Evidence map›Paper›PMID 15452204›Full record

ArticleJournal of virology2004

VP7 mediates the interaction of rotaviruses with integrin alphavbeta3 through a novel integrin-binding site.

Selene Zárate, Pedro Romero, Rafaela Espinosa, Carlos F Arias, Susana López

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

26 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Viruses Binding to Host Receptors Interacts with Autophagy.International journal of molecular sciences · 2023
    Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. Review
  11. Article
  12. Review
  13. Article
  14. Assessing the oncolytic potential of rotavirus on mouse myeloma cell line Sp2/0-Ag14.Biomedica : revista del Instituto Nacional de Salud · 2020
    Article
  15. Article
  16. Beyond the Matrix: The Many Non-ECM Ligands for Integrins.International journal of molecular sciences · 2018
    Review
  17. Review
  18. Article
  19. The integrin adhesome: from genes and proteins to human disease.Nature reviews. Molecular cell biology · 2014
    Review
  20. 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 1 institution in 1 country.

Selene ZárateDepartamento de Génetica del Desarrollo y Fisiología Molecular, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Avenida Universidad 2001, Col. Chamilpa, Cuernavaca, Morelos 62210, Mexico.
Pedro Romero
Rafaela Espinosa
Carlos F Arias
Susana López
Universidad Nacional Autónoma de México · MX

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rotavirus entry is a complex multistep process that depends on the trypsin cleavage of the virus spike protein VP4 into polypeptides VP5 and VP8 and on the interaction of these polypeptides and of VP7, the second viral surface protein, with several cell surface molecules, including integrin alphavbeta3. We characterized the effect of the trypsin cleavage of VP4 on the binding to MA104 cells of the sialic acid-dependent virus strain RRV and its sialic acid-independent variant, nar3. We found that, although the trypsin treatment did not affect the attachment of these viruses to the cell surface, their binding was qualitatively different. In contrast to the trypsin-treated viruses, which initially bound to the cell surface through VP4, the non-trypsin-treated variant nar3 bound to the cell through VP7. Amino acid sequence comparison of the surface proteins of rotavirus and hantavirus, both of which interact with integrin alphavbeta3 in an RGD-independent manner, identified a region shared by rotavirus VP7 and hantavirus G1G2 protein in which six of nine amino acids are identical. This region, which is highly conserved among the VP7 proteins of different rotavirus strains, mediates the binding of rotaviruses to integrin alphavbeta3 and probably represents a novel binding motif for this integrin.

Indexed as

Gene Expression Regulation, ViralAmino Acid SequenceAnimalsAntigens, ViralBinding SitesCapsid ProteinsCell LineIntegrin alphaVbeta3Macaca mulattaMolecular Sequence DataN-Acetylneuraminic AcidRotavirusTrypsinAntigens, ViralCapsid ProteinsIntegrin alphaVbeta3N-Acetylneuraminic AcidTrypsinVP4 protein, RotavirusVP7 protein, Rotavirus

Identifiers

PMID15452204
PMCPMC521812
OpenAlexW2098802906

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.