Sindbis Virus RNA Replication. I. Properties of the 38S RNA Species

Department of Microbiology, Georgetown University Medical and Dental Schools, Washington, D.C. 20007, U.S.A. Four species of single-stranded virus RNA (49S, 38S, 33S and 26S) were detected in chick embryo fibroblasts infected with Sindbis virus. The relative amounts of these RNAs were unaffected by...

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Bibliographic Details
Published in:Journal of general virology 1979-09, Vol.44 (3), p.759-771
Main Authors: Czarniecki, Christine W, Sreevalsan, T
Format: Article
Language:English
Subjects:
Animals
Chick Embryo
Culture Techniques
Cycloheximide - pharmacology
Dactinomycin - pharmacology
Defective Viruses - growth & development
Defective Viruses - metabolism
Fibroblasts
Nucleic Acid Conformation
RNA, Viral - biosynthesis
Sindbis Virus - growth & development
Sindbis Virus - metabolism
Virus Replication
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Summary:Department of Microbiology, Georgetown University Medical and Dental Schools, Washington, D.C. 20007, U.S.A. Four species of single-stranded virus RNA (49S, 38S, 33S and 26S) were detected in chick embryo fibroblasts infected with Sindbis virus. The relative amounts of these RNAs were unaffected by the m.o.i. There was also no significant difference in the molar proportions of the four RNA species when purified virion RNA was used as the inoculum. These findings suggest that the 38S and 33S species represent products of the transcription of non-defective virion RNAs. Kinetic analyses of RNA synthesis indicated that during a 1 min pulse more radioactivity was associated with the 38S than with the 49S RNA and as the length of the pulse increased, the ratio of 38S/49S decreased, with the 49S appearing as the predominant species. Furthermore, addition of cycloheximide within the first 3 h p.i. resulted in detection of only the 49S species. Synthesis of all four species was unaffected when the drug was added after this time period. These data suggest that the 38S species may represent newly synthesized 49S molecules and some protein(s) synthesized within the first 3 h p.i. is necessary for maintaining the 38S conformational form. * Present address: Laboratory of Experimental Pathology, National Institute of Arthritis, Metabolism and Digestive Diseases, National Institutes of Health, Bethesda, Maryland 20014, U.S.A. Received 4 January 1979; accepted 16 March 1979.
ISSN:0022-1317
1465-2099
DOI:10.1099/0022-1317-44-3-759