Protease bypass of temperature-sensitive murine leukemia virus maturation mutants
- Creators
- Traktman, Paula
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Baltimore, David
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.
Additional Information
Copyright © 1982 by the American Society for Microbiology. Received 10 June 1982. Accepted 13 August 1982. We thank Scott Schroeder and Chris Riser for expert technical assistance. This work was supported by American Cancer Society grant MV-34M and by Public Health Service grant CA-14051 (core grant to S.E. Luria) from the National Cancer Institute. David Baltimore is an American Cancer Society Research Professor.Files
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Additional details
- Eprint ID
- 3621
- Resolver ID
- CaltechAUTHORS:TRAjvir82
- Created
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2006-06-21Created from EPrint's datestamp field
- Updated
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2019-10-02Created from EPrint's last_modified field