---
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. <i>Nature Structural &#38;
    Molecular Biology</i>. 2025;32:268-276. doi:<a href="https://doi.org/10.1038/s41594-024-01390-8">10.1038/s41594-024-01390-8</a>
  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. <i>Nature Structural &#38; Molecular Biology</i>.
    Springer Nature. <a href="https://doi.org/10.1038/s41594-024-01390-8">https://doi.org/10.1038/s41594-024-01390-8</a>
  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.” <i>Nature Structural &#38; Molecular Biology</i>.
    Springer Nature, 2025. <a href="https://doi.org/10.1038/s41594-024-01390-8">https://doi.org/10.1038/s41594-024-01390-8</a>.
  ieee: M. Obr <i>et al.</i>, “Distinct stabilization of the human T cell leukemia
    virus type 1 immature Gag lattice,” <i>Nature Structural &#38; Molecular Biology</i>,
    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 &#38; Molecular
    Biology. 32, 268–276.
  mla: Obr, Martin, et al. “Distinct Stabilization of the Human T Cell Leukemia Virus
    Type 1 Immature Gag Lattice.” <i>Nature Structural &#38; Molecular Biology</i>,
    vol. 32, Springer Nature, 2025, pp. 268–76, doi:<a href="https://doi.org/10.1038/s41594-024-01390-8">10.1038/s41594-024-01390-8</a>.
  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 &#38; 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
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  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. <i>Nature Structural
    &#38; Molecular Biology</i>. 2024;31:1114-1123. doi:<a href="https://doi.org/10.1038/s41594-023-01201-6">10.1038/s41594-023-01201-6</a>
  apa: Datler, J., Hansen, J., Thader, A., Schlögl, A., Bauer, L. W., Hodirnau, V.-V.,
    &#38; Schur, F. K. (2024). Multi-modal cryo-EM reveals trimers of protein A10
    to form the palisade layer in poxvirus cores. <i>Nature Structural &#38; Molecular
    Biology</i>. Springer Nature. <a href="https://doi.org/10.1038/s41594-023-01201-6">https://doi.org/10.1038/s41594-023-01201-6</a>
  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.” <i>Nature Structural
    &#38; Molecular Biology</i>. Springer Nature, 2024. <a href="https://doi.org/10.1038/s41594-023-01201-6">https://doi.org/10.1038/s41594-023-01201-6</a>.
  ieee: J. Datler <i>et al.</i>, “Multi-modal cryo-EM reveals trimers of protein A10
    to form the palisade layer in poxvirus cores,” <i>Nature Structural &#38; Molecular
    Biology</i>, 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 &#38; 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.” <i>Nature Structural &#38; Molecular
    Biology</i>, vol. 31, Springer Nature, 2024, pp. 1114–23, doi:<a href="https://doi.org/10.1038/s41594-023-01201-6">10.1038/s41594-023-01201-6</a>.
  short: J. Datler, J. Hansen, A. Thader, A. Schlögl, L.W. Bauer, V.-V. Hodirnau,
    F.K. Schur, Nature Structural &#38; 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:
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  checksum: bda7bf65d81455480efaed8ca293b0db
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  creator: dernst
  date_created: 2024-07-22T11:27:22Z
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  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: '9431'
abstract:
- lang: eng
  text: Inositol hexakisphosphate (IP6) is an assembly cofactor for HIV-1. We report
    here that IP6 is also used for assembly of Rous sarcoma virus (RSV), a retrovirus
    from a different genus. IP6 is ~100-fold more potent at promoting RSV mature capsid
    protein (CA) assembly than observed for HIV-1 and removal of IP6 in cells reduces
    infectivity by 100-fold. Here, visualized by cryo-electron tomography and subtomogram
    averaging, mature capsid-like particles show an IP6-like density in the CA hexamer,
    coordinated by rings of six lysines and six arginines. Phosphate and IP6 have
    opposing effects on CA in vitro assembly, inducing formation of T = 1 icosahedrons
    and tubes, respectively, implying that phosphate promotes pentamer and IP6 hexamer
    formation. Subtomogram averaging and classification optimized for analysis of
    pleomorphic retrovirus particles reveal that the heterogeneity of mature RSV CA
    polyhedrons results from an unexpected, intrinsic CA hexamer flexibility. In contrast,
    the CA pentamer forms rigid units organizing the local architecture. These different
    features of hexamers and pentamers determine the structural mechanism to form
    CA polyhedrons of variable shape in mature RSV particles.
acknowledged_ssus:
- _id: ScienComp
- _id: LifeSc
- _id: EM-Fac
acknowledgement: This work was funded by the National Institute of Allergy and Infectious
  Diseases under awards R01AI147890 to R.A.D., R01AI150454 to V.M.V, R35GM136258 in
  support of J-P.R.F, and the Austrian Science Fund (FWF) grant P31445 to F.K.M.S.
  Access to high-resolution cryo-ET data acquisition at EMBL Heidelberg was supported
  by iNEXT (grant no. 653706), funded by the Horizon 2020 program of the European
  Union (PID 4246). We thank Wim Hagen and Felix Weis at EMBL Heidelberg for support
  in cryo-ET data acquisition. This work made use of the Cornell Center for Materials
  Research Shared Facilities, which are supported through the NSF MRSEC program (DMR-179875).
  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).
article_number: '3226'
article_processing_charge: No
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: Clifton L.
  full_name: Ricana, Clifton L.
  last_name: Ricana
- first_name: Nadia
  full_name: Nikulin, Nadia
  last_name: Nikulin
- first_name: Jon-Philip R.
  full_name: Feathers, Jon-Philip R.
  last_name: Feathers
- first_name: Marco
  full_name: Klanschnig, Marco
  last_name: Klanschnig
- first_name: Andreas
  full_name: Thader, Andreas
  id: 3A18A7B8-F248-11E8-B48F-1D18A9856A87
  last_name: Thader
- first_name: Marc C.
  full_name: Johnson, Marc C.
  last_name: Johnson
- first_name: Volker M.
  full_name: Vogt, Volker M.
  last_name: Vogt
- 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, Ricana CL, Nikulin N, et al. Structure of the mature Rous sarcoma virus
    lattice reveals a role for IP6 in the formation of the capsid hexamer. <i>Nature
    Communications</i>. 2021;12(1). doi:<a href="https://doi.org/10.1038/s41467-021-23506-0">10.1038/s41467-021-23506-0</a>
  apa: Obr, M., Ricana, C. L., Nikulin, N., Feathers, J.-P. R., Klanschnig, M., Thader,
    A., … Dick, R. A. (2021). Structure of the mature Rous sarcoma virus lattice reveals
    a role for IP6 in the formation of the capsid hexamer. <i>Nature Communications</i>.
    Nature Research. <a href="https://doi.org/10.1038/s41467-021-23506-0">https://doi.org/10.1038/s41467-021-23506-0</a>
  chicago: Obr, Martin, Clifton L. Ricana, Nadia Nikulin, Jon-Philip R. Feathers,
    Marco Klanschnig, Andreas Thader, Marc C. Johnson, Volker M. Vogt, Florian KM
    Schur, and Robert A. Dick. “Structure of the Mature Rous Sarcoma Virus Lattice
    Reveals a Role for IP6 in the Formation of the Capsid Hexamer.” <i>Nature Communications</i>.
    Nature Research, 2021. <a href="https://doi.org/10.1038/s41467-021-23506-0">https://doi.org/10.1038/s41467-021-23506-0</a>.
  ieee: M. Obr <i>et al.</i>, “Structure of the mature Rous sarcoma virus lattice
    reveals a role for IP6 in the formation of the capsid hexamer,” <i>Nature Communications</i>,
    vol. 12, no. 1. Nature Research, 2021.
  ista: Obr M, Ricana CL, Nikulin N, Feathers J-PR, Klanschnig M, Thader A, Johnson
    MC, Vogt VM, Schur FK, Dick RA. 2021. Structure of the mature Rous sarcoma virus
    lattice reveals a role for IP6 in the formation of the capsid hexamer. Nature
    Communications. 12(1), 3226.
  mla: Obr, Martin, et al. “Structure of the Mature Rous Sarcoma Virus Lattice Reveals
    a Role for IP6 in the Formation of the Capsid Hexamer.” <i>Nature Communications</i>,
    vol. 12, no. 1, 3226, Nature Research, 2021, doi:<a href="https://doi.org/10.1038/s41467-021-23506-0">10.1038/s41467-021-23506-0</a>.
  short: M. Obr, C.L. Ricana, N. Nikulin, J.-P.R. Feathers, M. Klanschnig, A. Thader,
    M.C. Johnson, V.M. Vogt, F.K. Schur, R.A. Dick, Nature Communications 12 (2021).
corr_author: '1'
date_created: 2021-05-28T14:25:50Z
date_published: 2021-05-28T00:00:00Z
date_updated: 2025-04-15T08:24:49Z
day: '28'
ddc:
- '570'
department:
- _id: FlSc
doi: 10.1038/s41467-021-23506-0
external_id:
  isi:
  - '000659145000011'
file:
- access_level: open_access
  checksum: 53ccc53d09a9111143839dbe7784e663
  content_type: application/pdf
  creator: kschuh
  date_created: 2021-06-09T15:21:14Z
  date_updated: 2021-06-09T15:21:14Z
  file_id: '9538'
  file_name: 2021_NatureCommunications_Obr.pdf
  file_size: 6166295
  relation: main_file
  success: 1
file_date_updated: 2021-06-09T15:21:14Z
has_accepted_license: '1'
intvolume: '        12'
isi: 1
issue: '1'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
- General Physics and Astronomy
- General Chemistry
language:
- iso: eng
month: '05'
oa: 1
oa_version: Published Version
project:
- _id: 26736D6A-B435-11E9-9278-68D0E5697425
  call_identifier: FWF
  grant_number: P31445
  name: Structural conservation and diversity in retroviral capsid
publication: Nature Communications
publication_identifier:
  eissn:
  - 2041-1723
publication_status: published
publisher: Nature Research
quality_controlled: '1'
related_material:
  link:
  - description: News on IST Homepage
    relation: press_release
    url: https://ist.ac.at/en/news/how-retroviruses-become-infectious/
scopus_import: '1'
status: public
title: Structure of the mature Rous sarcoma virus lattice reveals a role for IP6 in
  the formation of the capsid hexamer
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: 12
year: '2021'
...
---
_id: '5907'
abstract:
- lang: eng
  text: Microalgae of the genus Chlorella vulgaris are candidates for the production
    of lipids for biofuel production. Besides that, Chlorella vulgaris is marketed
    as protein and vitamin rich food additive. Its potential as a novel expression
    system for recombinant proteins inspired us to study its asparagine-linked oligosaccharides
    (N-glycans) by mass spectrometry, chromatography and gas chromatography. Oligomannosidic
    N-glycans with up to nine mannoses were the structures found in culture collection
    strains as well as several commercial products. These glycans co-eluted with plant
    N-glycans in the highly shape selective porous graphitic carbon chromatography.
    Thus, Chlorella vulgaris generates oligomannosidic N-glycans of the structural
    type known from land plants and animals. In fact, Man5 (Man5GlcNAc2) served as
    substrate for GlcNAc-transferase I and a trace of an endogenous structure with
    terminal GlcNAc was seen. The unusual more linear Man5 structure recently found
    on glycoproteins of Chlamydomonas reinhardtii occurred - if at all - in traces
    only. Notably, a majority of the oligomannosidic glycans was multiply O-methylated
    with 3-O-methyl and 3,6-di-O-methyl mannoses at the non-reducing termini. This
    modification has so far been neither found on plant nor vertebrate N-glycans.
    It’s possible immunogenicity raises concerns as to the use of C. vulgaris for
    production of pharmaceutical glycoproteins.
article_number: '331'
article_processing_charge: No
author:
- first_name: Réka
  full_name: Mócsai, Réka
  last_name: Mócsai
- first_name: Rudolf
  full_name: Figl, Rudolf
  last_name: Figl
- first_name: Clemens
  full_name: Troschl, Clemens
  last_name: Troschl
- first_name: Richard
  full_name: Strasser, Richard
  last_name: Strasser
- first_name: Elisabeth
  full_name: Svehla, Elisabeth
  last_name: Svehla
- first_name: Markus
  full_name: Windwarder, Markus
  last_name: Windwarder
- first_name: Andreas
  full_name: Thader, Andreas
  id: 3A18A7B8-F248-11E8-B48F-1D18A9856A87
  last_name: Thader
- first_name: Friedrich
  full_name: Altmann, Friedrich
  last_name: Altmann
citation:
  ama: Mócsai R, Figl R, Troschl C, et al. N-glycans of the microalga Chlorella vulgaris
    are of the oligomannosidic type but highly methylated. <i>Scientific Reports</i>.
    2019;9(1). doi:<a href="https://doi.org/10.1038/s41598-018-36884-1">10.1038/s41598-018-36884-1</a>
  apa: Mócsai, R., Figl, R., Troschl, C., Strasser, R., Svehla, E., Windwarder, M.,
    … Altmann, F. (2019). N-glycans of the microalga Chlorella vulgaris are of the
    oligomannosidic type but highly methylated. <i>Scientific Reports</i>. Nature
    Publishing Group. <a href="https://doi.org/10.1038/s41598-018-36884-1">https://doi.org/10.1038/s41598-018-36884-1</a>
  chicago: Mócsai, Réka, Rudolf Figl, Clemens Troschl, Richard Strasser, Elisabeth
    Svehla, Markus Windwarder, Andreas Thader, and Friedrich Altmann. “N-Glycans of
    the Microalga Chlorella Vulgaris Are of the Oligomannosidic Type but Highly Methylated.”
    <i>Scientific Reports</i>. Nature Publishing Group, 2019. <a href="https://doi.org/10.1038/s41598-018-36884-1">https://doi.org/10.1038/s41598-018-36884-1</a>.
  ieee: R. Mócsai <i>et al.</i>, “N-glycans of the microalga Chlorella vulgaris are
    of the oligomannosidic type but highly methylated,” <i>Scientific Reports</i>,
    vol. 9, no. 1. Nature Publishing Group, 2019.
  ista: Mócsai R, Figl R, Troschl C, Strasser R, Svehla E, Windwarder M, Thader A,
    Altmann F. 2019. N-glycans of the microalga Chlorella vulgaris are of the oligomannosidic
    type but highly methylated. Scientific Reports. 9(1), 331.
  mla: Mócsai, Réka, et al. “N-Glycans of the Microalga Chlorella Vulgaris Are of
    the Oligomannosidic Type but Highly Methylated.” <i>Scientific Reports</i>, vol.
    9, no. 1, 331, Nature Publishing Group, 2019, doi:<a href="https://doi.org/10.1038/s41598-018-36884-1">10.1038/s41598-018-36884-1</a>.
  short: R. Mócsai, R. Figl, C. Troschl, R. Strasser, E. Svehla, M. Windwarder, A.
    Thader, F. Altmann, Scientific Reports 9 (2019).
date_created: 2019-02-03T22:59:13Z
date_published: 2019-01-23T00:00:00Z
date_updated: 2023-08-24T14:33:16Z
day: '23'
ddc:
- '580'
department:
- _id: FlSc
doi: 10.1038/s41598-018-36884-1
external_id:
  isi:
  - '000456392400012'
file:
- access_level: open_access
  checksum: 4129c7d7663d1f8a1edf8c4232372f66
  content_type: application/pdf
  creator: dernst
  date_created: 2019-02-05T13:10:02Z
  date_updated: 2020-07-14T12:47:13Z
  file_id: '5923'
  file_name: 2019_ScientificReports_Mocsai.pdf
  file_size: 2124292
  relation: main_file
file_date_updated: 2020-07-14T12:47:13Z
has_accepted_license: '1'
intvolume: '         9'
isi: 1
issue: '1'
language:
- iso: eng
month: '01'
oa: 1
oa_version: Published Version
publication: Scientific Reports
publication_status: published
publisher: Nature Publishing Group
quality_controlled: '1'
scopus_import: '1'
status: public
title: N-glycans of the microalga Chlorella vulgaris are of the oligomannosidic type
  but highly methylated
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: 9
year: '2019'
...