An RGD (arginine-glycine-aspartic acid) motif in coxsackievirus A9 has
been implicated in internalization through an interaction with the in
tegrin alpha(v) beta(3). We have produced a number of virus mutants, l
acking the motif, which have a small-plaque phenotype in LLC-Mk(2) and
A-Vero cells and are phenotypically normal in RD cells. Substitution
of flanking amino acids also affected plaque size. The results suggest
that interaction between the RGD motif and alpha(v) beta(3) is not cr
itical for virus viability in the cell lines tested and therefore that
alternative regions of the CAV-9 capsid are involved in internalizati
on.