ANTIBODIES AGAINST A SYNTHETIC PEPTIDE OF THE POLIOVIRUS REPLICASE PROTEIN - REACTION WITH NATIVE, VIRUS-ENCODED PROTEINS AND INHIBITION OF VIRUS-SPECIFIC POLYMERASE ACTIVITIES INVITRO

A carboxy-terminal peptide of the poliovirus replicase protein (p63) was chemically synthesized, coupled to bovine serum albumin carrier and injected into rabbits. The resulting antisera reacted with 6 virus-specific proteins from human cervical carcinoma HeLa cells infected with poliovirus: NCVP 0b, NCVP 1b, NCVP 2, a protein of .apprx. 60,000 daltons, p63 and NCVP 6b. The identity of the 60,000-dalton protein is not known, but the other results were consistent with previous experimental approaches which demonstrated that p63 and the other 4 polypeptides have common coding sequences. An amino-terminal peptide of p63 failed to elicit an immune response in rabbits. Antibodies raised against the p63 carboxy-terminal peptide inhibited poliovirus replicase and poly (U) polymerase activities in vitro, providing strong support for earlier suggestions that these activities are a property of a single virus-specific polypeptide.