Evidence map›Paper›PMID 21775460›Full record

ArticleJournal of virology2011

An externalized polypeptide partitions between two distinct sites on genome-released poliovirus particles.

Jun Lin, Naiqian Cheng, Marie Chow, David J Filman, Alasdair C Steven, James M Hogle, David M Belnap

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

34 citing papers in PubMed, 43 citations in OpenAlex.

  1. Open questions in enterovirus uncoating.Journal of virology · 2026
    Review
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  8. Antibody-induced uncoating of human rhinovirus B14.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
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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

7 authors at 5 institutions in 1 country.

Jun LinDepartment of Chemistry and Biochemistry, Brigham Young University, Provo, UT 84602, USA.
Naiqian Cheng
Marie Chow
David J Filman
Alasdair C Steven
James M Hogle
David M Belnap
Harvard University · USNational Institute of Arthritis and Musculoskeletal and Skin Diseases · USBrigham Young University · USNational Institutes of Health · USUniversity of Arkansas for Medical Sciences · US

Funding

Structural Biology Of Virus AssemblyZIAAR027002 · NIAMS · NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES · PI WINGFIELD, PAUL T · 2009 to 2024
$19.2M
Structural Analysis of Enterovirus Cell Entry PathwaysR01AI020566 · NIAID · SCRIPPS RESEARCH INSTITUTE · PI HOGLE, JAMES M · 1985 to 2018
$9.0M
EARLY STAGES OF INFECTION BY NONENVELOPED VIRUSESR01AI042390 · NIAID · UNIVERSITY OF ARKANSAS MED SCIS LTL ROCK · PI CHOW, MARIE · 1998 to 2002
$961k
Temperature-dependent, Intermediate Particles from the Entry of Picornaviruses inR15AI084085 · NIAID · BRIGHAM YOUNG UNIVERSITY · PI BELNAP, DAVID MICHAEL · 2009 to 2009
$225k
MOLECULAR ANALYSIS OF POLIOVIRUS NEUTRALIZING EPITOPESR01AI022627 · NIAID · UNIVERSITY OF ARKANSAS MED SCIS LTL ROCK · PI CHOW, MARIE · 1985 to 1999
–
NIAID NIH HHS AI042390NIAID NIH HHS R01 AI020566NIAID NIH HHS R01AI020566NIAID NIH HHS R01 AI022627NIAID NIH HHS R01 AI042390NIAID NIH HHS R15 AI084085NIAID NIH HHS R15AI084085
6 · The paper itself

Abstract

During cell entry, native poliovirus (160S) converts to a cell-entry intermediate (135S) particle, resulting in the externalization of capsid proteins VP4 and the amino terminus of VP1 (residues 1 to 53). Externalization of these entities is followed by release of the RNA genome (uncoating), leaving an empty (80S) particle. The antigen-binding fragment (Fab) of a monospecific peptide 1 (P1) antibody, which was raised against a peptide corresponding to amino-terminal residues 24 to 40 of VP1, was utilized to track the location of the amino terminus of VP1 in the 135S and 80S states of poliovirus particles via cryogenic electron microscopy (cryo-EM) and three-dimensional image reconstruction. On 135S, P1 Fabs bind to a prominent feature on the external surface known as the "propeller tip." In contrast, our initial 80S-P1 reconstruction showed P1 Fabs also binding to a second site, at least 50 Å distant, at the icosahedral 2-fold axes. Further analysis showed that the overall population of 80S-P1 particles consisted of three kinds of capsids: those with P1 Fabs bound only at the propeller tips, P1 Fabs bound only at the 2-fold axes, or P1 Fabs simultaneously bound at both positions. Our results indicate that, in 80S particles, a significant fraction of VP1 can deviate from icosahedral symmetry. Hence, this portion of VP1 does not change conformation synchronously when switching from the 135S state. These conclusions are compatible with previous observations of multiple conformations of the 80S state and suggest that movement of the amino terminus of VP1 has a role in uncoating. Similar deviations from icosahedral symmetry may be biologically significant during other viral transitions.

Indexed as

Virus UncoatingCapsid ProteinsCryoelectron MicroscopyHeLa CellsHumansImaging, Three-DimensionalModels, MolecularPoliovirusRNA, ViralVirionCapsid ProteinsRNA, ViralVP1 protein, Poliovirus

Identifiers

PMID21775460
PMCPMC3196412
OpenAlexW2152938732

What OpenQuestion holds

Textmetadata
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.