---
_id: '14592'
abstract:
- lang: eng
text: Cryo-electron microscopy (cryo-EM) of cellular specimens provides insights
into biological processes and structures within a native context. However, a major
challenge still lies in the efficient and reproducible preparation of adherent
cells for subsequent cryo-EM analysis. This is due to the sensitivity of many
cellular specimens to the varying seeding and culturing conditions required for
EM experiments, the often limited amount of cellular material and also the fragility
of EM grids and their substrate. Here, we present low-cost and reusable 3D printed
grid holders, designed to improve specimen preparation when culturing challenging
cellular samples directly on grids. The described grid holders increase cell culture
reproducibility and throughput, and reduce the resources required for cell culturing.
We show that grid holders can be integrated into various cryo-EM workflows, including
micro-patterning approaches to control cell seeding on grids, and for generating
samples for cryo-focused ion beam milling and cryo-electron tomography experiments.
Their adaptable design allows for the generation of specialized grid holders customized
to a large variety of applications.
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. STL-files for 3D-printed grid holders described in Fäßler F, Zens
B, et al.; 3D printed cell culture grid holders for improved cellular specimen
preparation in cryo-electron microscopy. 2020. doi:10.15479/AT:ISTA:14592
apa: Schur, F. K. (2020). STL-files for 3D-printed grid holders described in Fäßler
F, Zens B, et al.; 3D printed cell culture grid holders for improved cellular
specimen preparation in cryo-electron microscopy. Institute of Science and Technology
Austria. https://doi.org/10.15479/AT:ISTA:14592
chicago: Schur, Florian KM. “STL-Files for 3D-Printed Grid Holders Described in
Fäßler F, Zens B, et Al.; 3D Printed Cell Culture Grid Holders for Improved Cellular
Specimen Preparation in Cryo-Electron Microscopy.” Institute of Science and Technology
Austria, 2020. https://doi.org/10.15479/AT:ISTA:14592.
ieee: F. K. Schur, “STL-files for 3D-printed grid holders described in Fäßler F,
Zens B, et al.; 3D printed cell culture grid holders for improved cellular specimen
preparation in cryo-electron microscopy.” Institute of Science and Technology
Austria, 2020.
ista: Schur FK. 2020. STL-files for 3D-printed grid holders described in Fäßler
F, Zens B, et al.; 3D printed cell culture grid holders for improved cellular
specimen preparation in cryo-electron microscopy, Institute of Science and Technology
Austria, 10.15479/AT:ISTA:14592.
mla: Schur, Florian KM. STL-Files for 3D-Printed Grid Holders Described in Fäßler
F, Zens B, et Al.; 3D Printed Cell Culture Grid Holders for Improved Cellular
Specimen Preparation in Cryo-Electron Microscopy. Institute of Science and
Technology Austria, 2020, doi:10.15479/AT:ISTA:14592.
short: F.K. Schur, (2020).
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: Bettina
id: 45FD126C-F248-11E8-B48F-1D18A9856A87
last_name: Zens
- contributor_type: researcher
first_name: Robert
id: 4E01D6B4-F248-11E8-B48F-1D18A9856A87
last_name: Hauschild
- contributor_type: researcher
first_name: Florian KM
id: 48AD8942-F248-11E8-B48F-1D18A9856A87
last_name: Schur
orcid: 0000-0003-4790-8078
date_created: 2023-11-22T15:00:57Z
date_published: 2020-12-01T00:00:00Z
date_updated: 2024-02-21T12:44:48Z
day: '01'
ddc:
- '570'
department:
- _id: FlSc
doi: 10.15479/AT:ISTA:14592
file:
- access_level: open_access
checksum: 0108616e2a59e51879ea51299a29b091
content_type: application/zip
creator: fschur
date_created: 2023-11-22T14:58:44Z
date_updated: 2023-11-22T14:58:44Z
file_id: '14593'
file_name: 3Dprint-files_download_v2.zip
file_size: 49297
relation: main_file
success: 1
- access_level: open_access
checksum: 4c66ddedee4d01c1c4a7978208350cfc
content_type: text/plain
creator: cchlebak
date_created: 2023-12-01T10:39:59Z
date_updated: 2023-12-01T10:39:59Z
file_id: '14637'
file_name: readme.txt
file_size: 641
relation: main_file
success: 1
file_date_updated: 2023-12-01T10:39:59Z
has_accepted_license: '1'
license: https://creativecommons.org/licenses/by-nc-sa/4.0/
month: '12'
oa: 1
oa_version: Published Version
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:
record:
- id: '8586'
relation: research_data
status: public
status: public
title: STL-files for 3D-printed grid holders described in Fäßler F, Zens B, et al.;
3D printed cell culture grid holders for improved cellular specimen preparation
in cryo-electron microscopy
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: research_data
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2020'
...
---
_id: '6890'
abstract:
- lang: eng
text: Describing the protein interactions that form pleomorphic and asymmetric viruses
represents a considerable challenge to most structural biology techniques, including
X-ray crystallography and single particle cryo-electron microscopy. Obtaining
a detailed understanding of these interactions is nevertheless important, considering
the number of relevant human pathogens that do not follow strict icosahedral or
helical symmetry. Cryo-electron tomography and subtomogram averaging methods provide
structural insights into complex biological environments and are well suited to
go beyond structures of perfectly symmetric viruses. This chapter discusses recent
developments showing that cryo-ET and subtomogram averaging can provide high-resolution
insights into hitherto unknown structural features of pleomorphic and asymmetric
virus particles. It also describes how these methods have significantly added
to our understanding of retrovirus capsid assemblies in immature and mature viruses.
Additional examples of irregular viruses and their associated proteins, whose
structures have been studied via cryo-ET and subtomogram averaging, further support
the versatility of these methods.
article_processing_charge: No
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
citation:
ama: 'Obr M, Schur FK. Structural analysis of pleomorphic and asymmetric viruses
using cryo-electron tomography and subtomogram averaging. In: Rey FA, ed. Complementary
Strategies to Study Virus Structure and Function. Vol 105. Advances in Virus
Research. Elsevier; 2019:117-159. doi:10.1016/bs.aivir.2019.07.008'
apa: Obr, M., & Schur, F. K. (2019). Structural analysis of pleomorphic and
asymmetric viruses using cryo-electron tomography and subtomogram averaging. In
F. A. Rey (Ed.), Complementary Strategies to Study Virus Structure and Function
(Vol. 105, pp. 117–159). Elsevier. https://doi.org/10.1016/bs.aivir.2019.07.008
chicago: Obr, Martin, and Florian KM Schur. “Structural Analysis of Pleomorphic
and Asymmetric Viruses Using Cryo-Electron Tomography and Subtomogram Averaging.”
In Complementary Strategies to Study Virus Structure and Function, edited
by Félix A. Rey, 105:117–59. Advances in Virus Research. Elsevier, 2019. https://doi.org/10.1016/bs.aivir.2019.07.008.
ieee: M. Obr and F. K. Schur, “Structural analysis of pleomorphic and asymmetric
viruses using cryo-electron tomography and subtomogram averaging,” in Complementary
Strategies to Study Virus Structure and Function, vol. 105, F. A. Rey, Ed.
Elsevier, 2019, pp. 117–159.
ista: 'Obr M, Schur FK. 2019.Structural analysis of pleomorphic and asymmetric viruses
using cryo-electron tomography and subtomogram averaging. In: Complementary Strategies
to Study Virus Structure and Function. vol. 105, 117–159.'
mla: Obr, Martin, and Florian KM Schur. “Structural Analysis of Pleomorphic and
Asymmetric Viruses Using Cryo-Electron Tomography and Subtomogram Averaging.”
Complementary Strategies to Study Virus Structure and Function, edited
by Félix A. Rey, vol. 105, Elsevier, 2019, pp. 117–59, doi:10.1016/bs.aivir.2019.07.008.
short: M. Obr, F.K. Schur, in:, F.A. Rey (Ed.), Complementary Strategies to Study
Virus Structure and Function, Elsevier, 2019, pp. 117–159.
date_created: 2019-09-18T08:15:37Z
date_published: 2019-08-27T00:00:00Z
date_updated: 2023-08-30T06:56:00Z
day: '27'
department:
- _id: FlSc
doi: 10.1016/bs.aivir.2019.07.008
editor:
- first_name: Félix A.
full_name: Rey, Félix A.
last_name: Rey
external_id:
isi:
- '000501594500006'
pmid:
- ' 31522703'
intvolume: ' 105'
isi: 1
language:
- iso: eng
month: '08'
oa_version: None
page: 117-159
pmid: 1
publication: Complementary Strategies to Study Virus Structure and Function
publication_identifier:
isbn:
- '9780128184561'
issn:
- 0065-3527
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
series_title: Advances in Virus Research
status: public
title: Structural analysis of pleomorphic and asymmetric viruses using cryo-electron
tomography and subtomogram averaging
type: book_chapter
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 105
year: '2019'
...
---
_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. Scientific Reports.
2019;9(1). doi:10.1038/s41598-018-36884-1
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. Scientific Reports. Nature
Publishing Group. https://doi.org/10.1038/s41598-018-36884-1
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.”
Scientific Reports. Nature Publishing Group, 2019. https://doi.org/10.1038/s41598-018-36884-1.
ieee: R. Mócsai et al., “N-glycans of the microalga Chlorella vulgaris are
of the oligomannosidic type but highly methylated,” Scientific Reports,
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.” Scientific Reports, vol.
9, no. 1, 331, Nature Publishing Group, 2019, doi:10.1038/s41598-018-36884-1.
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
license: https://creativecommons.org/licenses/by/4.0/
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'
...
---
_id: '6343'
abstract:
- lang: eng
text: Cryo-electron tomography (cryo-ET) provides unprecedented insights into the
molecular constituents of biological environments. In combination with an image
processing method called subtomogram averaging (STA), detailed 3D structures of
biological molecules can be obtained in large, irregular macromolecular assemblies
or in situ, without the need for purification. The contextual meta-information
these methods also provide, such as a protein’s location within its native environment,
can then be combined with functional data. This allows the derivation of a detailed
view on the physiological or pathological roles of proteins from the molecular
to cellular level. Despite their tremendous potential in in situ structural biology,
cryo-ET and STA have been restricted by methodological limitations, such as the
low obtainable resolution. Exciting progress now allows one to reach unprecedented
resolutions in situ, ranging in optimal cases beyond the nanometer barrier. Here,
I review current frontiers and future challenges in routinely determining high-resolution
structures in in situ environments using cryo-ET and STA.
acknowledgement: The author acknowledges support from IST Austria and the Austrian
Science Fund (FWF).
article_processing_charge: No
article_type: original
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. Toward high-resolution in situ structural biology with cryo-electron
tomography and subtomogram averaging. Current Opinion in Structural Biology.
2019;58(10):1-9. doi:10.1016/j.sbi.2019.03.018
apa: Schur, F. K. (2019). Toward high-resolution in situ structural biology with
cryo-electron tomography and subtomogram averaging. Current Opinion in Structural
Biology. Elsevier. https://doi.org/10.1016/j.sbi.2019.03.018
chicago: Schur, Florian KM. “Toward High-Resolution in Situ Structural Biology with
Cryo-Electron Tomography and Subtomogram Averaging.” Current Opinion in Structural
Biology. Elsevier, 2019. https://doi.org/10.1016/j.sbi.2019.03.018.
ieee: F. K. Schur, “Toward high-resolution in situ structural biology with cryo-electron
tomography and subtomogram averaging,” Current Opinion in Structural Biology,
vol. 58, no. 10. Elsevier, pp. 1–9, 2019.
ista: Schur FK. 2019. Toward high-resolution in situ structural biology with cryo-electron
tomography and subtomogram averaging. Current Opinion in Structural Biology. 58(10),
1–9.
mla: Schur, Florian KM. “Toward High-Resolution in Situ Structural Biology with
Cryo-Electron Tomography and Subtomogram Averaging.” Current Opinion in Structural
Biology, vol. 58, no. 10, Elsevier, 2019, pp. 1–9, doi:10.1016/j.sbi.2019.03.018.
short: F.K. Schur, Current Opinion in Structural Biology 58 (2019) 1–9.
date_created: 2019-04-19T11:19:13Z
date_published: 2019-10-01T00:00:00Z
date_updated: 2023-08-25T10:13:31Z
day: '01'
department:
- _id: FlSc
doi: 10.1016/j.sbi.2019.03.018
external_id:
isi:
- '000494891800004'
intvolume: ' 58'
isi: 1
issue: '10'
language:
- iso: eng
month: '10'
oa_version: None
page: 1-9
publication: Current Opinion in Structural Biology
publication_identifier:
issn:
- 0959-440X
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Toward high-resolution in situ structural biology with cryo-electron tomography
and subtomogram averaging
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 58
year: '2019'
...
---
_id: '5770'
abstract:
- lang: eng
text: Retroviruses assemble and bud from infected cells in an immature form and
require proteolytic maturation for infectivity. The CA (capsid) domains of the
Gag polyproteins assemble a protein lattice as a truncated sphere in the immature
virion. Proteolytic cleavage of Gag induces dramatic structural rearrangements;
a subset of cleaved CA subsequently assembles into the mature core, whose architecture
varies among retroviruses. Murine leukemia virus (MLV) is the prototypical γ-retrovirus
and serves as the basis of retroviral vectors, but the structure of the MLV CA
layer is unknown. Here we have combined X-ray crystallography with cryoelectron
tomography to determine the structures of immature and mature MLV CA layers within
authentic viral particles. This reveals the structural changes associated with
maturation, and, by comparison with HIV-1, uncovers conserved and variable features.
In contrast to HIV-1, most MLV CA is used for assembly of the mature core, which
adopts variable, multilayered morphologies and does not form a closed structure.
Unlike in HIV-1, there is similarity between protein–protein interfaces in the
immature MLV CA layer and those in the mature CA layer, and structural maturation
of MLV could be achieved through domain rotations that largely maintain hexameric
interactions. Nevertheless, the dramatic architectural change on maturation indicates
that extensive disassembly and reassembly are required for mature core growth.
The core morphology suggests that wrapping of the genome in CA sheets may be sufficient
to protect the MLV ribonucleoprotein during cell entry.
article_processing_charge: No
author:
- first_name: Kun
full_name: Qu, Kun
last_name: Qu
- first_name: Bärbel
full_name: Glass, Bärbel
last_name: Glass
- first_name: Michal
full_name: Doležal, Michal
last_name: Doležal
- first_name: Florian
full_name: Schur, Florian
id: 48AD8942-F248-11E8-B48F-1D18A9856A87
last_name: Schur
orcid: 0000-0003-4790-8078
- first_name: Brice
full_name: Murciano, Brice
last_name: Murciano
- first_name: Alan
full_name: Rein, Alan
last_name: Rein
- first_name: Michaela
full_name: Rumlová, Michaela
last_name: Rumlová
- first_name: Tomáš
full_name: Ruml, Tomáš
last_name: Ruml
- first_name: Hans-Georg
full_name: Kräusslich, Hans-Georg
last_name: Kräusslich
- first_name: John A. G.
full_name: Briggs, John A. G.
last_name: Briggs
citation:
ama: Qu K, Glass B, Doležal M, et al. Structure and architecture of immature and
mature murine leukemia virus capsids. Proceedings of the National Academy of
Sciences. 2018;115(50):E11751-E11760. doi:10.1073/pnas.1811580115
apa: Qu, K., Glass, B., Doležal, M., Schur, F. K., Murciano, B., Rein, A., … Briggs,
J. A. G. (2018). Structure and architecture of immature and mature murine leukemia
virus capsids. Proceedings of the National Academy of Sciences. Proceedings
of the National Academy of Sciences. https://doi.org/10.1073/pnas.1811580115
chicago: Qu, Kun, Bärbel Glass, Michal Doležal, Florian KM Schur, Brice Murciano,
Alan Rein, Michaela Rumlová, Tomáš Ruml, Hans-Georg Kräusslich, and John A. G.
Briggs. “Structure and Architecture of Immature and Mature Murine Leukemia Virus
Capsids.” Proceedings of the National Academy of Sciences. Proceedings
of the National Academy of Sciences, 2018. https://doi.org/10.1073/pnas.1811580115.
ieee: K. Qu et al., “Structure and architecture of immature and mature murine
leukemia virus capsids,” Proceedings of the National Academy of Sciences,
vol. 115, no. 50. Proceedings of the National Academy of Sciences, pp. E11751–E11760,
2018.
ista: Qu K, Glass B, Doležal M, Schur FK, Murciano B, Rein A, Rumlová M, Ruml T,
Kräusslich H-G, Briggs JAG. 2018. Structure and architecture of immature and mature
murine leukemia virus capsids. Proceedings of the National Academy of Sciences.
115(50), E11751–E11760.
mla: Qu, Kun, et al. “Structure and Architecture of Immature and Mature Murine Leukemia
Virus Capsids.” Proceedings of the National Academy of Sciences, vol. 115,
no. 50, Proceedings of the National Academy of Sciences, 2018, pp. E11751–60,
doi:10.1073/pnas.1811580115.
short: K. Qu, B. Glass, M. Doležal, F.K. Schur, B. Murciano, A. Rein, M. Rumlová,
T. Ruml, H.-G. Kräusslich, J.A.G. Briggs, Proceedings of the National Academy
of Sciences 115 (2018) E11751–E11760.
date_created: 2018-12-20T21:09:37Z
date_published: 2018-12-11T00:00:00Z
date_updated: 2023-09-19T09:57:45Z
day: '11'
department:
- _id: FlSc
doi: 10.1073/pnas.1811580115
external_id:
isi:
- '000452866000022'
pmid:
- '30478053'
intvolume: ' 115'
isi: 1
issue: '50'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.ncbi.nlm.nih.gov/pubmed/30478053
month: '12'
oa: 1
oa_version: Submitted Version
page: E11751-E11760
pmid: 1
publication: Proceedings of the National Academy of Sciences
publication_identifier:
issn:
- '00278424'
publication_status: published
publisher: Proceedings of the National Academy of Sciences
quality_controlled: '1'
scopus_import: '1'
status: public
title: Structure and architecture of immature and mature murine leukemia virus capsids
type: journal_article
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 115
year: '2018'
...
---
_id: '150'
abstract:
- lang: eng
text: A short, 14-amino-acid segment called SP1, located in the Gag structural protein1,
has a critical role during the formation of the HIV-1 virus particle. During virus
assembly, the SP1 peptide and seven preceding residues fold into a six-helix bundle,
which holds together the Gag hexamer and facilitates the formation of a curved
immature hexagonal lattice underneath the viral membrane2,3. Upon completion of
assembly and budding, proteolytic cleavage of Gag leads to virus maturation, in
which the immature lattice is broken down; the liberated CA domain of Gag then
re-assembles into the mature conical capsid that encloses the viral genome and
associated enzymes. Folding and proteolysis of the six-helix bundle are crucial
rate-limiting steps of both Gag assembly and disassembly, and the six-helix bundle
is an established target of HIV-1 inhibitors4,5. Here, using a combination of
structural and functional analyses, we show that inositol hexakisphosphate (InsP6,
also known as IP6) facilitates the formation of the six-helix bundle and assembly
of the immature HIV-1 Gag lattice. IP6 makes ionic contacts with two rings of
lysine residues at the centre of the Gag hexamer. Proteolytic cleavage then unmasks
an alternative binding site, where IP6 interaction promotes the assembly of the
mature capsid lattice. These studies identify IP6 as a naturally occurring small
molecule that promotes both assembly and maturation of HIV-1.
article_processing_charge: No
article_type: original
author:
- first_name: Robert
full_name: Dick, Robert
last_name: Dick
- first_name: Kaneil K
full_name: Zadrozny, Kaneil K
last_name: Zadrozny
- first_name: Chaoyi
full_name: Xu, Chaoyi
last_name: Xu
- first_name: Florian
full_name: Schur, Florian
id: 48AD8942-F248-11E8-B48F-1D18A9856A87
last_name: Schur
orcid: 0000-0003-4790-8078
- first_name: Terri D
full_name: Lyddon, Terri D
last_name: Lyddon
- first_name: Clifton L
full_name: Ricana, Clifton L
last_name: Ricana
- first_name: Jonathan M
full_name: Wagner, Jonathan M
last_name: Wagner
- first_name: Juan R
full_name: Perilla, Juan R
last_name: Perilla
- first_name: Pornillos Barbie K
full_name: Ganser, Pornillos Barbie K
last_name: Ganser
- first_name: Marc C
full_name: Johnson, Marc C
last_name: Johnson
- first_name: Owen
full_name: Pornillos, Owen
last_name: Pornillos
- first_name: Volker
full_name: Vogt, Volker
last_name: Vogt
citation:
ama: Dick R, Zadrozny KK, Xu C, et al. Inositol phosphates are assembly co-factors
for HIV-1. Nature. 2018;560(7719):509–512. doi:10.1038/s41586-018-0396-4
apa: Dick, R., Zadrozny, K. K., Xu, C., Schur, F. K., Lyddon, T. D., Ricana, C.
L., … Vogt, V. (2018). Inositol phosphates are assembly co-factors for HIV-1.
Nature. Nature Publishing Group. https://doi.org/10.1038/s41586-018-0396-4
chicago: Dick, Robert, Kaneil K Zadrozny, Chaoyi Xu, Florian KM Schur, Terri D Lyddon,
Clifton L Ricana, Jonathan M Wagner, et al. “Inositol Phosphates Are Assembly
Co-Factors for HIV-1.” Nature. Nature Publishing Group, 2018. https://doi.org/10.1038/s41586-018-0396-4.
ieee: R. Dick et al., “Inositol phosphates are assembly co-factors for HIV-1,”
Nature, vol. 560, no. 7719. Nature Publishing Group, pp. 509–512, 2018.
ista: Dick R, Zadrozny KK, Xu C, Schur FK, Lyddon TD, Ricana CL, Wagner JM, Perilla
JR, Ganser PBK, Johnson MC, Pornillos O, Vogt V. 2018. Inositol phosphates are
assembly co-factors for HIV-1. Nature. 560(7719), 509–512.
mla: Dick, Robert, et al. “Inositol Phosphates Are Assembly Co-Factors for HIV-1.”
Nature, vol. 560, no. 7719, Nature Publishing Group, 2018, pp. 509–512,
doi:10.1038/s41586-018-0396-4.
short: R. Dick, K.K. Zadrozny, C. Xu, F.K. Schur, T.D. Lyddon, C.L. Ricana, J.M.
Wagner, J.R. Perilla, P.B.K. Ganser, M.C. Johnson, O. Pornillos, V. Vogt, Nature
560 (2018) 509–512.
date_created: 2018-12-11T11:44:53Z
date_published: 2018-08-29T00:00:00Z
date_updated: 2023-09-12T07:44:37Z
day: '29'
department:
- _id: FlSc
doi: 10.1038/s41586-018-0396-4
external_id:
isi:
- '000442483400046'
pmid:
- '30158708'
intvolume: ' 560'
isi: 1
issue: '7719'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6242333/
month: '08'
oa: 1
oa_version: Submitted Version
page: 509–512
pmid: 1
publication: Nature
publication_identifier:
eissn:
- 1476-4687
publication_status: published
publisher: Nature Publishing Group
quality_controlled: '1'
related_material:
link:
- relation: erratum
url: https://doi.org/10.1038/s41586-018-0505-4
scopus_import: '1'
status: public
title: Inositol phosphates are assembly co-factors for HIV-1
type: journal_article
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 560
year: '2018'
...