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PMID: 6184485 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Protease bypass of temperature-sensitive murine leukemia virus maturation mutants.

Journal of virology ·Vol. 44 ·No. 3 ·1982-12-00 ·Pages 1039-46

Traktman P, Baltimore D

Abstract

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.

MeSH Terms
Animals Cells, Cultured Mice Moloney murine leukemia virus/drug effects,genetics Mutation Peptide Hydrolases/pharmacology RNA-Directed DNA Polymerase/metabolism Temperature Trypsin Viral Proteins/genetics
Chemicals
Viral Proteins RNA-Directed DNA Polymerase Peptide Hydrolases Trypsin
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Traktman P
Baltimore D
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21 references, click to expand
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
DOI
10.1128/JVI.44.3.1039-1046.1982
Published
1982-12-00
Pages
1039-46
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC256364
Subset
IM
Grants
NCI NIH HHS · CA-14051 · United States
External Links
PubMed source DOI: 10.1128/JVI.44.3.1039-1046.1982 PMC Full Text View journal details
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