Knipe, David and Lodish, Harvey F. and Baltimore, David (1977) Analysis of the defects of temperature-sensitive mutants of vesicular stomatitis virus: intracellular degradation of specific viral proteins. Journal of Virology, 21 (3). pp. 1140-1148. ISSN 0022-538X. PMCID PMC515655. http://resolver.caltech.edu/CaltechAUTHORS:20120727-110028203
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The metabolism of viral RNA and proteins has been studied in cells infected with temperature-sensitive mutant strains of vesicular stomatitis virus. Certain viral proteins encoded by the mutant strains, usually the putative mutant protein for the assigned complementation group, were shown to be degraded more rapidly at the nonpermissive temperature than were the wild-type proteins. Group III mutants (tsG33, tsM301) encode M proteins which are degraded three- to fourfold faster than the wild-type protein. This defect cannot be fully rescued by coinfection with wild-type virus, and thus the defect appears to be in the M protein itself. Mutants tsM601 (VI) and tsG41(IV) encode N proteins which are degraded much faster than the wild-type protein and also share the property of being defective in replication of viral RNA, suggesting a correlation between these phenotypic properties. Furthermore, the L proteins of tsG11(I) and tsG13(I) are more labile than the wild-type protein at the nonpermissive temperature. The G protein of tsM501(V) did not undergo the change in electrophoretic mobility previously shown to be the result of sialylation, suggesting that it is defective in maturation or glycosylation at the nonpermissive temperature. Three of the mutants previously isolated in this laboratory, tsM502(V), tsM601(VI), and tsM602(VI), were shown to be defective in viral RNA synthesis at the nonpermissive temperature. Mutant tsM601(VI) was defective mainly in viral RNA replication, whereas tsM502(V) appeared to be totally defective for viral RNA transcription and replication at the nonpermissive temperature.
|Additional Information:||© 1977 American Society for Microbiology. Received for publication 10 September 1976. We gratefully acknowledge the technical assistance of Martin Brock. D. K. was supported by a National Science Foundation predoctoral fellowship during part of this work and a Public Health Service traineeship during the remainder. H.F.L. was the recipient of Public Health Service research career development award GM-50175 from the National Institute of General Medical Sciences. D.B. is an American Cancer Society research professor. This work was supported by Public Health Service grants AI-08814 and AI-08388 from the National Institute of Allergy and Infectious Diseases, American Cancer Society grant E559, and Public Health Service grant CA-12174 from the National Cancer Institute.|
|PubMed Central ID:||PMC515655|
|Usage Policy:||No commercial reproduction, distribution, display or performance rights in this work are provided.|
|Deposited By:||Jason Perez|
|Deposited On:||30 Jul 2012 15:24|
|Last Modified:||05 Apr 2017 15:48|
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