Protease bypass of temperature-sensitive murine leukemia virus maturation mutants. J Virol 1982 Dec;44(3):1039-46
Date
12/01/1982Pubmed ID
6184485Pubmed Central ID
PMC256364DOI
10.1128/JVI.44.3.1039-1046.1982Scopus ID
2-s2.0-0020354781 (requires institutional sign-in at Scopus site) 5 CitationsAbstract
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.
Author List
Traktman P, Baltimore DMESH terms used to index this publication - Major topics in bold
AnimalsCells, Cultured
Mice
Moloney murine leukemia virus
Mutation
Peptide Hydrolases
RNA-Directed DNA Polymerase
Temperature
Trypsin
Viral Proteins