Evidence map›Paper›PMID 31986188›Full record

ArticlePLoS pathogens2020

Structures of immature EIAV Gag lattices reveal a conserved role for IP6 in lentivirus assembly.

Robert A Dick, Chaoyi Xu, Dustin R Morado, Vladyslav Kravchuk, Clifton L Ricana, Terri D Lyddon, Arianna M Broad, J Ryan Feathers, Marc C Johnson, Volker M Vogt and 3 more

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
6.0field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

38 citing papers in PubMed, 54 citations in OpenAlex.

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  10. Cryo-electron tomography to study viral infection.Biochemical Society transactions · 2023
    Review
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  14. Structural insights into HIV-1 polyanion-dependent capsid lattice formation revealed by single particle cryo-EM.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  15. Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

13 authors at 5 institutions in 4 countries.

Robert A DickDepartment of Molecular Biology and Genetics, Cornell University, Ithaca, New York, United States of America.ORCID 0000-0003-3693-2531
Chaoyi XuDepartment of Chemistry and Biochemistry, University of Delaware, Newark, Delaware, United States of America.
Dustin R MoradoStructural Studies Division, Medical Research Council Laboratory of Molecular Biology, Cambridge, United Kingdom.ORCID 0000-0003-4693-3220
Vladyslav KravchukInstitute of Science and Technology Austria, Klosterneuburg, Austria.ORCID 0000-0001-9523-9089
Clifton L RicanaDepartment of Molecular Microbiology and Immunology, University of Missouri, Columbia, Missouri, United States of America.ORCID 0000-0002-9733-9136
Terri D LyddonDepartment of Molecular Microbiology and Immunology, University of Missouri, Columbia, Missouri, United States of America.
Arianna M BroadDepartment of Molecular Biology and Genetics, Cornell University, Ithaca, New York, United States of America.ORCID 0000-0001-6566-8667
J Ryan FeathersDepartment of Molecular Biology and Genetics, Cornell University, Ithaca, New York, United States of America.
Marc C JohnsonDepartment of Molecular Microbiology and Immunology, University of Missouri, Columbia, Missouri, United States of America.ORCID 0000-0002-6431-7133
Volker M VogtDepartment of Molecular Biology and Genetics, Cornell University, Ithaca, New York, United States of America.
Juan R PerillaDepartment of Chemistry and Biochemistry, University of Delaware, Newark, Delaware, United States of America.ORCID 0000-0003-1171-6816
John A G BriggsStructural Studies Division, Medical Research Council Laboratory of Molecular Biology, Cambridge, United Kingdom.ORCID 0000-0003-3990-6910
Florian K M SchurInstitute of Science and Technology Austria, Klosterneuburg, Austria.ORCID 0000-0003-4790-8078
Cornell University · USUniversity of Missouri · USInstitute of Science and Technology Austria · ATMRC Laboratory of Molecular Biology · GBUniversity of Delaware · US

Funding

X-Ray Core P50GM082251 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI AHN, JINWOO · 2007 to 2018
$48.1M
Technology Development 2: MAS NMR and dynamic nuclear polarization for HIV-1 structural biologyP50AI150481 · NIAID · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI XIONG, YONG · 2019 to 2021
$14.1M
Pilot Research Subproject ProgramP30GM110758 · NIGMS · UNIVERSITY OF DELAWARE · PI POLENOVA, TATYANA · 2014 to 2018
$5.8M
Retrovirus Structure and Assembly with Inositol PhosphatesR01AI147890 · NIAID · EMORY UNIVERSITY · PI DICK, ROBERT A · 2019 to 2022
$1.6M
Structure and Assembly of RetrovirusesR01GM107013 · NIGMS · CORNELL UNIVERSITY · PI VOGT, VOLKER M. · 2013 to 2018
$1.5M
Structure and Assembly of RetrovirusesR01AI150454 · NIAID · CORNELL UNIVERSITY · PI VOGT, VOLKER M. · 2019 to 2020
$719k
Austrian Science Fund FWF P 31445Medical Research Council MC_UP_1201/16NIAID NIH HHS P50 AI150481NIAID NIH HHS R01 AI147890NIAID NIH HHS R01 AI150454NIGMS NIH HHS P30 GM110758NIGMS NIH HHS P50 GM082251NIGMS NIH HHS R01 GM107013
6 · The paper itself

Abstract

Retrovirus assembly is driven by the multidomain structural protein Gag. Interactions between the capsid domains (CA) of Gag result in Gag multimerization, leading to an immature virus particle that is formed by a protein lattice based on dimeric, trimeric, and hexameric protein contacts. Among retroviruses the inter- and intra-hexamer contacts differ, especially in the N-terminal sub-domain of CA (CANTD). For HIV-1 the cellular molecule inositol hexakisphosphate (IP6) interacts with and stabilizes the immature hexamer, and is required for production of infectious virus particles. We have used in vitro assembly, cryo-electron tomography and subtomogram averaging, atomistic molecular dynamics simulations and mutational analyses to study the HIV-related lentivirus equine infectious anemia virus (EIAV). In particular, we sought to understand the structural conservation of the immature lentivirus lattice and the role of IP6 in EIAV assembly. Similar to HIV-1, IP6 strongly promoted in vitro assembly of EIAV Gag proteins into virus-like particles (VLPs), which took three morphologically highly distinct forms: narrow tubes, wide tubes, and spheres. Structural characterization of these VLPs to sub-4Å resolution unexpectedly showed that all three morphologies are based on an immature lattice with preserved key structural components, highlighting the structural versatility of CA to form immature assemblies. A direct comparison between EIAV and HIV revealed that both lentiviruses maintain similar immature interfaces, which are established by both conserved and non-conserved residues. In both EIAV and HIV-1, IP6 regulates immature assembly via conserved lysine residues within the CACTD and SP. Lastly, we demonstrate that IP6 stimulates in vitro assembly of immature particles of several other retroviruses in the lentivirus genus, suggesting a conserved role for IP6 in lentiviral assembly.

Indexed as

Amino Acid SequenceAnimalsElectron Microscope TomographyEquine Infectious Anemiagag Gene Products, Human Immunodeficiency VirusGene Products, gagHIV-1HIV InfectionsHorsesHost-Pathogen InteractionsInfectious Anemia Virus, EquinePhytic AcidSequence AlignmentVirionVirus Assemblygag Gene Products, Human Immunodeficiency VirusGene Products, gagPhytic Acid

Identifiers

PMID31986188
PMCPMC7004409
OpenAlexW3000717531

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.