research was supported by the Scientific Service Units
of ISTA through resources provided by Scientific Computing, the Lab Support Facility,
and the Electron Microscopy Facility. We acknowledge funding support from the following
sources: Austrian Science Fund (FWF) grant P33367 (to F.K.M. Schur), the Federation
of European Biochemical Societies (to F.K.M. Schur), Niederösterreich (NÖ) Fonds
(to B. Zens), FWF grant E435 (to J.M. Hansen), European Research Council under the
European Union’s Horizon 2020 research (grant agreement No. 724373) (to M. Sixt),
and Jenny and Antti Wihuri Foundation (to J. Alanko). This publication has been
made possible in part by CZI grant DAF2021-234754 and grant DOI https://doi.org/10.37921/812628ebpcwg
from the Chan Zuckerberg Initiative DAF, an advised fund of Silicon Valley Community
Foundation (to F.K.M. Schur)."
article_number: e202309125
article_processing_charge: Yes (via OA deal)
article_type: original
author:
- first_name: Bettina
full_name: Zens, Bettina
id: 45FD126C-F248-11E8-B48F-1D18A9856A87
last_name: Zens
orcid: 0000-0002-9561-1239
- first_name: Florian
full_name: Fäßler, Florian
id: 404F5528-F248-11E8-B48F-1D18A9856A87
last_name: Fäßler
orcid: 0000-0001-7149-769X
- first_name: Jesse
full_name: Hansen, Jesse
id: 1063c618-6f9b-11ec-9123-f912fccded63
last_name: Hansen
orcid: 0000-0001-7967-2085
- first_name: Robert
full_name: Hauschild, Robert
id: 4E01D6B4-F248-11E8-B48F-1D18A9856A87
last_name: Hauschild
orcid: 0000-0001-9843-3522
- first_name: Julia
full_name: Datler, Julia
id: 3B12E2E6-F248-11E8-B48F-1D18A9856A87
last_name: Datler
orcid: 0000-0002-3616-8580
- first_name: Victor-Valentin
full_name: Hodirnau, Victor-Valentin
id: 3661B498-F248-11E8-B48F-1D18A9856A87
last_name: Hodirnau
orcid: 0000-0003-3904-947X
- first_name: Vanessa
full_name: Zheden, Vanessa
id: 39C5A68A-F248-11E8-B48F-1D18A9856A87
last_name: Zheden
orcid: 0000-0002-9438-4783
- first_name: Jonna H
full_name: Alanko, Jonna H
id: 2CC12E8C-F248-11E8-B48F-1D18A9856A87
last_name: Alanko
orcid: 0000-0002-7698-3061
- first_name: Michael K
full_name: Sixt, Michael K
id: 41E9FBEA-F248-11E8-B48F-1D18A9856A87
last_name: Sixt
orcid: 0000-0002-6620-9179
- first_name: Florian KM
full_name: Schur, Florian KM
id: 48AD8942-F248-11E8-B48F-1D18A9856A87
last_name: Schur
orcid: 0000-0003-4790-8078
citation:
ama: Zens B, Fäßler F, Hansen J, et al. Lift-out cryo-FIBSEM and cryo-ET reveal
the ultrastructural landscape of extracellular matrix. Journal of Cell Biology.
2024;223(6). doi:10.1083/jcb.202309125
apa: Zens, B., Fäßler, F., Hansen, J., Hauschild, R., Datler, J., Hodirnau, V.-V.,
… Schur, F. K. (2024). Lift-out cryo-FIBSEM and cryo-ET reveal the ultrastructural
landscape of extracellular matrix. Journal of Cell Biology. Rockefeller
University Press. https://doi.org/10.1083/jcb.202309125
chicago: Zens, Bettina, Florian Fäßler, Jesse Hansen, Robert Hauschild, Julia Datler,
Victor-Valentin Hodirnau, Vanessa Zheden, Jonna H Alanko, Michael K Sixt, and
Florian KM Schur. “Lift-out Cryo-FIBSEM and Cryo-ET Reveal the Ultrastructural
Landscape of Extracellular Matrix.” Journal of Cell Biology. Rockefeller
University Press, 2024. https://doi.org/10.1083/jcb.202309125.
ieee: B. Zens et al., “Lift-out cryo-FIBSEM and cryo-ET reveal the ultrastructural
landscape of extracellular matrix,” Journal of Cell Biology, vol. 223,
no. 6. Rockefeller University Press, 2024.
ista: Zens B, Fäßler F, Hansen J, Hauschild R, Datler J, Hodirnau V-V, Zheden V,
Alanko JH, Sixt MK, Schur FK. 2024. Lift-out cryo-FIBSEM and cryo-ET reveal the
ultrastructural landscape of extracellular matrix. Journal of Cell Biology. 223(6),
e202309125.
mla: Zens, Bettina, et al. “Lift-out Cryo-FIBSEM and Cryo-ET Reveal the Ultrastructural
Landscape of Extracellular Matrix.” Journal of Cell Biology, vol. 223,
no. 6, e202309125, Rockefeller University Press, 2024, doi:10.1083/jcb.202309125.
short: B. Zens, F. Fäßler, J. Hansen, R. Hauschild, J. Datler, V.-V. Hodirnau, V.
Zheden, J.H. Alanko, M.K. Sixt, F.K. Schur, Journal of Cell Biology 223 (2024).
corr_author: '1'
date_created: 2024-03-21T06:45:51Z
date_published: 2024-03-20T00:00:00Z
date_updated: 2025-09-04T13:17:16Z
day: '20'
ddc:
- '570'
department:
- _id: FlSc
- _id: MiSi
- _id: Bio
- _id: EM-Fac
doi: 10.1083/jcb.202309125
ec_funded: 1
external_id:
isi:
- '001264190100001'
pmid:
- '38506714'
file:
- access_level: open_access
checksum: 90d1984a93660735e506c2a304bc3f73
content_type: application/pdf
creator: dernst
date_created: 2024-03-25T12:52:04Z
date_updated: 2024-03-25T12:52:04Z
file_id: '15188'
file_name: 2024_JCB_Zens.pdf
file_size: 11907016
relation: main_file
success: 1
file_date_updated: 2024-03-25T12:52:04Z
has_accepted_license: '1'
intvolume: ' 223'
isi: 1
issue: '6'
language:
- iso: eng
month: '03'
oa: 1
oa_version: Published Version
pmid: 1
project:
- _id: 9B954C5C-BA93-11EA-9121-9846C619BF3A
grant_number: P33367
name: Structure and isoform diversity of the Arp2/3 complex
- _id: 7bd318a1-9f16-11ee-852c-cc9217763180
grant_number: E435
name: In Situ Actin Structures via Hybrid Cryo-electron Microscopy
- _id: 25FE9508-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '724373'
name: Cellular Navigation Along Spatial Gradients
- _id: 059B463C-7A3F-11EA-A408-12923DDC885E
name: "NÃ\x96-Fonds Preis für die Jungforscherin des Jahres am IST Austria"
- _id: 2615199A-B435-11E9-9278-68D0E5697425
grant_number: '21317'
name: Spatiotemporal regulation of chemokine-induced signalling in leukocyte chemotaxis
- _id: 62909c6f-2b32-11ec-9570-e1476aab5308
grant_number: CZI01
name: CryoMinflux-guided in-situ visual proteomics and structure determination
publication: Journal of Cell Biology
publication_identifier:
eissn:
- 1540-8140
issn:
- 0021-9525
publication_status: published
publisher: Rockefeller University Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: Lift-out cryo-FIBSEM and cryo-ET reveal the ultrastructural landscape of extracellular
matrix
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 317138e5-6ab7-11ef-aa6d-ffef3953e345
volume: 223
year: '2024'
...
---
OA_place: publisher
_id: '18766'
abstract:
- lang: eng
text: Poxviruses are large pleomorphic double-stranded DNA viruses that include
well known members such as variola virus, the causative agent of smallpox, Mpox
virus, as well as Vaccinia virus (VACV), which serves as a vaccination strain
for formerly mentioned viruses. VACV is a valuable model for studying large pleomorphic
DNA viruses in general and poxviruses specifically, as many features, such as
core morphology and structural proteins, are well conserved within this family.
Despite decades of research, our understanding of the structural components and
proteins that comprise the poxvirus core in mature virions remains limited. Although
major core proteins were identified via indirect experimental evidence, the core's
complexity, with its large size, structure and number of involved proteins, has
hindered efforts to achieve high-resolution insights and to define the roles of
the individual proteins. The specific protein composition of the core's individual
layers, including the palisade layer and the inner core wall, has remained unclear.
In this study, we have merged multiple approaches, including single particle cryo
electron microscopy of purified virus cores, cryo-electron tomography and subtomogram
averaging of mature virions and molecular modeling to elucidate the structural
determinants of the VACV core. Due to the lack of experimentally derived structures,
either in situ or reconstituted in vitro, we used Alphafold to predict models
of the putative major core protein candidates, A10, 23k, A3, A4, and L4. Our results
show that the VACV core is composed of several layers with varying local symmetries,
forming more intricate interactions than observed previously. This allowed us
to identify several molecular building blocks forming the viral core lattice.
In particular, we identified trimers of protein A10 as a major core structure
that forms the palisade layer of the viral core. Additionally, we revealed that
six petals of a flower shaped core pore within the core wall are composed of A10
trimers. Furthermore, we obtained a cryo-EM density for the inner core wall that
could potentially accommodate an A3 dimer. Integrating descriptions of protein
interactions from previous studies enabled us to provide a detailed structural
model of the poxvirus core wall, and our findings indicate that the interactions
within A10 trimers are likely consistent across orthopox- and parapoxviruses.
This combined application of cryo-SPA and cryo-ET can help overcome obstacles
in studying complex virus structures in the future, including their key assembly
proteins, interactions, and the formation into a core lattice. Our work provides
important fundamental new insights into poxvirus core architecture, also considering
the recent re-emergence of poxviruses.
acknowledged_ssus:
- _id: EM-Fac
- _id: LifeSc
- _id: ScienComp
acknowledgement: "This work was funded by the Austrian Science Fund (FWF) grant P31445
and ISTA. I\r\nwould like to express my gratitude to the Scientific Service Units,
particularly the Lab\r\nSupport Facility, the Scientific Computing Facility and
the Electron Microscopy Facility\r\nfor their tremendous support. I want to especially
thank Alois for assisting me with the\r\ninstallation of countless new software
and for troubleshooting cluster issues. A special\r\nthanks goes to Valentin for
his outstanding support in cryo-EM data acquisition and\r\nhis ongoing help in improving
the process to ensure that I obtained the best possible\r\ndata from my sample."
alternative_title:
- ISTA thesis
article_processing_charge: No
author:
- first_name: Julia
full_name: Datler, Julia
id: 3B12E2E6-F248-11E8-B48F-1D18A9856A87
last_name: Datler
orcid: 0000-0002-3616-8580
citation:
ama: Datler J. Elucidating the structural determinants of the poxvirus core using
multi-modal cryo-EM. 2024. doi:10.15479/at:ista:18766
apa: Datler, J. (2024). Elucidating the structural determinants of the poxvirus
core using multi-modal cryo-EM. Institute of Science and Technology Austria.
https://doi.org/10.15479/at:ista:18766
chicago: Datler, Julia. “Elucidating the Structural Determinants of the Poxvirus
Core Using Multi-Modal Cryo-EM.” Institute of Science and Technology Austria,
2024. https://doi.org/10.15479/at:ista:18766.
ieee: J. Datler, “Elucidating the structural determinants of the poxvirus core using
multi-modal cryo-EM,” Institute of Science and Technology Austria, 2024.
ista: Datler J. 2024. Elucidating the structural determinants of the poxvirus core
using multi-modal cryo-EM. Institute of Science and Technology Austria.
mla: Datler, Julia. Elucidating the Structural Determinants of the Poxvirus Core
Using Multi-Modal Cryo-EM. Institute of Science and Technology Austria, 2024,
doi:10.15479/at:ista:18766.
short: J. Datler, Elucidating the Structural Determinants of the Poxvirus Core Using
Multi-Modal Cryo-EM, Institute of Science and Technology Austria, 2024.
corr_author: '1'
date_created: 2025-01-07T10:23:12Z
date_published: 2024-12-30T00:00:00Z
date_updated: 2026-04-07T12:59:44Z
day: '30'
ddc:
- '570'
degree_awarded: PhD
department:
- _id: GradSch
- _id: FlSc
doi: 10.15479/at:ista:18766
file:
- access_level: closed
checksum: 3e51cab327c754045c3d29c1a50cc9a9
content_type: application/vnd.openxmlformats-officedocument.wordprocessingml.document
creator: jstanger
date_created: 2025-01-07T12:15:11Z
date_updated: 2025-01-07T12:15:11Z
file_id: '18769'
file_name: PhD_thesis_Julia_Datler.docx
file_size: 38814932
relation: source_file
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checksum: 22fabe5b97950bf852212f6edb555173
content_type: application/pdf
creator: jstanger
date_created: 2025-01-07T12:15:14Z
date_updated: 2025-01-07T12:15:14Z
file_id: '18770'
file_name: PhD_thesis_Julia_Datler.pdf
file_size: 12044865
relation: main_file
success: 1
file_date_updated: 2025-01-07T12:15:14Z
has_accepted_license: '1'
keyword:
- cryo-EM
- cryo-ET
- cryo-SPA
- Structural Virology
- Poxvirus
- Vaccinia Virus
- Structural Biology
language:
- iso: eng
license: https://creativecommons.org/licenses/by-nc-nd/4.0/
month: '12'
oa: 1
oa_version: Published Version
page: '106'
project:
- _id: 26736D6A-B435-11E9-9278-68D0E5697425
call_identifier: FWF
grant_number: P31445
name: Structural conservation and diversity in retroviral capsid
publication_identifier:
isbn:
- 978-3-99078-049-7
issn:
- 2663-337X
publication_status: published
publisher: Institute of Science and Technology Austria
related_material:
record:
- id: '12334'
relation: part_of_dissertation
status: public
- id: '14979'
relation: part_of_dissertation
status: public
status: public
supervisor:
- first_name: Florian KM
full_name: Schur, Florian KM
id: 48AD8942-F248-11E8-B48F-1D18A9856A87
last_name: Schur
orcid: 0000-0003-4790-8078
title: Elucidating the structural determinants of the poxvirus core using multi-modal
cryo-EM
tmp:
image: /images/cc_by_nc_nd.png
legal_code_url: https://creativecommons.org/licenses/by-nc-nd/4.0/legalcode
name: Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International
(CC BY-NC-ND 4.0)
short: CC BY-NC-ND (4.0)
type: dissertation
user_id: ba8df636-2132-11f1-aed0-ed93e2281fdd
year: '2024'
...
---
OA_place: publisher
OA_type: hybrid
_id: '18934'
abstract:
- lang: eng
text: The assembly of biomolecular condensate in eukaryotic cells and the accumulation
of amyloid deposits in neurons are processes involving the nucleation and growth
(NAG) of new protein phases. To therapeutically target protein phase separation,
drug candidates are tested in in vitro assays that monitor the increase in the
mass or size of the new phase. Limited mechanistic insight is, however, provided
if empirical or untestable kinetic models are fitted to these progress curves.
Here we present the web server NAGPKin that quantifies NAG rates using mass-based
or size-based progress curves as the input data. A report is generated containing
the fitted NAG parameters and elucidating the phase separation mechanisms at play.
The NAG parameters can be used to predict particle size distributions of, for
example, protein droplets formed by liquid-liquid phase separation (LLPS) or amyloid
fibrils formed by protein aggregation. Because minimal intervention is required
from the user, NAGPKin is a good platform for standardized reporting of LLPS and
protein self-assembly data. NAGPKin is useful for drug discovery as well as for
fundamental studies on protein phase separation. NAGPKin is freely available (no
login required) at https://nagpkin.i3s.up.pt .
acknowledgement: We thank Professor José Paulo Leal, Department of Computer Science
− Faculdade de Ciências da Universidade do Porto, for his invaluable help during
the Implementation of NAGPKin. This work is part of a project that has received
funding from the European Union’s Horizon 2020 research and innovation programme
under grant agreement no. 952334 (PhasAGE). This research was funded by the Portuguese
Foundation for Science and Technology (FCT) in the framework of project PTDC/QUI-COL/2444/2021.
article_number: mr1
article_processing_charge: Yes (in subscription journal)
article_type: original
author:
- first_name: Zsuzsa
full_name: Sárkány, Zsuzsa
last_name: Sárkány
- first_name: Francisco
full_name: Figueiredo, Francisco
id: 8125cbe2-9661-11ed-a754-afe96018f37d
last_name: Figueiredo
- first_name: Sandra
full_name: Macedo-Ribeiro, Sandra
last_name: Macedo-Ribeiro
- first_name: Pedro M.
full_name: Martins, Pedro M.
last_name: Martins
citation:
ama: 'Sárkány Z, Figueiredo F, Macedo-Ribeiro S, Martins PM. NAGPKin: Nucleation-and-growth
parameters from the kinetics of protein phase separation. Molecular Biology
of the Cell. 2024;35(3). doi:10.1091/mbc.e23-07-0289'
apa: 'Sárkány, Z., Figueiredo, F., Macedo-Ribeiro, S., & Martins, P. M. (2024).
NAGPKin: Nucleation-and-growth parameters from the kinetics of protein phase separation.
Molecular Biology of the Cell. American Society for Cell Biology. https://doi.org/10.1091/mbc.e23-07-0289'
chicago: 'Sárkány, Zsuzsa, Francisco Figueiredo, Sandra Macedo-Ribeiro, and Pedro
M. Martins. “NAGPKin: Nucleation-and-Growth Parameters from the Kinetics of Protein
Phase Separation.” Molecular Biology of the Cell. American Society for
Cell Biology, 2024. https://doi.org/10.1091/mbc.e23-07-0289.'
ieee: 'Z. Sárkány, F. Figueiredo, S. Macedo-Ribeiro, and P. M. Martins, “NAGPKin:
Nucleation-and-growth parameters from the kinetics of protein phase separation,”
Molecular Biology of the Cell, vol. 35, no. 3. American Society for Cell
Biology, 2024.'
ista: 'Sárkány Z, Figueiredo F, Macedo-Ribeiro S, Martins PM. 2024. NAGPKin: Nucleation-and-growth
parameters from the kinetics of protein phase separation. Molecular Biology of
the Cell. 35(3), mr1.'
mla: 'Sárkány, Zsuzsa, et al. “NAGPKin: Nucleation-and-Growth Parameters from the
Kinetics of Protein Phase Separation.” Molecular Biology of the Cell, vol.
35, no. 3, mr1, American Society for Cell Biology, 2024, doi:10.1091/mbc.e23-07-0289.'
short: Z. Sárkány, F. Figueiredo, S. Macedo-Ribeiro, P.M. Martins, Molecular Biology
of the Cell 35 (2024).
date_created: 2025-01-29T07:58:40Z
date_published: 2024-03-01T00:00:00Z
date_updated: 2025-01-29T08:16:20Z
day: '01'
ddc:
- '570'
department:
- _id: FlSc
doi: 10.1091/mbc.e23-07-0289
external_id:
pmid:
- '38117593'
file:
- access_level: open_access
checksum: d7deb6390f294da69321cfbe352ed611
content_type: application/pdf
creator: dernst
date_created: 2025-01-29T08:12:11Z
date_updated: 2025-01-29T08:12:11Z
file_id: '18935'
file_name: 2024_MolecularBioCell_Sarkany.pdf
file_size: 1699180
relation: main_file
success: 1
file_date_updated: 2025-01-29T08:12:11Z
has_accepted_license: '1'
intvolume: ' 35'
issue: '3'
language:
- iso: eng
license: https://creativecommons.org/licenses/by-nc-sa/4.0/
month: '03'
oa: 1
oa_version: Published Version
pmid: 1
publication: Molecular Biology of the Cell
publication_identifier:
eissn:
- 1939-4586
issn:
- 1059-1524
publication_status: published
publisher: American Society for Cell Biology
quality_controlled: '1'
scopus_import: '1'
status: public
title: 'NAGPKin: Nucleation-and-growth parameters from the kinetics of protein phase
separation'
tmp:
image: /images/cc_by_nc_sa.png
legal_code_url: https://creativecommons.org/licenses/by-nc-sa/4.0/legalcode
name: Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC
BY-NC-SA 4.0)
short: CC BY-NC-SA (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 35
year: '2024'
...
---
OA_place: publisher
_id: '18101'
abstract:
- lang: eng
text: "The Retroviridae family consists of two sub-families, the Orthoretrovirinae
and the\r\nSpumaretrovirinae. The Orthoretroviruses contain important human pathogens,
such as the\r\nhuman immunodeficiency virus 1 (HIV-1). They also harbor other
retrovirus species which\r\nare regularly used as model systems to study the retroviral
life cycle. The main structural\r\ncomponent of the retroviruses, is the Gag protein
and its truncation derivatives occurring\r\nduring viral maturation. Orthoretroviral
Gag assemblies have been extensively studied to\r\nunderstand the interactions
that confer stability and morphology to viral particles.\r\nThe Spumaretrovirinae
subfamily represent an early diverging branch of the Retroviridae.\r\nIts members,
the Foamy viruses (FV), share most of the conventional features found in\r\nretroviruses.
However, they also possess multiple characteristics that make them unique. In\r\nparticular,
FV Gag does not get extensively cleaved as in orthoretroviruses. Hence, the Gag\r\narchitecture
deviates from the canonical domain arrangement in FV. They also exhibit a\r\npeculiar
particle morphology, having no apparent immature state and a seemingly\r\nicosahedral
mature particle. Due to this, many fundamental questions on FV structural\r\nassembly
mechanisms remain open. To answer these questions, was the main focus of this\r\nthesis.\r\nMainly,
it is not known how FV assemble their core in a virus particle and what are the\r\nimportant
assembly interaction sites within said core. What is the minimum assembly\r\ncompetent
domain of FV Gag? Is there a morphological change in the assembly type of FVGag
lattices? If so, what is defining these morphological shifts? Finally, it would
be\r\ninteresting to know what is the evolutionary relationship between FV and
the rest of the\r\nretrotranscribing elements, from a structural point of view?\r\nTo
answer these questions, membrane-enveloped mammalian cell-derived FV virus-like\r\nparticles
(VLPs) were produced. Cryo-electron tomography (cryo-ET) analysis suggested\r\nthese
FV VLPs do not form a canonical retroviral Gag lattice structure, which is in
line with\r\nearlier observations. To further evaluate FV Gag assembly competence
and morphology,\r\nthe first bacterial cell-derived in vitro VLP assembly system
was designed and optimized.\r\nUsing this system with different truncation variants,
the minimum assembly competent\r\ndomain of FV Gag was found to be the putative
CA300-477 domain. Varying VLP\r\nmorphologies were also observed and strongly
suggested residues upstream of CA300-477\r\nplay a role in morphology determination.
Finally, a combined cryo-electron microscopy (cryoEM) and cryo-ET approach was
taken to analyze tubular assemblies from the minimal\r\nassembly competent domain.
This revealed an unexpectedly unique non-canonical\r\nassembly architecture. Three
novel lattice stabilizing interfaces were described which\r\nproved to be as unique
as the lattice arrangement. Comparison to a newly published FV CA\r\ncore structure
revealed the CA-CA interactions in the atypical assembly do not recapitulate\r\nwhat
is described for the FV core lattice. However, the new in vitro VLP assembly system\r\nobtained
in this thesis also provides an exciting opportunity to study still unresolved
FV\r\nassembly features in a potentially facilitated approach compared to conventional
methods.\r\nIn summary, this work provided a deeper understanding of the basic
FV Gag assembly unit,\r\nas well as presenting the first FV Gag-derived in vitro
VLP assembly system. This system\r\nreveals a novel and unique assembly architecture
among retroviral in vitro assemblies."
acknowledged_ssus:
- _id: EM-Fac
- _id: LifeSc
- _id: ScienComp
alternative_title:
- ISTA Thesis
article_processing_charge: No
author:
- first_name: Dario J
full_name: Porley, Dario J
id: 2FD6EA6C-F248-11E8-B48F-1D18A9856A87
last_name: Porley
citation:
ama: Porley Esteves D. Structural characterization of spumavirus capsid assemblies.
2024. doi:10.15479/at:ista:18101
apa: Porley Esteves, D. (2024). Structural characterization of spumavirus capsid
assemblies. Institute of Science and Technology Austria. https://doi.org/10.15479/at:ista:18101
chicago: Porley Esteves, Darío. “Structural Characterization of Spumavirus Capsid
Assemblies.” Institute of Science and Technology Austria, 2024. https://doi.org/10.15479/at:ista:18101.
ieee: D. Porley Esteves, “Structural characterization of spumavirus capsid assemblies,”
Institute of Science and Technology Austria, 2024.
ista: Porley Esteves D. 2024. Structural characterization of spumavirus capsid assemblies.
Institute of Science and Technology Austria.
mla: Porley Esteves, Darío. Structural Characterization of Spumavirus Capsid
Assemblies. Institute of Science and Technology Austria, 2024, doi:10.15479/at:ista:18101.
short: D. Porley Esteves, Structural Characterization of Spumavirus Capsid Assemblies,
Institute of Science and Technology Austria, 2024.
corr_author: '1'
date_created: 2024-09-20T10:21:03Z
date_published: 2024-09-26T00:00:00Z
date_updated: 2026-04-07T13:21:01Z
day: '26'
ddc:
- '570'
degree_awarded: PhD
department:
- _id: GradSch
- _id: FlSc
doi: 10.15479/at:ista:18101
ec_funded: 1
file:
- access_level: closed
checksum: 3b8b0bacfe61112f3852744f3170e468
content_type: application/vnd.openxmlformats-officedocument.wordprocessingml.document
creator: dporley
date_created: 2024-09-26T13:40:33Z
date_updated: 2025-03-25T23:30:03Z
embargo_to: open_access
file_id: '18149'
file_name: PhD_thesis_DPorley_final_20240919.docx
file_size: 14213128
relation: source_file
- access_level: open_access
checksum: 6c3a652a8eede874118e11d66a63652f
content_type: application/pdf
creator: dporley
date_created: 2024-09-26T13:41:39Z
date_updated: 2025-03-25T23:30:03Z
embargo: 2025-03-25
file_id: '18150'
file_name: PhD_thesis_DPorley_final_20240926_pdfa1.pdf
file_size: 18583031
relation: main_file
file_date_updated: 2025-03-25T23:30:03Z
has_accepted_license: '1'
language:
- iso: eng
month: '09'
oa: 1
oa_version: Published Version
page: '131'
project:
- _id: 2564DBCA-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '665385'
name: International IST Doctoral Program
- _id: 9B9C98E0-BA93-11EA-9121-9846C619BF3A
grant_number: '25762'
name: Structural characterization of spumavirus capsid assemblies to understand
conserved Ortervirales assembly mechanisms
publication_identifier:
isbn:
- 978-3-99078-041-1
issn:
- 2663-337X
publication_status: published
publisher: Institute of Science and Technology Austria
status: public
supervisor:
- first_name: Florian KM
full_name: Schur, Florian KM
id: 48AD8942-F248-11E8-B48F-1D18A9856A87
last_name: Schur
orcid: 0000-0003-4790-8078
title: Structural characterization of spumavirus capsid assemblies
type: dissertation
user_id: ba8df636-2132-11f1-aed0-ed93e2281fdd
year: '2024'
...
---
_id: '12334'
abstract:
- lang: eng
text: Regulation of the Arp2/3 complex is required for productive nucleation of
branched actin networks. An emerging aspect of regulation is the incorporation
of subunit isoforms into the Arp2/3 complex. Specifically, both ArpC5 subunit
isoforms, ArpC5 and ArpC5L, have been reported to fine-tune nucleation activity
and branch junction stability. We have combined reverse genetics and cellular
structural biology to describe how ArpC5 and ArpC5L differentially affect cell
migration. Both define the structural stability of ArpC1 in branch junctions and,
in turn, by determining protrusion characteristics, affect protein dynamics and
actin network ultrastructure. ArpC5 isoforms also affect the positioning of members
of the Ena/Vasodilator-stimulated phosphoprotein (VASP) family of actin filament
elongators, which mediate ArpC5 isoform–specific effects on the actin assembly
level. Our results suggest that ArpC5 and Ena/VASP proteins are part of a signaling
pathway enhancing cell migration.
acknowledged_ssus:
- _id: ScienComp
- _id: LifeSc
- _id: Bio
- _id: EM-Fac
acknowledgement: "We would like to thank K. von Peinen and B. Denker (Helmholtz Centre
for Infection Research, Braunschweig, Germany) for experimental and technical assistance,
respectively.\r\nThis research was supported by the Scientific Service Units (SSUs)
of ISTA through resources provided by Scientific Computing (SciComp), the Life Science
Facility (LSF), the Imaging and Optics facility (IOF), and the Electron Microscopy
Facility (EMF). We acknowledge support from ISTA and from the Austrian Science Fund
(FWF) (P33367) to F.K.M.S., from the Research Training Group GRK2223 and the Helmholtz
Society to K.R,. and from the Deutsche Forschungsgemeinschaft (DFG) to J.F. and
K.R."
article_number: add6495
article_processing_charge: No
article_type: original
author:
- first_name: Florian
full_name: Fäßler, Florian
id: 404F5528-F248-11E8-B48F-1D18A9856A87
last_name: Fäßler
orcid: 0000-0001-7149-769X
- first_name: Manjunath
full_name: Javoor, Manjunath
id: 305ab18b-dc7d-11ea-9b2f-b58195228ea2
last_name: Javoor
orcid: 0000-0003-2311-2112
- first_name: Julia
full_name: Datler, Julia
id: 3B12E2E6-F248-11E8-B48F-1D18A9856A87
last_name: Datler
orcid: 0000-0002-3616-8580
- first_name: Hermann
full_name: Döring, Hermann
last_name: Döring
- first_name: Florian
full_name: Hofer, Florian
id: b9d234ba-9e33-11ed-95b6-cd561df280e6
last_name: Hofer
- first_name: Georgi A
full_name: Dimchev, Georgi A
id: 38C393BE-F248-11E8-B48F-1D18A9856A87
last_name: Dimchev
orcid: 0000-0001-8370-6161
- first_name: Victor-Valentin
full_name: Hodirnau, Victor-Valentin
id: 3661B498-F248-11E8-B48F-1D18A9856A87
last_name: Hodirnau
orcid: 0000-0003-3904-947X
- first_name: Jan
full_name: Faix, Jan
last_name: Faix
- first_name: Klemens
full_name: Rottner, Klemens
last_name: Rottner
- first_name: Florian KM
full_name: Schur, Florian KM
id: 48AD8942-F248-11E8-B48F-1D18A9856A87
last_name: Schur
orcid: 0000-0003-4790-8078
citation:
ama: Fäßler F, Javoor M, Datler J, et al. ArpC5 isoforms regulate Arp2/3 complex–dependent
protrusion through differential Ena/VASP positioning. Science Advances.
2023;9(3). doi:10.1126/sciadv.add6495
apa: Fäßler, F., Javoor, M., Datler, J., Döring, H., Hofer, F., Dimchev, G. A.,
… Schur, F. K. (2023). ArpC5 isoforms regulate Arp2/3 complex–dependent protrusion
through differential Ena/VASP positioning. Science Advances. American Association
for the Advancement of Science. https://doi.org/10.1126/sciadv.add6495
chicago: Fäßler, Florian, Manjunath Javoor, Julia Datler, Hermann Döring, Florian
Hofer, Georgi A Dimchev, Victor-Valentin Hodirnau, Jan Faix, Klemens Rottner,
and Florian KM Schur. “ArpC5 Isoforms Regulate Arp2/3 Complex–Dependent Protrusion
through Differential Ena/VASP Positioning.” Science Advances. American
Association for the Advancement of Science, 2023. https://doi.org/10.1126/sciadv.add6495.
ieee: F. Fäßler et al., “ArpC5 isoforms regulate Arp2/3 complex–dependent
protrusion through differential Ena/VASP positioning,” Science Advances,
vol. 9, no. 3. American Association for the Advancement of Science, 2023.
ista: Fäßler F, Javoor M, Datler J, Döring H, Hofer F, Dimchev GA, Hodirnau V-V,
Faix J, Rottner K, Schur FK. 2023. ArpC5 isoforms regulate Arp2/3 complex–dependent
protrusion through differential Ena/VASP positioning. Science Advances. 9(3),
add6495.
mla: Fäßler, Florian, et al. “ArpC5 Isoforms Regulate Arp2/3 Complex–Dependent Protrusion
through Differential Ena/VASP Positioning.” Science Advances, vol. 9, no.
3, add6495, American Association for the Advancement of Science, 2023, doi:10.1126/sciadv.add6495.
short: F. Fäßler, M. Javoor, J. Datler, H. Döring, F. Hofer, G.A. Dimchev, V.-V.
Hodirnau, J. Faix, K. Rottner, F.K. Schur, Science Advances 9 (2023).
corr_author: '1'
date_created: 2023-01-23T07:26:42Z
date_published: 2023-01-20T00:00:00Z
date_updated: 2026-04-07T12:59:44Z
day: '20'
ddc:
- '570'
department:
- _id: FlSc
- _id: EM-Fac
doi: 10.1126/sciadv.add6495
external_id:
isi:
- '000964550100015'
pmid:
- '36662867'
file:
- access_level: open_access
checksum: ce81a6d0b84170e5e8c62f6acfa15d9e
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creator: dernst
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name: Structure and isoform diversity of the Arp2/3 complex
publication: Science Advances
publication_identifier:
issn:
- 2375-2548
publication_status: published
publisher: American Association for the Advancement of Science
quality_controlled: '1'
related_material:
record:
- id: '14562'
relation: research_data
status: public
- id: '18766'
relation: dissertation_contains
status: public
scopus_import: '1'
status: public
title: ArpC5 isoforms regulate Arp2/3 complex–dependent protrusion through differential
Ena/VASP positioning
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 9
year: '2023'
...
---
_id: '12421'
abstract:
- lang: eng
text: The actin cytoskeleton plays a key role in cell migration and cellular morphodynamics
in most eukaryotes. The ability of the actin cytoskeleton to assemble and disassemble
in a spatiotemporally controlled manner allows it to form higher-order structures,
which can generate forces required for a cell to explore and navigate through
its environment. It is regulated not only via a complex synergistic and competitive
interplay between actin-binding proteins (ABP), but also by filament biochemistry
and filament geometry. The lack of structural insights into how geometry and ABPs
regulate the actin cytoskeleton limits our understanding of the molecular mechanisms
that define actin cytoskeleton remodeling and, in turn, impact emerging cell migration
characteristics. With the advent of cryo-electron microscopy (cryo-EM) and advanced
computational methods, it is now possible to define these molecular mechanisms
involving actin and its interactors at both atomic and ultra-structural levels
in vitro and in cellulo. In this review, we will provide an overview of the available
cryo-EM methods, applicable to further our understanding of the actin cytoskeleton,
specifically in the context of cell migration. We will discuss how these methods
have been employed to elucidate ABP- and geometry-defined regulatory mechanisms
in initiating, maintaining, and disassembling cellular actin networks in migratory
protrusions.
acknowledgement: 'We apologize for not being able to mention and cite additional excellent
work that would have fit the scope of this review, due to space restraints. We thank
Jesse Hansen for comments on the manuscript. We acknowledge support from the Austrian
Science Fund (FWF): P33367 and the Institute of Science and Technology Austria.'
article_processing_charge: No
article_type: original
author:
- first_name: Florian
full_name: Fäßler, Florian
id: 404F5528-F248-11E8-B48F-1D18A9856A87
last_name: Fäßler
orcid: 0000-0001-7149-769X
- first_name: Manjunath
full_name: Javoor, Manjunath
id: 305ab18b-dc7d-11ea-9b2f-b58195228ea2
last_name: Javoor
- first_name: Florian KM
full_name: Schur, Florian KM
id: 48AD8942-F248-11E8-B48F-1D18A9856A87
last_name: Schur
orcid: 0000-0003-4790-8078
citation:
ama: Fäßler F, Javoor M, Schur FK. Deciphering the molecular mechanisms of actin
cytoskeleton regulation in cell migration using cryo-EM. Biochemical Society
Transactions. 2023;51(1):87-99. doi:10.1042/bst20220221
apa: Fäßler, F., Javoor, M., & Schur, F. K. (2023). Deciphering the molecular
mechanisms of actin cytoskeleton regulation in cell migration using cryo-EM. Biochemical
Society Transactions. Portland Press. https://doi.org/10.1042/bst20220221
chicago: Fäßler, Florian, Manjunath Javoor, and Florian KM Schur. “Deciphering the
Molecular Mechanisms of Actin Cytoskeleton Regulation in Cell Migration Using
Cryo-EM.” Biochemical Society Transactions. Portland Press, 2023. https://doi.org/10.1042/bst20220221.
ieee: F. Fäßler, M. Javoor, and F. K. Schur, “Deciphering the molecular mechanisms
of actin cytoskeleton regulation in cell migration using cryo-EM,” Biochemical
Society Transactions, vol. 51, no. 1. Portland Press, pp. 87–99, 2023.
ista: Fäßler F, Javoor M, Schur FK. 2023. Deciphering the molecular mechanisms of
actin cytoskeleton regulation in cell migration using cryo-EM. Biochemical Society
Transactions. 51(1), 87–99.
mla: Fäßler, Florian, et al. “Deciphering the Molecular Mechanisms of Actin Cytoskeleton
Regulation in Cell Migration Using Cryo-EM.” Biochemical Society Transactions,
vol. 51, no. 1, Portland Press, 2023, pp. 87–99, doi:10.1042/bst20220221.
short: F. Fäßler, M. Javoor, F.K. Schur, Biochemical Society Transactions 51 (2023)
87–99.
corr_author: '1'
date_created: 2023-01-27T10:08:19Z
date_published: 2023-02-01T00:00:00Z
date_updated: 2025-04-23T08:47:15Z
day: '01'
ddc:
- '570'
department:
- _id: FlSc
doi: 10.1042/bst20220221
external_id:
isi:
- '000926043100001'
pmid:
- '36695514'
file:
- access_level: open_access
checksum: 4e7069845e3dad22bb44fb71ec624c60
content_type: application/pdf
creator: dernst
date_created: 2023-03-16T07:58:16Z
date_updated: 2023-03-16T07:58:16Z
file_id: '12728'
file_name: 2023_BioChemicalSocietyTransactions_Faessler.pdf
file_size: 10045006
relation: main_file
success: 1
file_date_updated: 2023-03-16T07:58:16Z
has_accepted_license: '1'
intvolume: ' 51'
isi: 1
issue: '1'
keyword:
- Biochemistry
language:
- iso: eng
month: '02'
oa: 1
oa_version: Published Version
page: 87-99
pmid: 1
project:
- _id: 9B954C5C-BA93-11EA-9121-9846C619BF3A
grant_number: P33367
name: Structure and isoform diversity of the Arp2/3 complex
publication: Biochemical Society Transactions
publication_identifier:
eissn:
- 1470-8752
issn:
- 0300-5127
publication_status: published
publisher: Portland Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: Deciphering the molecular mechanisms of actin cytoskeleton regulation in cell
migration using cryo-EM
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 51
year: '2023'
...
---
_id: '14255'
abstract:
- lang: eng
text: Toscana virus is a major cause of arboviral disease in humans in the Mediterranean
basin during summer. However, early virus-host cell interactions and entry mechanisms
remain poorly characterized. Investigating iPSC-derived human neurons and cell
lines, we found that virus binding to the cell surface was specific, and 50% of
bound virions were endocytosed within 10 min. Virions entered Rab5a+ early endosomes
and, subsequently, Rab7a+ and LAMP-1+ late endosomal compartments. Penetration
required intact late endosomes and occurred within 30 min following internalization.
Virus entry relied on vacuolar acidification, with an optimal pH for viral membrane
fusion at pH 5.5. The pH threshold increased to 5.8 with longer pre-exposure of
virions to the slightly acidic pH in early endosomes. Strikingly, the particles
remained infectious after entering late endosomes with a pH below the fusion threshold.
Overall, our study establishes Toscana virus as a late-penetrating virus and reveals
an atypical use of vacuolar acidity by this virus to enter host cells.
acknowledged_ssus:
- _id: EM-Fac
acknowledgement: "We acknowledge Elodie Chatre and the Imaging Platform Platim, SFR
Biosciences, Lyon, as well as Vibor Laketa and the Infectious Diseases Imaging Platform
(IDIP) at the Center for Integrative Infectious Disease Research (CIID) Heidelberg.
The sand fly cell lines were supplied by the Tick Cell Biobank at the University
of Liverpool. F.K.M.S. acknowledges support from the Scientific Service Units (SSUs)
of ISTA through resources provided by the Electron Microscopy Facility (EMF).\r\nThis
work was supported by CellNetworks Research Group funds and Deutsche Forschungsgemeinschaft
(DFG) funding (LO-2338/3-1) and the Agence Nationale de la Recherche (ANR) funding
(grant numbers ANR-21-CE11-0012 and ANR-22-CE15-0034), all awarded to P.-Y.L. This
work was also supported by the LABEX ECOFECT (ANR-11-LABX-0048) of Université de
Lyon (UDL), within the program “Investissements d’Avenir” (ANR-11-IDEX-0007) operated
by the ANR and by the RESPOND program of the UDL (awarded to P.-Y.L) . C.A. was
supported by the Chica and Heinz Schaller Research Group funds, NARSAD 2019 award,
a Fritz Thyssen Research Grant, and the SFB1158-S02 grant. L.B-S. is supported by
a United Kingdom Biotechnology and Biological Sciences Research Council grant (BB/P024270/1)
and a Wellcome Trust grant (223743/Z/21/Z). F.K.M.S acknowledges support from the
Austrian Science Fund (FWF, P31445). J.K. received a salary from the DFG (LO-2338/3-1)
and then from the ANR (ANR-11-LABX-0048). The salary of Z.M.U. was partially covered
by the DFG (LO-2338/3-1). S.K. received a salary from the DFG (SFB1129). We are
grateful to the Chinese Scholarship Council (CSC; 201904910701), DAAD/ANID (57451854/62180003),
the Rufus A. Kellogg fellowship program (Amherst College, Massachusetts, USA) for
awarding fellowships to Q.X., J.C., and H.A.A., respectively."
article_number: e1011562
article_processing_charge: Yes
article_type: original
author:
- first_name: Jana
full_name: Koch, Jana
last_name: Koch
- first_name: Qilin
full_name: Xin, Qilin
last_name: Xin
- first_name: Martin
full_name: Obr, Martin
id: 4741CA5A-F248-11E8-B48F-1D18A9856A87
last_name: Obr
orcid: 0000-0003-1756-6564
- first_name: Alicia
full_name: Schäfer, Alicia
last_name: Schäfer
- first_name: Nina
full_name: Rolfs, Nina
last_name: Rolfs
- first_name: Holda A.
full_name: Anagho, Holda A.
last_name: Anagho
- first_name: Aiste
full_name: Kudulyte, Aiste
last_name: Kudulyte
- first_name: Lea
full_name: Woltereck, Lea
last_name: Woltereck
- first_name: Susann
full_name: Kummer, Susann
last_name: Kummer
- first_name: Joaquin
full_name: Campos, Joaquin
last_name: Campos
- first_name: Zina M.
full_name: Uckeley, Zina M.
last_name: Uckeley
- first_name: Lesley
full_name: Bell-Sakyi, Lesley
last_name: Bell-Sakyi
- first_name: Hans Georg
full_name: Kräusslich, Hans Georg
last_name: Kräusslich
- first_name: Florian Km
full_name: Schur, Florian Km
id: 48AD8942-F248-11E8-B48F-1D18A9856A87
last_name: Schur
orcid: 0000-0003-4790-8078
- first_name: Claudio
full_name: Acuna, Claudio
last_name: Acuna
- first_name: Pierre Yves
full_name: Lozach, Pierre Yves
last_name: Lozach
citation:
ama: Koch J, Xin Q, Obr M, et al. The phenuivirus Toscana virus makes an atypical
use of vacuolar acidity to enter host cells. PLoS Pathogens. 2023;19(8).
doi:10.1371/journal.ppat.1011562
apa: Koch, J., Xin, Q., Obr, M., Schäfer, A., Rolfs, N., Anagho, H. A., … Lozach,
P. Y. (2023). The phenuivirus Toscana virus makes an atypical use of vacuolar
acidity to enter host cells. PLoS Pathogens. Public Library of Science.
https://doi.org/10.1371/journal.ppat.1011562
chicago: Koch, Jana, Qilin Xin, Martin Obr, Alicia Schäfer, Nina Rolfs, Holda A.
Anagho, Aiste Kudulyte, et al. “The Phenuivirus Toscana Virus Makes an Atypical
Use of Vacuolar Acidity to Enter Host Cells.” PLoS Pathogens. Public Library
of Science, 2023. https://doi.org/10.1371/journal.ppat.1011562.
ieee: J. Koch et al., “The phenuivirus Toscana virus makes an atypical use
of vacuolar acidity to enter host cells,” PLoS Pathogens, vol. 19, no.
8. Public Library of Science, 2023.
ista: Koch J, Xin Q, Obr M, Schäfer A, Rolfs N, Anagho HA, Kudulyte A, Woltereck
L, Kummer S, Campos J, Uckeley ZM, Bell-Sakyi L, Kräusslich HG, Schur FK, Acuna
C, Lozach PY. 2023. The phenuivirus Toscana virus makes an atypical use of vacuolar
acidity to enter host cells. PLoS Pathogens. 19(8), e1011562.
mla: Koch, Jana, et al. “The Phenuivirus Toscana Virus Makes an Atypical Use of
Vacuolar Acidity to Enter Host Cells.” PLoS Pathogens, vol. 19, no. 8,
e1011562, Public Library of Science, 2023, doi:10.1371/journal.ppat.1011562.
short: J. Koch, Q. Xin, M. Obr, A. Schäfer, N. Rolfs, H.A. Anagho, A. Kudulyte,
L. Woltereck, S. Kummer, J. Campos, Z.M. Uckeley, L. Bell-Sakyi, H.G. Kräusslich,
F.K. Schur, C. Acuna, P.Y. Lozach, PLoS Pathogens 19 (2023).
date_created: 2023-09-03T22:01:14Z
date_published: 2023-08-14T00:00:00Z
date_updated: 2025-04-15T08:24:50Z
day: '14'
ddc:
- '570'
department:
- _id: FlSc
doi: 10.1371/journal.ppat.1011562
external_id:
isi:
- '001050846300004'
pmid:
- '37578957'
file:
- access_level: open_access
checksum: 47ca3bb54b27f28b05644be0ad064bc6
content_type: application/pdf
creator: dernst
date_created: 2023-09-06T06:41:52Z
date_updated: 2023-09-06T06:41:52Z
file_id: '14269'
file_name: 2023_PloSPathogens_Koch.pdf
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isi: 1
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month: '08'
oa: 1
oa_version: Published Version
pmid: 1
project:
- _id: 26736D6A-B435-11E9-9278-68D0E5697425
call_identifier: FWF
grant_number: P31445
name: Structural conservation and diversity in retroviral capsid
publication: PLoS Pathogens
publication_identifier:
eissn:
- 1553-7374
issn:
- 1553-7366
publication_status: published
publisher: Public Library of Science
quality_controlled: '1'
scopus_import: '1'
status: public
title: The phenuivirus Toscana virus makes an atypical use of vacuolar acidity to
enter host cells
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 19
year: '2023'
...
---
_id: '14562'
abstract:
- lang: eng
text: "Regulation of the Arp2/3 complex is required for productive nucleation of
branched actin networks. An emerging aspect of regulation is the incorporation
of subunit isoforms into the Arp2/3 complex. Specifically, both ArpC5 subunit
isoforms, ArpC5 and ArpC5L, have been reported to fine-tune nucleation activity
and branch junction stability. We have combined reverse genetics and cellular
structural biology to describe how ArpC5 and ArpC5L differentially affect cell
migration. Both define the structural stability of ArpC1 in branch junctions and,
in turn, by determining protrusion characteristics, affect protein dynamics and
actin network ultrastructure. ArpC5 isoforms also affect the positioning of members
of the Ena/Vasodilator-stimulated phosphoprotein (VASP) family of actin filament
elongators, which mediate ArpC5 isoform–specific effects on the actin assembly
level. Our results suggest that ArpC5 and Ena/VASP proteins are part of a signaling
pathway enhancing cell migration.\r\n"
acknowledged_ssus:
- _id: LifeSc
- _id: Bio
- _id: ScienComp
- _id: EM-Fac
acknowledgement: "We would like to thank K. von Peinen and B. Denker (Helmholtz Centre
for Infection Research, Braunschweig, Germany) for experimental and technical assistance,
respectively.\r\nFunding: This research was supported by the Scientific Service
Units (SSUs) of ISTA through resources provided by Scientific Computing (SciComp),
the Life Science Facility (LSF), the Imaging and Optics facility (IOF), and the
Electron Microscopy Facility (EMF). We acknowledge support from ISTA and from the
Austrian Science Fund (FWF) (P33367) to F.K.M.S., from the Research Training Group
GRK2223 and the Helmholtz Society to K.R,. and from the Deutsche Forschungsgemeinschaft
(DFG) to J.F. and K.R."
article_processing_charge: No
author:
- first_name: Florian KM
full_name: Schur, Florian KM
id: 48AD8942-F248-11E8-B48F-1D18A9856A87
last_name: Schur
orcid: 0000-0003-4790-8078
citation:
ama: Schur FK. Research data of the publication “ArpC5 isoforms regulate Arp2/3
complex-dependent protrusion through differential Ena/VASP positioning.” 2023.
doi:10.15479/AT:ISTA:14562
apa: Schur, F. K. (2023). Research data of the publication “ArpC5 isoforms regulate
Arp2/3 complex-dependent protrusion through differential Ena/VASP positioning.”
Institute of Science and Technology Austria. https://doi.org/10.15479/AT:ISTA:14562
chicago: Schur, Florian KM. “Research Data of the Publication ‘ArpC5 Isoforms Regulate
Arp2/3 Complex-Dependent Protrusion through Differential Ena/VASP Positioning.’”
Institute of Science and Technology Austria, 2023. https://doi.org/10.15479/AT:ISTA:14562.
ieee: F. K. Schur, “Research data of the publication ‘ArpC5 isoforms regulate Arp2/3
complex-dependent protrusion through differential Ena/VASP positioning.’” Institute
of Science and Technology Austria, 2023.
ista: Schur FK. 2023. Research data of the publication ‘ArpC5 isoforms regulate
Arp2/3 complex-dependent protrusion through differential Ena/VASP positioning’,
Institute of Science and Technology Austria, 10.15479/AT:ISTA:14562.
mla: Schur, Florian KM. Research Data of the Publication “ArpC5 Isoforms Regulate
Arp2/3 Complex-Dependent Protrusion through Differential Ena/VASP Positioning.”
Institute of Science and Technology Austria, 2023, doi:10.15479/AT:ISTA:14562.
short: F.K. Schur, (2023).
contributor:
- contributor_type: researcher
first_name: Florian
id: 404F5528-F248-11E8-B48F-1D18A9856A87
last_name: Fäßler
orcid: 0000-0001-7149-769X
- contributor_type: researcher
first_name: Manjunath
id: 305ab18b-dc7d-11ea-9b2f-b58195228ea2
last_name: Javoor
- contributor_type: researcher
first_name: Julia
id: 3B12E2E6-F248-11E8-B48F-1D18A9856A87
last_name: Datler
orcid: 0000-0002-3616-8580
- contributor_type: researcher
first_name: Hermann
last_name: Döring
- contributor_type: researcher
first_name: Florian
id: b9d234ba-9e33-11ed-95b6-cd561df280e6
last_name: Hofer
- contributor_type: researcher
first_name: Georgi A
id: 38C393BE-F248-11E8-B48F-1D18A9856A87
last_name: Dimchev
orcid: 0000-0001-8370-6161
- contributor_type: researcher
first_name: Victor-Valentin
id: 3661B498-F248-11E8-B48F-1D18A9856A87
last_name: Hodirnau
- contributor_type: researcher
first_name: Jan
last_name: Faix
- contributor_type: researcher
first_name: Klemens
last_name: Rottner
- contributor_type: researcher
first_name: Florian KM
id: 48AD8942-F248-11E8-B48F-1D18A9856A87
last_name: Schur
orcid: 0000-0003-4790-8078
corr_author: '1'
date_created: 2023-11-20T09:22:33Z
date_published: 2023-11-21T00:00:00Z
date_updated: 2025-04-23T08:46:21Z
day: '21'
ddc:
- '570'
department:
- _id: FlSc
doi: 10.15479/AT:ISTA:14562
file:
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checksum: e9bab797b44614f144a5b02d9636f8c3
content_type: application/zip
creator: fschur
date_created: 2023-11-20T10:27:17Z
date_updated: 2023-11-20T10:27:17Z
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file_name: Figure2.zip
file_size: 1581687449
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content_type: application/zip
creator: fschur
date_created: 2023-11-20T10:29:18Z
date_updated: 2023-11-20T10:29:18Z
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oa: 1
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grant_number: P33367
name: Structure and isoform diversity of the Arp2/3 complex
publisher: Institute of Science and Technology Austria
related_material:
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status: public
title: Research data of the publication "ArpC5 isoforms regulate Arp2/3 complex-dependent
protrusion through differential Ena/VASP positioning"
tmp:
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legal_code_url: https://creativecommons.org/licenses/by-sa/4.0/legalcode
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...
---
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abstract:
- lang: eng
text: The next steps of deep space exploration are manned missions to Moon and Mars.
For safe space missions for crew members, it is important to understand the impact
of space flight on the immune system. We studied the effects of 21 days dry immersion
(DI) exposure on the transcriptomes of T cells isolated from blood samples of
eight healthy volunteers. Samples were collected 7 days before DI, at day 7, 14,
and 21 during DI, and 7 days after DI. RNA sequencing of CD3+T cells revealed
transcriptional alterations across all time points, with most changes occurring
14 days after DI exposure. At day 21, T cells showed evidence of adaptation with
a transcriptional profile resembling that of 7 days before DI. At 7 days after
DI, T cells again changed their transcriptional profile. These data suggest that
T cells adapt by rewiring their transcriptomes in response to simulated weightlessness
and that remodeling cues persist when reexposed to normal gravity.
acknowledgement: This work was supported by a postdoctoral fellowship from the Swedish
Society for Medical Research to J.R., a CAPES-STINT joint grant to R.G.G. and L.S.W.,
a PhD fellowship from Karolinska Institutet (KID) to E.D., a PhD fellowship from
Fundação para a Ciência e a Tecnologia and European Social Fund to M.M.S.O., the
program of fundamental research (theme 65.1) of the Institute for Biomedical Problems
of the Russian Academy of Sciences (IBMP RAS) to A.A.S., S.M.S., V.A.S., O.V.K.,
D.D.V., K.D.O., M.P.R., and S.A.P., the Tamkeen under the NYU Abu Dhabi Research
Institute Award to the NYUAD Center for Genomics and Systems Biology (ADHPG-CGSB)
to P.P., the Knut and Alice Wallenberg foundation to C.K., the Swedish National
Space Agency to N.V.K. and L.S.W., Swedish Research Council, Gösta Fraenckel Foundation,
and Karolinska Institutet to L.S.W.
article_number: adg1610
article_processing_charge: Yes
article_type: original
author:
- first_name: Carlos J.
full_name: Gallardo-Dodd, Carlos J.
last_name: Gallardo-Dodd
- first_name: Christian
full_name: Oertlin, Christian
last_name: Oertlin
- first_name: Julien
full_name: Record, Julien
last_name: Record
- first_name: Rômulo G.
full_name: Galvani, Rômulo G.
last_name: Galvani
- first_name: Christian
full_name: Sommerauer, Christian
last_name: Sommerauer
- first_name: Nikolai V.
full_name: Kuznetsov, Nikolai V.
last_name: Kuznetsov
- first_name: Evangelos
full_name: Doukoumopoulos, Evangelos
last_name: Doukoumopoulos
- first_name: Liaqat
full_name: Ali, Liaqat
last_name: Ali
- first_name: Mariana M. S.
full_name: Oliveira, Mariana M. S.
last_name: Oliveira
- first_name: Christina
full_name: Seitz, Christina
last_name: Seitz
- first_name: Mathias
full_name: Percipalle, Mathias
id: 4986e21c-eb97-11eb-a6c2-a4ef0b629971
last_name: Percipalle
- first_name: Tijana
full_name: Nikić, Tijana
last_name: Nikić
- first_name: Anastasia A.
full_name: Sadova, Anastasia A.
last_name: Sadova
- first_name: Sofia M.
full_name: Shulgina, Sofia M.
last_name: Shulgina
- first_name: Vjacheslav A.
full_name: Shmarov, Vjacheslav A.
last_name: Shmarov
- first_name: Olga V.
full_name: Kutko, Olga V.
last_name: Kutko
- first_name: Daria D.
full_name: Vlasova, Daria D.
last_name: Vlasova
- first_name: Kseniya D.
full_name: Orlova, Kseniya D.
last_name: Orlova
- first_name: Marina P.
full_name: Rykova, Marina P.
last_name: Rykova
- first_name: John
full_name: Andersson, John
last_name: Andersson
- first_name: Piergiorgio
full_name: Percipalle, Piergiorgio
last_name: Percipalle
- first_name: Claudia
full_name: Kutter, Claudia
last_name: Kutter
- first_name: Sergey A.
full_name: Ponomarev, Sergey A.
last_name: Ponomarev
- first_name: Lisa S.
full_name: Westerberg, Lisa S.
last_name: Westerberg
citation:
ama: Gallardo-Dodd CJ, Oertlin C, Record J, et al. Exposure of volunteers to microgravity
by dry immersion bed over 21 days results in gene expression changes and adaptation
of T cells. Science Advances. 2023;9(34). doi:10.1126/sciadv.adg1610
apa: Gallardo-Dodd, C. J., Oertlin, C., Record, J., Galvani, R. G., Sommerauer,
C., Kuznetsov, N. V., … Westerberg, L. S. (2023). Exposure of volunteers to microgravity
by dry immersion bed over 21 days results in gene expression changes and adaptation
of T cells. Science Advances. American Association for the Advancement
of Science. https://doi.org/10.1126/sciadv.adg1610
chicago: Gallardo-Dodd, Carlos J., Christian Oertlin, Julien Record, Rômulo G. Galvani,
Christian Sommerauer, Nikolai V. Kuznetsov, Evangelos Doukoumopoulos, et al. “Exposure
of Volunteers to Microgravity by Dry Immersion Bed over 21 Days Results in Gene
Expression Changes and Adaptation of T Cells.” Science Advances. American
Association for the Advancement of Science, 2023. https://doi.org/10.1126/sciadv.adg1610.
ieee: C. J. Gallardo-Dodd et al., “Exposure of volunteers to microgravity
by dry immersion bed over 21 days results in gene expression changes and adaptation
of T cells,” Science Advances, vol. 9, no. 34. American Association for
the Advancement of Science, 2023.
ista: Gallardo-Dodd CJ, Oertlin C, Record J, Galvani RG, Sommerauer C, Kuznetsov
NV, Doukoumopoulos E, Ali L, Oliveira MMS, Seitz C, Percipalle M, Nikić T, Sadova
AA, Shulgina SM, Shmarov VA, Kutko OV, Vlasova DD, Orlova KD, Rykova MP, Andersson
J, Percipalle P, Kutter C, Ponomarev SA, Westerberg LS. 2023. Exposure of volunteers
to microgravity by dry immersion bed over 21 days results in gene expression changes
and adaptation of T cells. Science Advances. 9(34), adg1610.
mla: Gallardo-Dodd, Carlos J., et al. “Exposure of Volunteers to Microgravity by
Dry Immersion Bed over 21 Days Results in Gene Expression Changes and Adaptation
of T Cells.” Science Advances, vol. 9, no. 34, adg1610, American Association
for the Advancement of Science, 2023, doi:10.1126/sciadv.adg1610.
short: C.J. Gallardo-Dodd, C. Oertlin, J. Record, R.G. Galvani, C. Sommerauer, N.V.
Kuznetsov, E. Doukoumopoulos, L. Ali, M.M.S. Oliveira, C. Seitz, M. Percipalle,
T. Nikić, A.A. Sadova, S.M. Shulgina, V.A. Shmarov, O.V. Kutko, D.D. Vlasova,
K.D. Orlova, M.P. Rykova, J. Andersson, P. Percipalle, C. Kutter, S.A. Ponomarev,
L.S. Westerberg, Science Advances 9 (2023).
date_created: 2024-01-10T09:48:01Z
date_published: 2023-08-25T00:00:00Z
date_updated: 2024-09-09T08:03:13Z
day: '25'
ddc:
- '570'
department:
- _id: FlSc
doi: 10.1126/sciadv.adg1610
external_id:
isi:
- '001054596800007'
pmid:
- '37624890'
file:
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checksum: b9072e20e2d5d9d34d2c53319bafee41
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intvolume: ' 9'
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keyword:
- Multidisciplinary
language:
- iso: eng
month: '08'
oa: 1
oa_version: Published Version
pmid: 1
publication: Science Advances
publication_identifier:
issn:
- 2375-2548
publication_status: published
publisher: American Association for the Advancement of Science
quality_controlled: '1'
status: public
title: Exposure of volunteers to microgravity by dry immersion bed over 21 days results
in gene expression changes and adaptation of T cells
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 9
year: '2023'
...
---
_id: '14502'
abstract:
- lang: eng
text: A precise quantitative description of the ultrastructural characteristics
underlying biological mechanisms is often key to their understanding. This is
particularly true for dynamic extra- and intracellular filamentous assemblies,
playing a role in cell motility, cell integrity, cytokinesis, tissue formation
and maintenance. For example, genetic manipulation or modulation of actin regulatory
proteins frequently manifests in changes of the morphology, dynamics, and ultrastructural
architecture of actin filament-rich cell peripheral structures, such as lamellipodia
or filopodia. However, the observed ultrastructural effects often remain subtle
and require sufficiently large datasets for appropriate quantitative analysis.
The acquisition of such large datasets has been enabled by recent advances in
high-throughput cryo-electron tomography (cryo-ET) methods. This also necessitates
the development of complementary approaches to maximize the extraction of relevant
biological information. We have developed a computational toolbox for the semi-automatic
quantification of segmented and vectorized fila- mentous networks from pre-processed
cryo-electron tomograms, facilitating the analysis and cross-comparison of multiple
experimental conditions. GUI-based components simplify the processing of data
and allow users to obtain a large number of ultrastructural parameters describing
filamentous assemblies. We demonstrate the feasibility of this workflow by analyzing
cryo-ET data of untreated and chemically perturbed branched actin filament networks
and that of parallel actin filament arrays. In principle, the computational toolbox
presented here is applicable for data analysis comprising any type of filaments
in regular (i.e. parallel) or random arrangement. We show that it can ease the
identification of key differences between experimental groups and facilitate the
in-depth analysis of ultrastructural data in a time-efficient manner.
author:
- first_name: Georgi A
full_name: Dimchev, Georgi A
id: 38C393BE-F248-11E8-B48F-1D18A9856A87
last_name: Dimchev
orcid: 0000-0001-8370-6161
- first_name: Behnam
full_name: Amiri, Behnam
last_name: Amiri
- first_name: Florian
full_name: Fäßler, Florian
id: 404F5528-F248-11E8-B48F-1D18A9856A87
last_name: Fäßler
orcid: 0000-0001-7149-769X
- first_name: Martin
full_name: Falcke, Martin
last_name: Falcke
- first_name: Florian KM
full_name: Schur, Florian KM
id: 48AD8942-F248-11E8-B48F-1D18A9856A87
last_name: Schur
orcid: 0000-0003-4790-8078
citation:
ama: Dimchev GA, Amiri B, Fäßler F, Falcke M, Schur FK. Computational toolbox for
ultrastructural quantitative analysis of filament networks in cryo-ET data. 2023.
doi:10.15479/AT:ISTA:14502
apa: Dimchev, G. A., Amiri, B., Fäßler, F., Falcke, M., & Schur, F. K. (2023).
Computational toolbox for ultrastructural quantitative analysis of filament networks
in cryo-ET data. Institute of Science and Technology Austria. https://doi.org/10.15479/AT:ISTA:14502
chicago: Dimchev, Georgi A, Behnam Amiri, Florian Fäßler, Martin Falcke, and Florian
KM Schur. “Computational Toolbox for Ultrastructural Quantitative Analysis of
Filament Networks in Cryo-ET Data.” Institute of Science and Technology Austria,
2023. https://doi.org/10.15479/AT:ISTA:14502.
ieee: G. A. Dimchev, B. Amiri, F. Fäßler, M. Falcke, and F. K. Schur, “Computational
toolbox for ultrastructural quantitative analysis of filament networks in cryo-ET
data.” Institute of Science and Technology Austria, 2023.
ista: Dimchev GA, Amiri B, Fäßler F, Falcke M, Schur FK. 2023. Computational toolbox
for ultrastructural quantitative analysis of filament networks in cryo-ET data,
Institute of Science and Technology Austria, 10.15479/AT:ISTA:14502.
mla: Dimchev, Georgi A., et al. Computational Toolbox for Ultrastructural Quantitative
Analysis of Filament Networks in Cryo-ET Data. Institute of Science and Technology
Austria, 2023, doi:10.15479/AT:ISTA:14502.
short: G.A. Dimchev, B. Amiri, F. Fäßler, M. Falcke, F.K. Schur, (2023).
corr_author: '1'
date_created: 2023-11-08T19:40:54Z
date_published: 2023-11-21T00:00:00Z
date_updated: 2026-07-06T12:57:43Z
day: '21'
ddc:
- '570'
department:
- _id: FlSc
doi: 10.15479/AT:ISTA:14502
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creator: fschur
date_created: 2023-11-08T20:23:07Z
date_updated: 2023-11-08T20:23:07Z
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file_name: Computational_Toolbox_v1.2.zip
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content_type: text/plain
creator: dernst
date_created: 2023-11-21T08:20:23Z
date_updated: 2023-11-21T08:20:23Z
file_id: '14586'
file_name: Readme.txt
file_size: 1522
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success: 1
file_date_updated: 2023-11-21T08:20:23Z
has_accepted_license: '1'
keyword:
- cryo-electron tomography
- actin cytoskeleton
- toolbox
license: https://choosealicense.com/licenses/agpl-3.0/
month: '11'
oa: 1
project:
- _id: 9B954C5C-BA93-11EA-9121-9846C619BF3A
grant_number: P33367
name: Structure and isoform diversity of the Arp2/3 complex
publisher: Institute of Science and Technology Austria
related_material:
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- id: '10290'
relation: used_for_analysis_in
status: public
status: public
title: Computational toolbox for ultrastructural quantitative analysis of filament
networks in cryo-ET data
tmp:
legal_code_url: https://www.gnu.org/licenses/agpl-3.0.html
name: GNU Affero General Public License v3.0
short: 'GNU AGPLv3 '
type: software
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2023'
...
---
OA_place: publisher
_id: '12491'
abstract:
- lang: eng
text: "The extracellular matrix (ECM) is a hydrated and complex three-dimensional
network consisting of proteins, polysaccharides, and water. It provides structural
scaffolding for the cells embedded within it and is essential in regulating numerous
physiological processes, including cell migration and proliferation, wound healing,
and stem cell fate. \r\nDespite extensive study, detailed structural knowledge
of ECM components in physiologically relevant conditions is still rudimentary.
This is due to methodological limitations in specimen preparation protocols which
are incompatible with keeping large samples, such as the ECM, in their native
state for subsequent imaging. Conventional electron microscopy (EM) techniques
rely on fixation, dehydration, contrasting, and sectioning. This results in the
alteration of a highly hydrated environment and the potential introduction of
artifacts. Other structural biology techniques, such as nuclear magnetic resonance
(NMR) spectroscopy and X-ray crystallography, allow high-resolution analysis of
protein structures but only work on homogenous and purified samples, hence lacking
contextual information. Currently, no approach exists for the ultrastructural
and structural study of extracellular components under native conditions in a
physiological, 3D environment. \r\nIn this thesis, I have developed a workflow
that allows for the ultrastructural analysis of the ECM in near-native conditions
at molecular resolution. The developments I introduced include implementing a
novel specimen preparation workflow for cell-derived matrices (CDMs) to render
them compatible with ion-beam milling and subsequent high-resolution cryo-electron
tomography (ET). \r\nTo this end, I have established protocols to generate CDMs
grown over several weeks on EM grids that are compatible with downstream cryo-EM
sample preparation and imaging techniques. Characterization of these ECMs confirmed
that they contain essential ECM components such as collagen I, collagen VI, and
fibronectin I in high abundance and hence represent a bona fide biologically-relevant
sample. I successfully optimized vitrification of these specimens by testing various
vitrification techniques and cryoprotectants. \r\nIn order to obtain high-resolution
molecular insights into the ultrastructure and organization of CDMs, I established
cryo-focused ion beam scanning electron microscopy (FIBSEM) on these challenging
and complex specimens. I explored different approaches for the creation of thin
cryo-lamellae by FIB milling and succeeded in optimizing the cryo-lift-out technique,
resulting in high-quality lamellae of approximately 200 nm thickness. \r\nHigh-resolution
Cryo-ET of these lamellae revealed for the first time the architecture of native
CDM in the context of matrix-secreting cells. This allowed for the in situ visualization
of fibrillar matrix proteins such as collagen, laying the foundation for future
structural and ultrastructural characterization of these proteins in their near-native
environment. \r\nIn summary, in this thesis, I present a novel workflow that combines
state-of-the-art cryo-EM specimen preparation and imaging technologies to permit
characterization of the ECM, an important tissue component in higher organisms.
This innovative and highly versatile workflow will enable addressing far-reaching
questions on ECM architecture, composition, and reciprocal ECM-cell interactions."
acknowledged_ssus:
- _id: EM-Fac
- _id: LifeSc
- _id: Bio
alternative_title:
- ISTA Thesis
article_processing_charge: No
author:
- first_name: Bettina
full_name: Zens, Bettina
id: 45FD126C-F248-11E8-B48F-1D18A9856A87
last_name: Zens
orcid: 0000-0002-9561-1239
citation:
ama: Zens B. Ultrastructural characterization of natively preserved extracellular
matrix by cryo-electron tomography. 2023. doi:10.15479/at:ista:12491
apa: Zens, B. (2023). Ultrastructural characterization of natively preserved
extracellular matrix by cryo-electron tomography. Institute of Science and
Technology Austria. https://doi.org/10.15479/at:ista:12491
chicago: Zens, Bettina. “Ultrastructural Characterization of Natively Preserved
Extracellular Matrix by Cryo-Electron Tomography.” Institute of Science and Technology
Austria, 2023. https://doi.org/10.15479/at:ista:12491.
ieee: B. Zens, “Ultrastructural characterization of natively preserved extracellular
matrix by cryo-electron tomography,” Institute of Science and Technology Austria,
2023.
ista: Zens B. 2023. Ultrastructural characterization of natively preserved extracellular
matrix by cryo-electron tomography. Institute of Science and Technology Austria.
mla: Zens, Bettina. Ultrastructural Characterization of Natively Preserved Extracellular
Matrix by Cryo-Electron Tomography. Institute of Science and Technology Austria,
2023, doi:10.15479/at:ista:12491.
short: B. Zens, Ultrastructural Characterization of Natively Preserved Extracellular
Matrix by Cryo-Electron Tomography, Institute of Science and Technology Austria,
2023.
corr_author: '1'
date_created: 2023-02-02T14:50:20Z
date_published: 2023-02-02T00:00:00Z
date_updated: 2026-04-07T13:49:23Z
day: '02'
ddc:
- '570'
degree_awarded: PhD
department:
- _id: GradSch
- _id: FlSc
doi: 10.15479/at:ista:12491
file:
- access_level: open_access
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content_type: application/pdf
creator: bzens
date_created: 2023-02-07T13:07:38Z
date_updated: 2024-02-08T23:30:04Z
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file_size: 106169509
relation: source_file
file_date_updated: 2024-02-08T23:30:04Z
has_accepted_license: '1'
keyword:
- cryo-EM
- cryo-ET
- FIB milling
- method development
- FIBSEM
- extracellular matrix
- ECM
- cell-derived matrices
- CDMs
- cell culture
- high pressure freezing
- HPF
- structural biology
- tomography
- collagen
language:
- iso: eng
month: '02'
oa: 1
oa_version: Published Version
page: '187'
project:
- _id: eba3b5f6-77a9-11ec-83b8-cf0905748aa3
name: Integrated visual proteomics of reciprocal cell-extracellular matrix interactions
- _id: 059B463C-7A3F-11EA-A408-12923DDC885E
name: "NÃ\x96-Fonds Preis für die Jungforscherin des Jahres am IST Austria"
publication_identifier:
isbn:
- 978-3-99078-027-5
issn:
- 2663-337X
publication_status: published
publisher: Institute of Science and Technology Austria
related_material:
record:
- id: '8586'
relation: part_of_dissertation
status: public
status: public
supervisor:
- first_name: Florian KM
full_name: Schur, Florian KM
id: 48AD8942-F248-11E8-B48F-1D18A9856A87
last_name: Schur
orcid: 0000-0003-4790-8078
title: Ultrastructural characterization of natively preserved extracellular matrix
by cryo-electron tomography
type: dissertation
user_id: ba8df636-2132-11f1-aed0-ed93e2281fdd
year: '2023'
...
---
_id: '11155'
abstract:
- lang: eng
text: The potential of energy filtering and direct electron detection for cryo-electron
microscopy (cryo-EM) has been well documented. Here, we assess the performance
of recently introduced hardware for cryo-electron tomography (cryo-ET) and subtomogram
averaging (STA), an increasingly popular structural determination method for complex
3D specimens. We acquired cryo-ET datasets of EIAV virus-like particles (VLPs)
on two contemporary cryo-EM systems equipped with different energy filters and
direct electron detectors (DED), specifically a Krios G4, equipped with a cold
field emission gun (CFEG), Thermo Fisher Scientific Selectris X energy filter,
and a Falcon 4 DED; and a Krios G3i, with a Schottky field emission gun (XFEG),
a Gatan Bioquantum energy filter, and a K3 DED. We performed constrained cross-correlation-based
STA on equally sized datasets acquired on the respective systems. The resulting
EIAV CA hexamer reconstructions show that both systems perform comparably in the
4–6 Å resolution range based on Fourier-Shell correlation (FSC). In addition,
by employing a recently introduced multiparticle refinement approach, we obtained
a reconstruction of the EIAV CA hexamer at 2.9 Å. Our results demonstrate the
potential of the new generation of energy filters and DEDs for STA, and the effects
of using different processing pipelines on their STA outcomes.
acknowledged_ssus:
- _id: LifeSc
- _id: ScienComp
- _id: EM-Fac
acknowledgement: This work was funded by the Austrian Science Fund (FWF) grant P31445
to F.K.M.S and the National Institute of Allergy and Infectious Diseases under awards
R01AI147890 to R.A.D. This research was also supported by the Scientific Service
Units (SSUs) of IST Austria through resources provided by Scientific Computing (SciComp),
the Life Science Facility (LSF), and the Electron Microscopy Facility (EMF). We
thank Dustin Morado for providing the software SubTOM for data processing. We also
thank William Wan for critical reading of the manuscript and valuable feedback.
article_number: '107852'
article_processing_charge: Yes (via OA deal)
article_type: original
author:
- first_name: Martin
full_name: Obr, Martin
id: 4741CA5A-F248-11E8-B48F-1D18A9856A87
last_name: Obr
orcid: 0000-0003-1756-6564
- first_name: Wim J.H.
full_name: Hagen, Wim J.H.
last_name: Hagen
- first_name: Robert A.
full_name: Dick, Robert A.
last_name: Dick
- first_name: Lingbo
full_name: Yu, Lingbo
last_name: Yu
- first_name: Abhay
full_name: Kotecha, Abhay
last_name: Kotecha
- first_name: Florian KM
full_name: Schur, Florian KM
id: 48AD8942-F248-11E8-B48F-1D18A9856A87
last_name: Schur
orcid: 0000-0003-4790-8078
citation:
ama: Obr M, Hagen WJH, Dick RA, Yu L, Kotecha A, Schur FK. Exploring high-resolution
cryo-ET and subtomogram averaging capabilities of contemporary DEDs. Journal
of Structural Biology. 2022;214(2). doi:10.1016/j.jsb.2022.107852
apa: Obr, M., Hagen, W. J. H., Dick, R. A., Yu, L., Kotecha, A., & Schur, F.
K. (2022). Exploring high-resolution cryo-ET and subtomogram averaging capabilities
of contemporary DEDs. Journal of Structural Biology. Elsevier. https://doi.org/10.1016/j.jsb.2022.107852
chicago: Obr, Martin, Wim J.H. Hagen, Robert A. Dick, Lingbo Yu, Abhay Kotecha,
and Florian KM Schur. “Exploring High-Resolution Cryo-ET and Subtomogram Averaging
Capabilities of Contemporary DEDs.” Journal of Structural Biology. Elsevier,
2022. https://doi.org/10.1016/j.jsb.2022.107852.
ieee: M. Obr, W. J. H. Hagen, R. A. Dick, L. Yu, A. Kotecha, and F. K. Schur, “Exploring
high-resolution cryo-ET and subtomogram averaging capabilities of contemporary
DEDs,” Journal of Structural Biology, vol. 214, no. 2. Elsevier, 2022.
ista: Obr M, Hagen WJH, Dick RA, Yu L, Kotecha A, Schur FK. 2022. Exploring high-resolution
cryo-ET and subtomogram averaging capabilities of contemporary DEDs. Journal of
Structural Biology. 214(2), 107852.
mla: Obr, Martin, et al. “Exploring High-Resolution Cryo-ET and Subtomogram Averaging
Capabilities of Contemporary DEDs.” Journal of Structural Biology, vol.
214, no. 2, 107852, Elsevier, 2022, doi:10.1016/j.jsb.2022.107852.
short: M. Obr, W.J.H. Hagen, R.A. Dick, L. Yu, A. Kotecha, F.K. Schur, Journal of
Structural Biology 214 (2022).
corr_author: '1'
date_created: 2022-04-15T07:10:26Z
date_published: 2022-06-01T00:00:00Z
date_updated: 2025-04-15T08:24:50Z
day: '01'
ddc:
- '570'
department:
- _id: FlSc
doi: 10.1016/j.jsb.2022.107852
external_id:
isi:
- '000790733600001'
pmid:
- '35351542'
file:
- access_level: open_access
checksum: 0b1eb53447aae8e95ae4c12d193b0b00
content_type: application/pdf
creator: dernst
date_created: 2022-08-02T11:07:58Z
date_updated: 2022-08-02T11:07:58Z
file_id: '11722'
file_name: 2022_JourStructuralBiology_Obr.pdf
file_size: 7080863
relation: main_file
success: 1
file_date_updated: 2022-08-02T11:07:58Z
has_accepted_license: '1'
intvolume: ' 214'
isi: 1
issue: '2'
keyword:
- Structural Biology
language:
- iso: eng
month: '06'
oa: 1
oa_version: Published Version
pmid: 1
project:
- _id: 26736D6A-B435-11E9-9278-68D0E5697425
call_identifier: FWF
grant_number: P31445
name: Structural conservation and diversity in retroviral capsid
publication: Journal of Structural Biology
publication_identifier:
issn:
- 1047-8477
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Exploring high-resolution cryo-ET and subtomogram averaging capabilities of
contemporary DEDs
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 214
year: '2022'
...
---
_id: '11351'
abstract:
- lang: eng
text: 'One hallmark of plant cells is their cell wall. They protect cells against
the environment and high turgor and mediate morphogenesis through the dynamics
of their mechanical and chemical properties. The walls are a complex polysaccharidic
structure. Although their biochemical composition is well known, how the different
components organize in the volume of the cell wall and interact with each other
is not well understood and yet is key to the wall’s mechanical properties. To
investigate the ultrastructure of the plant cell wall, we imaged the walls of
onion (Allium cepa) bulbs in a near-native state via cryo-focused ion beam milling
(cryo-FIB milling) and cryo-electron tomography (cryo-ET). This allowed the high-resolution
visualization of cellulose fibers in situ. We reveal the coexistence of dense
fiber fields bathed in a reticulated matrix we termed “meshing,” which is more
abundant at the inner surface of the cell wall. The fibers adopted a regular bimodal
angular distribution at all depths in the cell wall and bundled according to their
orientation, creating layers within the cell wall. Concomitantly, employing homogalacturonan
(HG)-specific enzymatic digestion, we observed changes in the meshing, suggesting
that it is—at least in part—composed of HG pectins. We propose the following model
for the construction of the abaxial epidermal primary cell wall: the cell deposits
successive layers of cellulose fibers at −45° and +45° relative to the cell’s
long axis and secretes the surrounding HG-rich meshing proximal to the plasma
membrane, which then migrates to more distal regions of the cell wall.'
acknowledgement: This work was supported by the Howard Hughes Medical Institute (HHMI)
and grant R35 GM122588 to G.J. and the Austrian Science Fund (FWF) P33367 to F.K.M.S.
We thank Noé Cochetel for his guidance and great help in data analysis, discovery,
and representation with the R software. We thank Hans-Ulrich Endress for graciously
providing us with the purified citrus pectin and Jozef Mravec for generating and
providing the COS488 probe. Cryo-EM work was done in the Beckman Institute Resource
Center for Transmission Electron Microscopy at Caltech. This article is subject
to HHMI’s Open Access to Publications policy. HHMI lab heads have previously granted
a nonexclusive CC BY 4.0 license to the public and a sublicensable license to HHMI
in their research articles. Pursuant to those licenses, the author accepted manuscript
of this article can be made freely available under a CC BY 4.0 license immediately
upon publication.
article_processing_charge: No
article_type: original
author:
- first_name: William J.
full_name: Nicolas, William J.
last_name: Nicolas
- first_name: Florian
full_name: Fäßler, Florian
id: 404F5528-F248-11E8-B48F-1D18A9856A87
last_name: Fäßler
orcid: 0000-0001-7149-769X
- first_name: Przemysław
full_name: Dutka, Przemysław
last_name: Dutka
- first_name: Florian KM
full_name: Schur, Florian KM
id: 48AD8942-F248-11E8-B48F-1D18A9856A87
last_name: Schur
orcid: 0000-0003-4790-8078
- first_name: Grant
full_name: Jensen, Grant
last_name: Jensen
- first_name: Elliot
full_name: Meyerowitz, Elliot
last_name: Meyerowitz
citation:
ama: Nicolas WJ, Fäßler F, Dutka P, Schur FK, Jensen G, Meyerowitz E. Cryo-electron
tomography of the onion cell wall shows bimodally oriented cellulose fibers and
reticulated homogalacturonan networks. Current Biology. 2022;32(11):P2375-2389.
doi:10.1016/j.cub.2022.04.024
apa: Nicolas, W. J., Fäßler, F., Dutka, P., Schur, F. K., Jensen, G., & Meyerowitz,
E. (2022). Cryo-electron tomography of the onion cell wall shows bimodally oriented
cellulose fibers and reticulated homogalacturonan networks. Current Biology.
Elsevier. https://doi.org/10.1016/j.cub.2022.04.024
chicago: Nicolas, William J., Florian Fäßler, Przemysław Dutka, Florian KM Schur,
Grant Jensen, and Elliot Meyerowitz. “Cryo-Electron Tomography of the Onion Cell
Wall Shows Bimodally Oriented Cellulose Fibers and Reticulated Homogalacturonan
Networks.” Current Biology. Elsevier, 2022. https://doi.org/10.1016/j.cub.2022.04.024.
ieee: W. J. Nicolas, F. Fäßler, P. Dutka, F. K. Schur, G. Jensen, and E. Meyerowitz,
“Cryo-electron tomography of the onion cell wall shows bimodally oriented cellulose
fibers and reticulated homogalacturonan networks,” Current Biology, vol.
32, no. 11. Elsevier, pp. P2375-2389, 2022.
ista: Nicolas WJ, Fäßler F, Dutka P, Schur FK, Jensen G, Meyerowitz E. 2022. Cryo-electron
tomography of the onion cell wall shows bimodally oriented cellulose fibers and
reticulated homogalacturonan networks. Current Biology. 32(11), P2375-2389.
mla: Nicolas, William J., et al. “Cryo-Electron Tomography of the Onion Cell Wall
Shows Bimodally Oriented Cellulose Fibers and Reticulated Homogalacturonan Networks.”
Current Biology, vol. 32, no. 11, Elsevier, 2022, pp. P2375-2389, doi:10.1016/j.cub.2022.04.024.
short: W.J. Nicolas, F. Fäßler, P. Dutka, F.K. Schur, G. Jensen, E. Meyerowitz,
Current Biology 32 (2022) P2375-2389.
date_created: 2022-05-04T06:22:06Z
date_published: 2022-06-06T00:00:00Z
date_updated: 2025-04-15T08:25:40Z
day: '06'
ddc:
- '570'
department:
- _id: FlSc
doi: 10.1016/j.cub.2022.04.024
external_id:
isi:
- '000822399200019'
pmid:
- '35508170'
file:
- access_level: open_access
checksum: af3f24d97c016d844df237abef987639
content_type: application/pdf
creator: dernst
date_created: 2022-08-05T06:29:18Z
date_updated: 2022-08-05T06:29:18Z
file_id: '11730'
file_name: 2022_CurrentBiology_Nicolas.pdf
file_size: 12827717
relation: main_file
success: 1
file_date_updated: 2022-08-05T06:29:18Z
has_accepted_license: '1'
intvolume: ' 32'
isi: 1
issue: '11'
keyword:
- General Agricultural and Biological Sciences
- General Biochemistry
- Genetics and Molecular Biology
language:
- iso: eng
month: '06'
oa: 1
oa_version: Published Version
page: P2375-2389
pmid: 1
project:
- _id: 9B954C5C-BA93-11EA-9121-9846C619BF3A
grant_number: P33367
name: Structure and isoform diversity of the Arp2/3 complex
publication: Current Biology
publication_identifier:
issn:
- 0960-9822
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Cryo-electron tomography of the onion cell wall shows bimodally oriented cellulose
fibers and reticulated homogalacturonan networks
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 32
year: '2022'
...
---
_id: '10639'
abstract:
- lang: eng
text: With more than 80 members worldwide, the Orthobunyavirus genus in the Peribunyaviridae
family is a large genus of enveloped RNA viruses, many of which are emerging pathogens
in humans and livestock. How orthobunyaviruses (OBVs) penetrate and infect mammalian
host cells remains poorly characterized. Here, we investigated the entry mechanisms
of the OBV Germiston (GERV). Viral particles were visualized by cryo-electron
microscopy and appeared roughly spherical with an average diameter of 98 nm. Labeling
of the virus with fluorescent dyes did not adversely affect its infectivity and
allowed the monitoring of single particles in fixed and live cells. Using this
approach, we found that endocytic internalization of bound viruses was asynchronous
and occurred within 30-40 min. The virus entered Rab5a+ early endosomes and, subsequently,
late endosomal vacuoles containing Rab7a but not LAMP-1. Infectious entry did
not require proteolytic cleavage, and endosomal acidification was sufficient and
necessary for viral fusion. Acid-activated penetration began 15-25 min after initiation
of virus internalization and relied on maturation of early endosomes to late endosomes.
The optimal pH for viral membrane fusion was slightly below 6.0, and penetration
was hampered when the potassium influx was abolished. Overall, our study provides
real-time visualization of GERV entry into host cells and demonstrates the importance
of late endosomal maturation in facilitating OBV penetration.
acknowledged_ssus:
- _id: EM-Fac
acknowledgement: This work was supported by INRAE starter funds, Project IDEXLYON (University of Lyon)
within the Programme Investissements d’Avenir (ANR-16-IDEX-0005), and FINOVIAO14
(Fondation pour l’Université de Lyon), all to P.Y.L. This work was also supported by
CellNetworks Research Group funds and Deutsche Forschungsgemeinschaft (DFG) funding
(grant numbers LO-2338/1-1 and LO-2338/3-1) awarded to P.Y.L., Austrian Science Fund
(FWF) grant P31445 to F.K.M.S., a Chinese Scholarship Council (CSC;no. 201904910701)
fellowship to Q.X., and a ministére de l’enseignement supérieur, de la recherche et de
l’innovation (MESRI) doctoral thesis grant to M.D.
article_number: e02146-21
article_processing_charge: No
article_type: original
author:
- first_name: Stefan
full_name: Windhaber, Stefan
last_name: Windhaber
- first_name: Qilin
full_name: Xin, Qilin
last_name: Xin
- first_name: Zina M.
full_name: Uckeley, Zina M.
last_name: Uckeley
- first_name: Jana
full_name: Koch, Jana
last_name: Koch
- first_name: Martin
full_name: Obr, Martin
id: 4741CA5A-F248-11E8-B48F-1D18A9856A87
last_name: Obr
orcid: 0000-0003-1756-6564
- first_name: Céline
full_name: Garnier, Céline
last_name: Garnier
- first_name: Catherine
full_name: Luengo-Guyonnot, Catherine
last_name: Luengo-Guyonnot
- first_name: Maëva
full_name: Duboeuf, Maëva
last_name: Duboeuf
- first_name: Florian KM
full_name: Schur, Florian KM
id: 48AD8942-F248-11E8-B48F-1D18A9856A87
last_name: Schur
orcid: 0000-0003-4790-8078
- first_name: Pierre-Yves
full_name: Lozach, Pierre-Yves
last_name: Lozach
citation:
ama: Windhaber S, Xin Q, Uckeley ZM, et al. The Orthobunyavirus Germiston enters
host cells from late endosomes. Journal of Virology. 2022;96(5). doi:10.1128/jvi.02146-21
apa: Windhaber, S., Xin, Q., Uckeley, Z. M., Koch, J., Obr, M., Garnier, C., … Lozach,
P.-Y. (2022). The Orthobunyavirus Germiston enters host cells from late endosomes.
Journal of Virology. American Society for Microbiology. https://doi.org/10.1128/jvi.02146-21
chicago: Windhaber, Stefan, Qilin Xin, Zina M. Uckeley, Jana Koch, Martin Obr, Céline
Garnier, Catherine Luengo-Guyonnot, Maëva Duboeuf, Florian KM Schur, and Pierre-Yves
Lozach. “The Orthobunyavirus Germiston Enters Host Cells from Late Endosomes.”
Journal of Virology. American Society for Microbiology, 2022. https://doi.org/10.1128/jvi.02146-21.
ieee: S. Windhaber et al., “The Orthobunyavirus Germiston enters host cells
from late endosomes,” Journal of Virology, vol. 96, no. 5. American Society
for Microbiology, 2022.
ista: Windhaber S, Xin Q, Uckeley ZM, Koch J, Obr M, Garnier C, Luengo-Guyonnot
C, Duboeuf M, Schur FK, Lozach P-Y. 2022. The Orthobunyavirus Germiston enters
host cells from late endosomes. Journal of Virology. 96(5), e02146-21.
mla: Windhaber, Stefan, et al. “The Orthobunyavirus Germiston Enters Host Cells
from Late Endosomes.” Journal of Virology, vol. 96, no. 5, e02146-21, American
Society for Microbiology, 2022, doi:10.1128/jvi.02146-21.
short: S. Windhaber, Q. Xin, Z.M. Uckeley, J. Koch, M. Obr, C. Garnier, C. Luengo-Guyonnot,
M. Duboeuf, F.K. Schur, P.-Y. Lozach, Journal of Virology 96 (2022).
date_created: 2022-01-18T10:04:18Z
date_published: 2022-03-01T00:00:00Z
date_updated: 2026-06-18T08:44:25Z
day: '01'
ddc:
- '570'
department:
- _id: FlSc
doi: 10.1128/jvi.02146-21
external_id:
isi:
- '000779305000033'
pmid:
- '35019710'
intvolume: ' 96'
isi: 1
issue: '5'
keyword:
- virology
- insect science
- immunology
- microbiology
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8906410
month: '03'
oa: 1
oa_version: Published Version
pmid: 1
project:
- _id: 26736D6A-B435-11E9-9278-68D0E5697425
call_identifier: FWF
grant_number: P31445
name: Structural conservation and diversity in retroviral capsid
publication: Journal of Virology
publication_identifier:
eissn:
- 1098-5514
issn:
- 0022-538X
publication_status: published
publisher: American Society for Microbiology
quality_controlled: '1'
scopus_import: '1'
status: public
title: The Orthobunyavirus Germiston enters host cells from late endosomes
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 96
year: '2022'
...
---
_id: '15283'
article_processing_charge: No
article_type: original
author:
- first_name: William
full_name: Nicolas, William
last_name: Nicolas
- first_name: Florian
full_name: Fäßler, Florian
id: 404F5528-F248-11E8-B48F-1D18A9856A87
last_name: Fäßler
orcid: 0000-0001-7149-769X
- first_name: Elliot
full_name: Meyerowitz, Elliot
last_name: Meyerowitz
- first_name: Grant
full_name: Jensen, Grant
last_name: Jensen
citation:
ama: Nicolas W, Fäßler F, Meyerowitz E, Jensen G. Peaking into the plant cell wall
using cryo-FIB milling and electron cryo-tomography. Microscopy and Microanalysis.
2021;27(S1):3024-3026. doi:10.1017/s1431927621010503
apa: Nicolas, W., Fäßler, F., Meyerowitz, E., & Jensen, G. (2021). Peaking into
the plant cell wall using cryo-FIB milling and electron cryo-tomography. Microscopy
and Microanalysis. Oxford University Press. https://doi.org/10.1017/s1431927621010503
chicago: Nicolas, William, Florian Fäßler, Elliot Meyerowitz, and Grant Jensen.
“Peaking into the Plant Cell Wall Using Cryo-FIB Milling and Electron Cryo-Tomography.”
Microscopy and Microanalysis. Oxford University Press, 2021. https://doi.org/10.1017/s1431927621010503.
ieee: W. Nicolas, F. Fäßler, E. Meyerowitz, and G. Jensen, “Peaking into the plant
cell wall using cryo-FIB milling and electron cryo-tomography,” Microscopy
and Microanalysis, vol. 27, no. S1. Oxford University Press, pp. 3024–3026,
2021.
ista: Nicolas W, Fäßler F, Meyerowitz E, Jensen G. 2021. Peaking into the plant
cell wall using cryo-FIB milling and electron cryo-tomography. Microscopy and
Microanalysis. 27(S1), 3024–3026.
mla: Nicolas, William, et al. “Peaking into the Plant Cell Wall Using Cryo-FIB Milling
and Electron Cryo-Tomography.” Microscopy and Microanalysis, vol. 27, no.
S1, Oxford University Press, 2021, pp. 3024–26, doi:10.1017/s1431927621010503.
short: W. Nicolas, F. Fäßler, E. Meyerowitz, G. Jensen, Microscopy and Microanalysis
27 (2021) 3024–3026.
date_created: 2024-04-03T08:57:23Z
date_published: 2021-08-01T00:00:00Z
date_updated: 2024-04-09T07:55:56Z
day: '01'
department:
- _id: FlSc
doi: 10.1017/s1431927621010503
intvolume: ' 27'
issue: S1
keyword:
- Instrumentation
language:
- iso: eng
month: '08'
oa_version: None
page: 3024-3026
publication: Microscopy and Microanalysis
publication_identifier:
eissn:
- 1435-8115
issn:
- 1431-9276
publication_status: published
publisher: Oxford University Press
quality_controlled: '1'
status: public
title: Peaking into the plant cell wall using cryo-FIB milling and electron cryo-tomography
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 27
year: '2021'
...