Protease bypass of temperature-sensitive murine leukemia virus maturation mutants.
Cells infected with certain temperature-sensitive mutants of Moloney murine leukemia virus synthesize the virion precursor proteins but neither bud virions nor cleave precursor proteins to their mature form. Addition of proteases to cells infected with these mutants caused cleavage of the precursor proteins Pr65gag and Pr180gag-pol to their mature forms at the nonpermissive temperature. Concomitantly there was release from the cells of morphologically normal virions. The enzymatically inactive Pr180gag-pol was cleaved to active reverse transcriptase (p85), which was found in the released particles. External protease treatment apparently bypassed the lesion in these viral mutants, suggesting that their defect may involve a virus-specific protease.
D000818:Animals; D002478:Cells, Cultured; D051379:Mice; D008979:Moloney murine leukemia virus / Q000187:drug effects / Q000235:genetics*; D009154:Mutation; D010447:Peptide Hydrolases / Q000494:pharmacology*; D012194:RNA-Directed DNA Polymerase / Q000378:metabolism; D013696:Temperature; D014357:Trypsin; D014764:Viral Proteins / Q000235:genetics*
D014764:Viral Proteins; D012194:RNA-Directed DNA Polymerase; D010447:Peptide Hydrolases; D014357:Trypsin