Abstract
Our studies on the formation of Sindbis virus proteins have established that: 1. one of the two envelope proteins (E2) accumulates in infected cells as a higher molecular weight precursor that is slowly converted to the virion protein; 2. the large protein (mol. wt ≧ 130000 daltons), that accumulates in cells infected with a temperature-sensitive mutant of Sindbis virus contains sequences of the three virion proteins; and 3. the protein (mol. wt. ≧ 100000 daltons) isolated from BHK cells infected with Sindbis virus is related in sequence to the two envelope proteins.
We have investigated the formation of defective-interfering (DI) particles of Sindbis virus and their ability to inhibit the replication of standard virus. BHK cells infected with passages of Sindbis virus containing DI particles accumulate a species of RNA (20S) that is about half the molecular weight of the 26S RNA. We have demonstrated by competitive hybridization experiments that 20S RNA contains half the sequences of 26S RNA. We also present evidence that in contrast to 26S RNA, 20S does not bind to polysomesin vivo and is not translatedin vitro.
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Presented on the Meeting on Studies on Virus Replication of the Commission of the European Communities in Brüssel, May 1974.
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Schlesinger, S., Weiss, B., Goran, D. et al. Formation of RNA and protein in cells infected with standard and defective Sindbis virus. Med Microbiol Immunol 160, 311–329 (1974). https://doi.org/10.1007/BF02121446
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DOI: https://doi.org/10.1007/BF02121446