A recombinant, arginine-glycine-aspartic acid (RGD) motif from foot-and-mouth disease virus binds mammalian cells through vitronectin and, to a lower extent, fibronectin receptors

A. Villaverde, J. X. Feliu, R. P. Harbottle, A. Benito, C. Coutelle

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20 Citations (Scopus)

Abstract

The cell-binding abilities of a recombinant, RGD-containing peptide from foot-and-mouth disease virus (FMDV) have been characterized in HeLa and BHK cells. This peptide represents the aa sequence of the solvent-exposed G-H loop of protein VP1 which is involved in cell recognition and infection. The efficiency of the viral motif in promoting cell attachment and spreading is comparable to that shown by fibronectin or vitronectin. Cell binding is inhibited by a monoclonal antibody directed against a viral, RGD-involving B-cell epitope and also by sera against vitronectin (α(V)β3/β5) and fibronectin (α5β1) receptors. In addition, a synthetic RGD peptide, which is a ligand for both integrins, prevents the cell binding mediated by the FMDV domain. These data demonstrate that the FMDV RGD motif is a potent ligand for cell-receptor integrins and sufficient to promote cell attachment to susceptible cells mainly through the vitronectin receptor.
Original languageEnglish
Pages (from-to)101-106
JournalGene
Volume180
Issue number1-2
DOIs
Publication statusPublished - 21 Nov 1996

Keywords

  • Antigenic site
  • Cellular receptor
  • Fusion protein
  • Integrin
  • Picornavirus
  • Protein VP1

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