Deciphering foot-and-mouth disease (FMD) virus-host tropism.

The pattern of interactions between foot and mouth disease (FMD) viral protein 1 (VP1) with susceptible and resistant host integrins were deciphered. The putative effect of site-directed mutation on alteration of interaction is illustrated using predicted and validated 3D structures of VP1, mutated VP1 and integrins of , and . Strong interactions were observed between FMDV-VP1 protein motifs at conserved tripeptide, Arg-Gly-Asp RGD and at domain SIPLQ in alpha-integrin of Notably, site-directed mutation in FMDV-VP1 protein led to complete loss of interaction between FMD-VP1 protein and integrin, which confirmed the active role of arginine-glycine-aspartic acid (RGD) domain.