Synthesis and cleavage processing of oncornavirus proteins during interferon inhibition of virus particle release.

The effect of interferon on the rate of synthesis and the cleavage processing of viral proteins in mouse cells, chronically infected with Rauscher murine leukemia virus, has been studied by immunoprecipitation of newly synthesized viral proteins from virus-infected cells pulse-labeled with [35S]methionine. Immuno-precipitated, labeled polypeptides were resolved by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate and then examined by autoradiography. Cleavage processing was studied in the same manner with cells that had been pulse-labeled and then incubated with non-radioactive media for a sufficient time to allow normal cleavage processing to occur. At a concentration that strongly inhibited the release of virus particles, interferon had no effect on the synthesis of proteins carrying antigenic determinants of the major core protein p30 or of the envelope glycoprotein gp69/71. Nor did it affect the post-translational cleavage processing of the precursors to these proteins. Similarly, interferon did not affect labeling or chasing of precursor protein carrying the p15 determinants; labeling of p15 itself could not be studied because it does not contain methionine.