INDUCTION OF NEUTRALIZING ANTIBODIES BY SYNTHETIC PEPTIDES REPRESENTING THE C-TERMINUS OF COXSACKIEVIRUS A9 CAPSID PROTEIN VP1

The arginine-glycine-aspartic acid motif at the C terminus of coxsacki evirus A9 capsid protein VP1 has been shown to play a role in specific attachment of the virus to alpha(v)beta(3) integrin on the host cell surface. The C-terminal region of the VP1 protein has also been shown to be highly antigenic by using peptide scanning techniques. To find o ut whether this region contains a neutralizing epitope, three overlapp ing peptides covering the C-terminal end of VP1 were synthesized and r abbit antisera were raised against these peptides. Neutralization of t he virus was observed with all three antipeptide antisera in A549 cell s and with two antisera in RD cells.