Evidence map›Paper›PMID 23772035›Full record

ArticleJournal of immunology (Baltimore, Md. : 1950)2013

Conformational shift of a major poliovirus antigen confirmed by immuno-cryogenic electron microscopy.

Jun Lin, Naiqian Cheng, James M Hogle, Alasdair C Steven, David M Belnap

Open access · bronzeAbstract read
In one paragraph

Article in Journal of immunology (Baltimore, Md. : 1950), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.0field-weighted citation impact, top 12% 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

13 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Antibody-induced uncoating of human rhinovirus B14.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  8. Article
  9. Article
  10. Native immunogold labeling of cell surface proteins and viral glycoproteins for cryo-electron microscopy and cryo-electron tomography applications.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2015
    Article
  11. Article
  12. Cross-neutralizing human anti-poliovirus antibodies bind the recognition site for cellular receptor.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  13. Article
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

5 authors at 4 institutions in 1 country.

Jun LinDepartment of Chemistry and Biochemistry, Brigham Young University, Provo, UT 84602, USA.
Naiqian Cheng
James M Hogle
Alasdair C Steven
David M Belnap
National Institutes of Health · USBrigham Young University · USHarvard University · USNational Institute of Arthritis and Musculoskeletal and Skin Diseases · 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
Temperature-dependent, Intermediate Particles from the Entry of Picornaviruses inR15AI084085 · NIAID · BRIGHAM YOUNG UNIVERSITY · PI BELNAP, DAVID MICHAEL · 2009 to 2009
$225k
Intramural NIH HHSNIAID NIH HHS R01 AI020566NIAID NIH HHS R01AI020566NIAID NIH HHS R15 AI084085NIAID NIH HHS R15AI084085
6 · The paper itself

Abstract

Small, interfacial conformational changes occur in some Ag-Ab interactions. Using cryogenic electron microscopy (cryo-EM), we have demonstrated such changes in a major antigenic site of a poliovirus capsid protein. During cell entry, native human poliovirus (160S particle) converts to a cell entry intermediate (135S particle) and later to an RNA-released (80S) particle. By mixing particles with Fabs of the neutralizing C3 mAb, we labeled the external loop connecting the B and C β-strands (BC loop) of the capsid protein VP1 (residues 95-105) in the 160S and 135S states. We then determined three-dimensional structures by cryo-EM and enhanced their interpretability by fitting high-resolution coordinates of C3 Fab and the capsid proteins into the density maps. Binding of C3 to either 160S or 135S particles caused residues of the BC loop, located on the tip of a prominent peak known as the "mesa," to move by an estimated 5 Å. C3 Abs are neutralizing and can bind bivalently. The orientation of the bound Fabs in our reconstructions suggests that C3 neutralizes poliovirus by binding two adjacent BC loops on the same mesa and inhibiting conformational changes in the viral capsid.

Indexed as

Protein ConformationAntibodies, MonoclonalAntibodies, ViralAntigen-Antibody ReactionsCapsidCapsid ProteinsCryoelectron MicroscopyHumansImmunoglobulin Fab FragmentsMicroscopy, ImmunoelectronPoliovirusProtein Structure, TertiaryRNA, ViralAntibodies, MonoclonalAntibodies, ViralCapsid ProteinsImmunoglobulin Fab FragmentsRNA, ViralVP1 protein, Poliovirus

Identifiers

PMID23772035
PMCPMC3816737
OpenAlexW2127479556

What OpenQuestion holds

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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.