The coxsackievirus A9 RGD motif is not essential for virus viability.
An RGD (arginine-glycine-aspartic acid) motif in coxsackievirus A9 has been implicated in internalization through an interaction with the integrin alpha v beta 3. We have produced a number of virus mutants, lacking the motif, which have a small-plaque phenotype in LLC-Mk2 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 critical for virus viability in the cell lines tested and therefore that alternative regions of the CAV-9 capsid are involved in internalization.
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002460:Cell Line; D002522:Chlorocebus aethiops; D018076:DNA, Complementary; D004770:Enterovirus / Q000235:genetics / Q000502:physiology*; D007700:Kinetics; D008969:Molecular Sequence Data; D016296:Mutagenesis; D009838:Oligodeoxyribonucleotides; D009842:Oligopeptides; D010641:Phenotype; D019030:Receptors, Vitronectin / Q000502:physiology; D017384:Sequence Deletion; D014709:Vero Cells; D010948:Viral Plaque Assay
D018076:DNA, Complementary; D009838:Oligodeoxyribonucleotides; D009842:Oligopeptides; D019030:Receptors, Vitronectin; C047981:arginyl-glycyl-aspartic acid