ArticleJournal of virology2006
Specificity of the VP1 GH loop of Foot-and-Mouth Disease virus for alphav integrins.
Article in Journal of virology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
What it found
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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.
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.
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Who cites it
60 citing papers in PubMed, 131 citations in OpenAlex.
- Cattle antibodies identify a cross-serotype broadly neutralising foot-and-mouth disease virus epitope.NPJ vaccines · 2026Article
- The multifaceted roles of fibronectin in viral pathogenesis.Archives of virology · 2026Review
- Adaptive Evolution of Serotype O Foot-and-Mouth Disease Virus Under Vaccine Pressure: Combined VP1 T142/Q153 Mutations Drive Antigenic Alteration and Immune Evasion.Transboundary and emerging diseases · 2026Article
- Genome-wide CRISPR screen identifies RNF24 as a critical host factor for foot-and-mouth disease virus entry.Frontiers in cell and developmental biology · 2026Article
- Foot-and-mouth disease virus vaccine with VP1 G-H loop substitution of the Cathay strain broadens antigen spectrum.Applied microbiology and biotechnology · 2025Article
- Foot-and-mouth disease: genomic and proteomic structure, antigenic sites, serotype relationships, immune evasion, recent vaccine development strategies, and future perspectives.Veterinary research · 2025Review
- Distinct mutations emerge in the genome of serotype O foot-and-mouth disease virus during persistence in cattle.Journal of virology · 2025Article
- Mapping cross-reactive residues in the G-H loop of foot-and-mouth disease virus: insights for serotype-specific design.Frontiers in microbiology · 2025Article
- Review
- Discovery, recognized antigenic structures, and evolution of cross-serotype broadly neutralizing antibodies from porcine B-cell repertoires against foot-and-mouth disease virus.PLoS pathogens · 2024Article
- A ferritin-based nanoparticle displaying a neutralizing epitope for foot-and-mouth disease virus (FMDV) confers partial protection in guinea pigs.BMC veterinary research · 2024Article
- Self-Assembling Nanovaccine Fused with Flagellin Enhances Protective Effect against Foot-and-Mouth Disease Virus.Vaccines · 2023Article
- Development of a primary cell model derived from porcine dorsal soft palate for foot-and-mouth disease virus research and diagnosis.Frontiers in microbiology · 2023Article
- The prevalence of foot-and-mouth disease in Asia.Frontiers in veterinary science · 2023Review
- Development of reverse-transcriptase, real-time PCR assays to distinguish the Southern African Territories (SAT) serotypes 1 and 3 and topotype VII of SAT2 of Foot-and-Mouth Disease Virus.Frontiers in veterinary science · 2022Article
- Rational design of novel fusion rabies glycoproteins displaying a major antigenic site of foot-and-mouth disease virus for vaccine applications.Applied microbiology and biotechnology · 2022Article
- The RGD-binding integrins αvβ6 and αvβ8 are receptors for mouse adenovirus-1 and -3 infection.PLoS pathogens · 2021Article
- Halting the Spread of Herpes Simplex Virus-1: The Discovery of an Effective Dual αvβ6/αvβ8 Integrin Ligand.Journal of medicinal chemistry · 2021Article
- Review
- Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Foot-and-mouth disease virus (FMDV) can use a number of integrins as receptors to initiate infection. Attachment to the integrin is mediated by a highly conserved arginine-glycine-aspartic acid (RGD) tripeptide located on the GH loop of VP1. Other residues of this loop are also conserved and may contribute to integrin binding. In this study we have used a 17-mer peptide, whose sequence corresponds to the GH loop of VP1 of type O FMDV, as a competitor of integrin-mediated virus binding and infection. Alanine substitution through this peptide identified the leucines at the first and fourth positions following RGD (RGD+1 and RGD+4 sites) as key for inhibition of virus binding and infection mediated by alphavbeta6 or alphavbeta8 but not for inhibition of virus binding to alphavbeta3. We also show that FMDV peptides containing either methionine or arginine at the RGD+1 site, which reflects the natural sequence variation seen across the FMDV serotypes, are effective inhibitors for alphavbeta6. In contrast, although RGDM-containing peptides were effective for alphavbeta8, RGDR-containing peptides were not. These observations were confirmed by showing that a virus containing an RGDR motif uses alphavbeta8 less efficiently than alphavbeta6 as a receptor for infection. Finally, evidence is presented that shows alphavbeta3 to be a poor receptor for infection by type O FMDV. Taken together, our data suggest that the integrin binding loop of FMDV has most likely evolved for binding to alphavbeta6 with a higher affinity than to alphavbeta3 and alphavbeta8.
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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.