ArticleJournal of virology2003
Integrin-using rotaviruses bind alpha2beta1 integrin alpha2 I domain via VP4 DGE sequence and recognize alphaXbeta2 and alphaVbeta3 by using VP7 during cell entry.
Article in Journal of virology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.
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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.
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Who cites it
82 citing papers in PubMed, 157 citations in OpenAlex.
- Rotavirus specific maternal antibodies and immune response to RV3-BB neonatal rotavirus vaccine in New Zealand.Human vaccines & immunotherapeutics · 2017Trial
- Bridging antiviral drug discovery with a large language model-powered framework.Communications biology · 2026Article
- Generation of G9 genotype porcine rotavirus using reverse genetics system and its application for antiviral screen and vaccine development.Virologica Sinica · 2026Article
- Integrin α2: mode of regulation and functioning in the metastatic cancer cascade.Journal of translational medicine · 2026Review
- CLDN3 inhibits rotavirus attachment by targeting residue 74 of VP7.PLoS pathogens · 2026Article
- Article
- Review
- Precursor of H-type II histo-blood group antigen and subterminal sialic acids on gangliosides are significantly implicated in cell entry and infection by a porcine P[11] rotavirus.Emerging microbes & infections · 2025Article
- Identifying and validating PLAU as a potential prognostic biomarker for PDAC.Scientific reports · 2025Article
- The reticulocyte restriction: invasion ligand RBP1a ofFrontiers in cellular and infection microbiology · 2025Article
- Antiviral Effects and Mechanisms of Active Ingredients in Tea.Molecules (Basel, Switzerland) · 2024Review
- An Overview of the Characteristics, Pathogenesis, Epidemiology, and Detection of Human Enterovirus in the Arabian Gulf Region.Viruses · 2024Review
- Human Rotaviruses of Multiple Genotypes Acquire Conserved VP4 Mutations during Serial Passage.Viruses · 2024Article
- Interaction of species A rotavirus VP4 with the cellular proteins vimentin and actin related protein 2 discovered by a proximity interactome assay.Journal of virology · 2023Article
- Molecular mimicry of host short linear motif-mediated interactions utilised by viruses for entry.Molecular biology reports · 2023Review
- Vaccinomics Approach for Multi-Epitope Vaccine Design against Group A Rotavirus Using VP4 and VP7 Proteins.Vaccines · 2023Article
- How the Competition for Cysteine May Promote Infection of SARS-CoV-2 by Triggering Oxidative Stress.Antioxidants (Basel, Switzerland) · 2023Article
- Review
- Rotavirus Spike Protein VP4 Mediates Viroplasm Assembly by Association to Actin Filaments.Journal of virology · 2022Article
- An antibody-based proximity labeling map reveals mechanisms of SARS-CoV-2 inhibition of antiviral immunity.Cell chemical biology · 2022Article
22 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 4 institutions in 3 countries.
Funding
Abstract
Integrins alpha2beta1, alphaXbeta2, and alphaVbeta3 have been implicated in rotavirus cell attachment and entry. The virus spike protein VP4 contains the alpha2beta1 ligand sequence DGE at amino acid positions 308 to 310, and the outer capsid protein VP7 contains the alphaXbeta2 ligand sequence GPR. To determine the viral proteins and sequences involved and to define the roles of alpha2beta1, alphaXbeta2, and alphaVbeta3, we analyzed the ability of rotaviruses and their reassortants to use these integrins for cell binding and infection and the effect of peptides DGEA and GPRP on these events. Many laboratory-adapted human, monkey, and bovine viruses used integrins, whereas all porcine viruses were integrin independent. The integrin-using rotavirus strains each interacted with all three integrins. Integrin usage related to VP4 serotype independently of sialic acid usage. Analysis of rotavirus reassortants and assays of virus binding and infectivity in integrin-transfected cells showed that VP4 bound alpha2beta1, and VP7 interacted with alphaXbeta2 and alphaVbeta3 at a postbinding stage. DGEA inhibited rotavirus binding to alpha2beta1 and infectivity, whereas GPRP binding to alphaXbeta2 inhibited infectivity but not binding. The truncated VP5* subunit of VP4, expressed as a glutathione S-transferase fusion protein, bound the expressed alpha2 I domain. Alanine mutagenesis of D308 and G309 in VP5* eliminated VP5* binding to the alpha2 I domain. In a novel process, integrin-using viruses bind the alpha2 I domain of alpha2beta1 via DGE in VP4 and interact with alphaXbeta2 (via GPR) and alphaVbeta3 by using VP7 to facilitate cell entry and infection.
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Registered trials
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.