Evidence map›Paper›PMID 11867517›Full record

ArticleThe EMBO journal2002

The rhesus rotavirus VP4 sialic acid binding domain has a galectin fold with a novel carbohydrate binding site.

Philip R Dormitzer, Zhen-Yu J Sun, Gerhard Wagner, Stephen C Harrison

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 167 papers.

0numbers the graph read from it
0cells of the map it votes in
167citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

167 citing papers in PubMed, 349 citations in OpenAlex.

  1. Trial
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  9. Viruses · 2025
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107 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

4 authors at 1 institution in 1 country.

Philip R DormitzerLaboratory of Molecular Medicine, Enders 673, Children's Hospital, 320 Longwood Avenue, Boston, MA 02115, USA. dormitze@crystal.harvard.edu
Zhen-Yu J Sun
Gerhard Wagner
Stephen C Harrison
Boston Children's Hospital · US

Funding

T CELL SPECIFIC TRANSCRIPTION COMPLEXESP01GM047467 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WAGNER, GERHARD · 1992 to 2017
$28.6M
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
STRUCTURAL BASIS FOR ROTAVIRUS ENTRY INTO CELLSK08AI001496 · NIAID · CHILDREN'S HOSPITAL BOSTON · PI DORMITZER, PHILIP R · 1998 to 2000
$121k
NCI NIH HHS CA 13202NCI NIH HHS R01 CA013202NCI NIH HHS R37 CA013202NIAID NIH HHS K08 AI 01496NIGMS NIH HHS GM 47467NIGMS NIH HHS P01 GM047467
6 · The paper itself

Abstract

Cell attachment and membrane penetration are functions of the rotavirus outer capsid spike protein, VP4. An activating tryptic cleavage of VP4 produces the N-terminal fragment, VP8*, which is the viral hemagglutinin and an important target of neutralizing antibodies. We have determined, by X-ray crystallography, the atomic structure of the VP8* core bound to sialic acid and, by NMR spectroscopy, the structure of the unliganded VP8* core. The domain has the beta-sandwich fold of the galectins, a family of sugar binding proteins. The surface corresponding to the galectin carbohydrate binding site is blocked, and rotavirus VP8* instead binds sialic acid in a shallow groove between its two beta-sheets. There appears to be a small induced fit on binding. The residues that contact sialic acid are conserved in sialic acid-dependent rotavirus strains. Neutralization escape mutations are widely distributed over the VP8* surface and cluster in four epitopes. From the fit of the VP8* core into the virion spikes, we propose that VP4 arose from the insertion of a host carbohydrate binding domain into a viral membrane interaction protein.

Indexed as

Capsid ProteinsCarbohydrate MetabolismAmino Acid SequenceBinding SitesCapsidConsensus SequenceCrystallography, X-RayEpitopesEvolution, MolecularGalectinsHemagglutininsHemagglutinins, ViralHydrogen BondingModels, MolecularMolecular Sequence DataN-Acetylneuraminic AcidCapsid ProteinsEpitopesGalectinsHemagglutininsHemagglutinins, ViralN-Acetylneuraminic AcidNS35 protein, rotavirusnsp1 protein, RotavirusPeptide FragmentsRecombinant Fusion ProteinsRNA-Binding ProteinsViral Nonstructural ProteinsVP4 protein, Rotavirus

Identifiers

PMID11867517
PMCPMC125907
OpenAlexW2039737871

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.