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

The cell-binding abilities of a recombinant, RGD-containing peptide fr om 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 at tachment and spreading is comparable to that shown by fibronectin or v itronectin. Cell binding is inhibited by a monoclonal antibody directe d against a viral, RGD-involving B-cell epitope and also by sera again st vitronectin (alpha(v) beta(3)/beta(5)) and fibronectin (alpha(5) be ta(1)) receptors. In addition, a synthetic RGD peptide, which is a lig and for both integrins, prevents the cell binding mediated by the FMDV domain. These data demonstrate that the FMDV RGD motif is a potent li gand for cell-receptor integrins and sufficient to promote cell attach ment to susceptible cells mainly through the vitronectin receptor.