Evidence map›Paper›PMID 19520960›Full record

ArticleScience (New York, N.Y.)2009

Structure of rotavirus outer-layer protein VP7 bound with a neutralizing Fab.

Scott T Aoki, Ethan C Settembre, Shane D Trask, Harry B Greenberg, Stephen C Harrison, Philip R Dormitzer

Open access · greenAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 140 papers.

0numbers the graph read from it
0cells of the map it votes in
140citing papers in PubMed
7.9field-weighted citation impact, top 2% 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

140 citing papers in PubMed, 260 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Mechanism of membrane perforation in rotavirus cell entry.bioRxiv : the preprint server for biology · 2026
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Viruses · 2025
    Article
  19. Article
  20. Article

80 more citing papers are in PubMed but not listed here.

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

6 authors at 2 institutions in 1 country.

Scott T AokiLaboratory of Molecular Medicine, Children's Hospital, Boston, MA 02115, USA.
Ethan C Settembre
Shane D Trask
Harry B Greenberg
Stephen C Harrison
Philip R Dormitzer
Boston Children's Hospital · USHoward Hughes Medical Institute · US

Funding

Proteomics/GenomicsP30DK056339 · NIDDK · STANFORD UNIVERSITY · PI GREENBERG, HARRY BERNARD · 2001 to 2010
$10.4M
VIRAL GASTROENTERITIS--BASIS OF PROTECTION AND VIRULENCER01AI021362 · NIAID · STANFORD UNIVERSITY · PI GREENBERG, HARRY BERNARD · 1989 to 2014
$5.4M
STRUCTURE AND ASSEMBLY OF VIRUSES AND OF COATED VESICLESR01CA013202 · NCI · HARVARD UNIVERSITY · PI HARRISON, STEPHEN COPLAN · 1985 to 2024
$4.9M
Structure and Assembly of VirusesR37CA013202 · NCI · CHILDREN'S HOSPITAL BOSTON · PI HARRISON, STEPHEN COPLAN · 2003 to 2012
$3.7M
VIRAL GASTROENTERITIS--BASIS OF PROTECTION AND VIRULENCER37AI021362 · NIAID · STANFORD UNIVERSITY · PI GREENBERG, HARRY BERNARD · 1994 to 2003
$789k
Viral Gastroenteritis: Basis of Virulence and ProtectionR56AI021362 · NIAID · PALO ALTO VETERANS INSTIT FOR RESEARCH · PI GREENBERG, HARRY BERNARD · 2015 to 2015
$506k
VIRAL GASTROENTERITIS: BASIS OF VIRULENCE AND PROTECTIONR22AI021362 · NIAID · STANFORD UNIVERSITY · PI GREENBERG, HARRY BERNARD · 1985 to 1991
–
Howard Hughes Medical InstituteNCI NIH HHS CA-13202NCI NIH HHS R01 CA013202NCI NIH HHS R37 CA013202NIAID NIH HHS AI-21362NIDDK NIH HHS DK-56339
6 · The paper itself

Abstract

Rotavirus outer-layer protein VP7 is a principal target of protective antibodies. Removal of free calcium ions (Ca2+) dissociates VP7 trimers into monomers, releasing VP7 from the virion, and initiates penetration-inducing conformational changes in the other outer-layer protein, VP4. We report the crystal structure at 3.4 angstrom resolution of VP7 bound with the Fab fragment of a neutralizing monoclonal antibody. The Fab binds across the outer surface of the intersubunit contact, which contains two Ca2+ sites. Mutations that escape neutralization by other antibodies suggest that the same region bears the epitopes of most neutralizing antibodies. The monovalent Fab is sufficient to neutralize infectivity. We propose that neutralizing antibodies against VP7 act by stabilizing the trimer, thereby inhibiting the uncoating trigger for VP4 rearrangement. A disulfide-linked trimer is a potential subunit immunogen.

Indexed as

Amino Acid SequenceAntibodies, MonoclonalAntibodies, ViralAntigens, ViralBinding SitesBinding Sites, AntibodyCalciumCapsid ProteinsCrystallography, X-RayEpitopesImmunoglobulin Fab FragmentsModels, MolecularMolecular Sequence DataMutationNeutralization TestsProtein FoldingAntibodies, MonoclonalAntibodies, ViralAntigens, ViralCalciumCapsid ProteinsEpitopesImmunoglobulin Fab FragmentsProtein SubunitsRecombinant ProteinsVP7 protein, Rotavirus

Identifiers

PMID19520960
PMCPMC2995306
OpenAlexW2103211789

What OpenQuestion holds

Textmetadata
LicenceTDM
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.