---
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'
...
---
_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: 2025-04-15T08:24:49Z
day: '01'
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: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 96
year: '2022'
...
---
_id: '15270'
abstract:
- lang: eng
text: Various toxic compounds disrupt bacterial physiology. While bacteria harbor
defense mechanisms to mitigate the toxicity, these mechanisms are often coupled
to the physiological state of the cells and become ineffective when the physiology
is severely disrupted.
article_number: '676'
article_processing_charge: Yes
article_type: original
author:
- first_name: Dai
full_name: Le, Dai
last_name: Le
- first_name: Ekaterina
full_name: Krasnopeeva, Ekaterina
id: 1F1EE44A-BF83-11EA-B3C1-BB9CC619BF3A
last_name: Krasnopeeva
- first_name: Faris
full_name: Sinjab, Faris
last_name: Sinjab
- first_name: Teuta
full_name: Pilizota, Teuta
last_name: Pilizota
- first_name: Minsu
full_name: Kim, Minsu
last_name: Kim
citation:
ama: Le D, Krasnopeeva E, Sinjab F, Pilizota T, Kim M. Active efflux leads to heterogeneous
dissipation of proton motive force by protonophores in bacteria. mBio.
2021;12(4). doi:10.1128/mbio.00676-21
apa: Le, D., Krasnopeeva, E., Sinjab, F., Pilizota, T., & Kim, M. (2021). Active
efflux leads to heterogeneous dissipation of proton motive force by protonophores
in bacteria. MBio. American Society for Microbiology. https://doi.org/10.1128/mbio.00676-21
chicago: Le, Dai, Ekaterina Krasnopeeva, Faris Sinjab, Teuta Pilizota, and Minsu
Kim. “Active Efflux Leads to Heterogeneous Dissipation of Proton Motive Force
by Protonophores in Bacteria.” MBio. American Society for Microbiology,
2021. https://doi.org/10.1128/mbio.00676-21.
ieee: D. Le, E. Krasnopeeva, F. Sinjab, T. Pilizota, and M. Kim, “Active efflux
leads to heterogeneous dissipation of proton motive force by protonophores in
bacteria,” mBio, vol. 12, no. 4. American Society for Microbiology, 2021.
ista: Le D, Krasnopeeva E, Sinjab F, Pilizota T, Kim M. 2021. Active efflux leads
to heterogeneous dissipation of proton motive force by protonophores in bacteria.
mBio. 12(4), 676.
mla: Le, Dai, et al. “Active Efflux Leads to Heterogeneous Dissipation of Proton
Motive Force by Protonophores in Bacteria.” MBio, vol. 12, no. 4, 676,
American Society for Microbiology, 2021, doi:10.1128/mbio.00676-21.
short: D. Le, E. Krasnopeeva, F. Sinjab, T. Pilizota, M. Kim, MBio 12 (2021).
date_created: 2024-04-03T07:51:57Z
date_published: 2021-08-31T00:00:00Z
date_updated: 2024-04-10T09:13:59Z
day: '31'
ddc:
- '570'
department:
- _id: CaGu
doi: 10.1128/mbio.00676-21
external_id:
pmid:
- '34253054'
file:
- access_level: open_access
checksum: 529e3f97ae5c5f5cc743c4fc130c9440
content_type: application/pdf
creator: dernst
date_created: 2024-04-10T09:05:49Z
date_updated: 2024-04-10T09:05:49Z
file_id: '15309'
file_name: 2021_mBio_Le.pdf
file_size: 1344204
relation: main_file
success: 1
file_date_updated: 2024-04-10T09:05:49Z
has_accepted_license: '1'
intvolume: ' 12'
issue: '4'
keyword:
- Virology
- Microbiology
language:
- iso: eng
month: '08'
oa: 1
oa_version: Published Version
pmid: 1
publication: mBio
publication_identifier:
issn:
- 2150-7511
publication_status: published
publisher: American Society for Microbiology
quality_controlled: '1'
status: public
title: Active efflux leads to heterogeneous dissipation of proton motive force by
protonophores in bacteria
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: 12
year: '2021'
...
---
_id: '15274'
abstract:
- lang: eng
text: Copper (Cu) is a redox-active micronutrient that is both essential and toxic.
Its cellular homeostasis is critical for supporting cuproprotein maturation while
avoiding excessive oxidative stress. The Cu importer CcoA is the prototype of
the widespread CalT subfamily of the MFS-type transporters. Hence, understanding
its molecular mechanism of function is significant. Here, we show that CcoA undergoes
a thiol:disulfide oxidoreduction cycle, which is important for its Cu import activity.
article_number: e01567
article_processing_charge: No
article_type: original
author:
- first_name: Bahia
full_name: Khalfaoui-Hassani, Bahia
last_name: Khalfaoui-Hassani
- first_name: Petru Iulian
full_name: Trasnea, Petru Iulian
id: D560034C-10C4-11EA-ABF4-A4B43DDC885E
last_name: Trasnea
- first_name: Stefan
full_name: Steimle, Stefan
last_name: Steimle
- first_name: Hans-Georg
full_name: Koch, Hans-Georg
last_name: Koch
- first_name: Fevzi
full_name: Daldal, Fevzi
last_name: Daldal
citation:
ama: Khalfaoui-Hassani B, Trasnea PI, Steimle S, Koch H-G, Daldal F. Cysteine mutants
of the major facilitator superfamily-type transporter CcoA provide insight into
copper import. mBio. 2021;12(4). doi:10.1128/mbio.01567-21
apa: Khalfaoui-Hassani, B., Trasnea, P. I., Steimle, S., Koch, H.-G., & Daldal,
F. (2021). Cysteine mutants of the major facilitator superfamily-type transporter
CcoA provide insight into copper import. MBio. American Society for Microbiology.
https://doi.org/10.1128/mbio.01567-21
chicago: Khalfaoui-Hassani, Bahia, Petru Iulian Trasnea, Stefan Steimle, Hans-Georg
Koch, and Fevzi Daldal. “Cysteine Mutants of the Major Facilitator Superfamily-Type
Transporter CcoA Provide Insight into Copper Import.” MBio. American Society
for Microbiology, 2021. https://doi.org/10.1128/mbio.01567-21.
ieee: B. Khalfaoui-Hassani, P. I. Trasnea, S. Steimle, H.-G. Koch, and F. Daldal,
“Cysteine mutants of the major facilitator superfamily-type transporter CcoA provide
insight into copper import,” mBio, vol. 12, no. 4. American Society for
Microbiology, 2021.
ista: Khalfaoui-Hassani B, Trasnea PI, Steimle S, Koch H-G, Daldal F. 2021. Cysteine
mutants of the major facilitator superfamily-type transporter CcoA provide insight
into copper import. mBio. 12(4), e01567.
mla: Khalfaoui-Hassani, Bahia, et al. “Cysteine Mutants of the Major Facilitator
Superfamily-Type Transporter CcoA Provide Insight into Copper Import.” MBio,
vol. 12, no. 4, e01567, American Society for Microbiology, 2021, doi:10.1128/mbio.01567-21.
short: B. Khalfaoui-Hassani, P.I. Trasnea, S. Steimle, H.-G. Koch, F. Daldal, MBio
12 (2021).
date_created: 2024-04-03T07:59:04Z
date_published: 2021-08-31T00:00:00Z
date_updated: 2024-04-09T10:47:16Z
day: '31'
ddc:
- '570'
department:
- _id: LeSa
doi: 10.1128/mbio.01567-21
external_id:
pmid:
- '34281385'
file:
- access_level: open_access
checksum: 2f6a57637cb3162eaeeb155a5b031e76
content_type: application/pdf
creator: dernst
date_created: 2024-04-09T10:45:11Z
date_updated: 2024-04-09T10:45:11Z
file_id: '15306'
file_name: 2021_mBio_KhalfaouiHassani.pdf
file_size: 3383398
relation: main_file
success: 1
file_date_updated: 2024-04-09T10:45:11Z
has_accepted_license: '1'
intvolume: ' 12'
issue: '4'
keyword:
- Virology
- Microbiology
language:
- iso: eng
month: '08'
oa: 1
oa_version: Published Version
pmid: 1
publication: mBio
publication_identifier:
issn:
- 2150-7511
publication_status: published
publisher: American Society for Microbiology
quality_controlled: '1'
status: public
title: Cysteine mutants of the major facilitator superfamily-type transporter CcoA
provide insight into copper import
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: 12
year: '2021'
...
---
_id: '15276'
abstract:
- lang: eng
text: Biotrophic plant pathogens secrete effector proteins to manipulate the host
physiology. Effectors suppress defenses and induce an environment favorable to
disease development. Sequence-based prediction of effector function is impeded
by their rapid evolution rate. In the maize pathogen Ustilago maydis,
effector-coding genes frequently organize in clusters. Here we describe the functional
characterization of the pleiades, a cluster of ten
effector genes, by analyzing the micro- and macroscopic phenotype of the cluster
deletion and expressing these proteins in planta. Deletion
of the pleiades leads to strongly impaired virulence
and accumulation of reactive oxygen species (ROS) in infected tissue. Eight of
the Pleiades suppress the production of ROS upon perception of pathogen associated
molecular patterns (PAMPs). Although functionally redundant, the Pleiades target
different host components. The paralogs Taygeta1 and Merope1 suppress ROS production
in either the cytoplasm or nucleus, respectively. Merope1 targets and promotes
the auto-ubiquitination activity of RFI2, a conserved family of E3 ligases that
regulates the production of PAMP-triggered ROS burst in plants.
article_number: e1009641
article_processing_charge: Yes
article_type: original
author:
- first_name: Fernando
full_name: Navarrete, Fernando
last_name: Navarrete
- first_name: Nenad
full_name: Grujic, Nenad
last_name: Grujic
- first_name: Alexandra
full_name: Stirnberg, Alexandra
last_name: Stirnberg
- first_name: Indira
full_name: Saado, Indira
last_name: Saado
- first_name: David
full_name: Aleksza, David
last_name: Aleksza
- first_name: Michelle C
full_name: Gallei, Michelle C
id: 35A03822-F248-11E8-B48F-1D18A9856A87
last_name: Gallei
orcid: 0000-0003-1286-7368
- first_name: Hazem
full_name: Adi, Hazem
last_name: Adi
- first_name: André
full_name: Alcântara, André
last_name: Alcântara
- first_name: Mamoona
full_name: Khan, Mamoona
last_name: Khan
- first_name: Janos
full_name: Bindics, Janos
last_name: Bindics
- first_name: Marco
full_name: Trujillo, Marco
last_name: Trujillo
- first_name: Armin
full_name: Djamei, Armin
last_name: Djamei
citation:
ama: Navarrete F, Grujic N, Stirnberg A, et al. The Pleiades are a cluster of fungal
effectors that inhibit host defenses. PLOS Pathogens. 2021;17(6). doi:10.1371/journal.ppat.1009641
apa: Navarrete, F., Grujic, N., Stirnberg, A., Saado, I., Aleksza, D., Gallei, M.
C., … Djamei, A. (2021). The Pleiades are a cluster of fungal effectors that inhibit
host defenses. PLOS Pathogens. Public Library of Science. https://doi.org/10.1371/journal.ppat.1009641
chicago: Navarrete, Fernando, Nenad Grujic, Alexandra Stirnberg, Indira Saado, David
Aleksza, Michelle C Gallei, Hazem Adi, et al. “The Pleiades Are a Cluster of Fungal
Effectors That Inhibit Host Defenses.” PLOS Pathogens. Public Library of
Science, 2021. https://doi.org/10.1371/journal.ppat.1009641.
ieee: F. Navarrete et al., “The Pleiades are a cluster of fungal effectors
that inhibit host defenses,” PLOS Pathogens, vol. 17, no. 6. Public Library
of Science, 2021.
ista: Navarrete F, Grujic N, Stirnberg A, Saado I, Aleksza D, Gallei MC, Adi H,
Alcântara A, Khan M, Bindics J, Trujillo M, Djamei A. 2021. The Pleiades are a
cluster of fungal effectors that inhibit host defenses. PLOS Pathogens. 17(6),
e1009641.
mla: Navarrete, Fernando, et al. “The Pleiades Are a Cluster of Fungal Effectors
That Inhibit Host Defenses.” PLOS Pathogens, vol. 17, no. 6, e1009641,
Public Library of Science, 2021, doi:10.1371/journal.ppat.1009641.
short: F. Navarrete, N. Grujic, A. Stirnberg, I. Saado, D. Aleksza, M.C. Gallei,
H. Adi, A. Alcântara, M. Khan, J. Bindics, M. Trujillo, A. Djamei, PLOS Pathogens
17 (2021).
date_created: 2024-04-03T08:00:34Z
date_published: 2021-06-24T00:00:00Z
date_updated: 2024-04-09T10:26:12Z
day: '24'
ddc:
- '580'
department:
- _id: JiFr
doi: 10.1371/journal.ppat.1009641
external_id:
pmid:
- '34166468'
file:
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checksum: ab8428291a0c14607c4ea5656c029cff
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date_updated: 2024-04-09T10:24:43Z
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file_size: 2616563
relation: main_file
success: 1
file_date_updated: 2024-04-09T10:24:43Z
has_accepted_license: '1'
intvolume: ' 17'
issue: '6'
keyword:
- Virology
- Genetics
- Molecular Biology
- Immunology
- Microbiology
- Parasitology
language:
- iso: eng
month: '06'
oa: 1
oa_version: Published Version
pmid: 1
publication: PLOS Pathogens
publication_identifier:
issn:
- 1553-7374
publication_status: published
publisher: Public Library of Science
quality_controlled: '1'
status: public
title: The Pleiades are a cluster of fungal effectors that inhibit host defenses
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: 17
year: '2021'
...
---
_id: '10103'
abstract:
- lang: eng
text: The small cellular molecule inositol hexakisphosphate (IP6) has been known
for ~20 years to promote the in vitro assembly of HIV-1 into immature virus-like
particles. However, the molecular details underlying this effect have been determined
only recently, with the identification of the IP6 binding site in the immature
Gag lattice. IP6 also promotes formation of the mature capsid protein (CA) lattice
via a second IP6 binding site, and enhances core stability, creating a favorable
environment for reverse transcription. IP6 also enhances assembly of other retroviruses,
from both the Lentivirus and the Alpharetrovirus genera. These findings suggest
that IP6 may have a conserved function throughout the family Retroviridae. Here,
we discuss the different steps in the viral life cycle that are influenced by
IP6, and describe in detail how IP6 interacts with the immature and mature lattices
of different retroviruses.
acknowledgement: We thank Volker M. Vogt for his critical comments in preparation
of the review.
article_number: '1853'
article_processing_charge: Yes
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: Florian KM
full_name: Schur, Florian KM
id: 48AD8942-F248-11E8-B48F-1D18A9856A87
last_name: Schur
orcid: 0000-0003-4790-8078
- first_name: Robert A.
full_name: Dick, Robert A.
last_name: Dick
citation:
ama: Obr M, Schur FK, Dick RA. A structural perspective of the role of IP6 in immature
and mature retroviral assembly. Viruses. 2021;13(9). doi:10.3390/v13091853
apa: Obr, M., Schur, F. K., & Dick, R. A. (2021). A structural perspective of
the role of IP6 in immature and mature retroviral assembly. Viruses. MDPI.
https://doi.org/10.3390/v13091853
chicago: Obr, Martin, Florian KM Schur, and Robert A. Dick. “A Structural Perspective
of the Role of IP6 in Immature and Mature Retroviral Assembly.” Viruses.
MDPI, 2021. https://doi.org/10.3390/v13091853.
ieee: M. Obr, F. K. Schur, and R. A. Dick, “A structural perspective of the role
of IP6 in immature and mature retroviral assembly,” Viruses, vol. 13, no.
9. MDPI, 2021.
ista: Obr M, Schur FK, Dick RA. 2021. A structural perspective of the role of IP6
in immature and mature retroviral assembly. Viruses. 13(9), 1853.
mla: Obr, Martin, et al. “A Structural Perspective of the Role of IP6 in Immature
and Mature Retroviral Assembly.” Viruses, vol. 13, no. 9, 1853, MDPI, 2021,
doi:10.3390/v13091853.
short: M. Obr, F.K. Schur, R.A. Dick, Viruses 13 (2021).
corr_author: '1'
date_created: 2021-10-07T09:13:29Z
date_published: 2021-09-17T00:00:00Z
date_updated: 2025-04-15T08:24:49Z
day: '17'
ddc:
- '616'
department:
- _id: FlSc
doi: 10.3390/v13091853
external_id:
isi:
- '000699841100001'
pmid:
- '34578434'
file:
- access_level: open_access
checksum: bcfd72a12977d48e22df3d0cc55aacf1
content_type: application/pdf
creator: cchlebak
date_created: 2021-10-08T10:38:15Z
date_updated: 2021-10-08T10:38:15Z
file_id: '10115'
file_name: 2021_Viruses_Obr.pdf
file_size: 4146796
relation: main_file
success: 1
file_date_updated: 2021-10-08T10:38:15Z
has_accepted_license: '1'
intvolume: ' 13'
isi: 1
issue: '9'
keyword:
- virology
- infectious diseases
language:
- iso: eng
month: '09'
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: Viruses
publication_identifier:
issn:
- 1999-4915
publication_status: published
publisher: MDPI
quality_controlled: '1'
scopus_import: '1'
status: public
title: A structural perspective of the role of IP6 in immature and mature retroviral
assembly
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: 13
year: '2021'
...