Abstract
The structural proteins of wild-type Sindbis virus were shown to arise by posttranslational cleavage of larger precursors. The proteins synthesized in wildtype infection were compared with those specified by ts-11, a temperature-sensitive mutant unable to synthesize viral RNA at the restrictive temperature. Abnormally large, virus-specific proteins were found in the mutant-infected cells after the shift from 28 C to 41.5 C. These large polypeptides were presumably precursors which were cleaved too rapidly to be detected in the wild-type infection. The largest had a molecular weight of 133,000 and was the same size as the apparent precursor detected during infection with a group of Sindbis mutants which could not form nucleocapsids at the nonpermissive temperature. The stability of ts-11-specific RNA synthesis, after shift from permissive to restrictive conditions, differed from that in cells infected by wild-type virus, indicating that the virus had a genetic lesion in an enzyme involved in RNA synthesis. This mutation might have caused the precursor to fold incorrectly so that it could not be cleaved. The possibility cannot be excluded, however, that a second lesion in an uncharacterized viral function, such as a protease, was the cause of the accumulation of the precursors.
Full text
PDF








Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Burge B. W., Pfefferkorn E. R. Complementation between temperature-sensitive mutants of Sindbis virus. Virology. 1966 Oct;30(2):214–223. doi: 10.1016/0042-6822(66)90097-3. [DOI] [PubMed] [Google Scholar]
- Burge B. W., Pfefferkorn E. R. Functional defects of temperature-sensitive mutants of Sindbis virus. J Mol Biol. 1968 Jul 14;35(1):193–205. doi: 10.1016/s0022-2836(68)80047-6. [DOI] [PubMed] [Google Scholar]
- Burge B. W., Pfefferkorn E. R. Isolation and characterization of conditional-lethal mutants of Sindbis virus. Virology. 1966 Oct;30(2):204–213. doi: 10.1016/0042-6822(66)90096-1. [DOI] [PubMed] [Google Scholar]
- Burrell C. J., Martin E. M., Cooper P. D. Posttranslational cleavage of virus polypeptides in arbovirus-infected cells. J Gen Virol. 1970 Feb;6(2):319–323. doi: 10.1099/0022-1317-6-2-319. [DOI] [PubMed] [Google Scholar]
- Dobos P., Faulkner P. Molecular weight of Sindbis virus ribonucleic acid as measured by polyacrylamide gel electrophoresis. J Virol. 1970 Jul;6(1):145–147. doi: 10.1128/jvi.6.1.145-147.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Eaton B. T., Donaghue T. P., Faulkner P. Presence of poly (A) in the polyribosome-associated RNA of Sindbis-infected BHK cells. Nat New Biol. 1972 Jul 26;238(82):109–111. doi: 10.1038/newbio238109a0. [DOI] [PubMed] [Google Scholar]
- Friedman R. M. Primary gene products of an arbovirus. Biochem Biophys Res Commun. 1969 Oct 8;37(2):369–373. doi: 10.1016/0006-291x(69)90744-x. [DOI] [PubMed] [Google Scholar]
- Jacobson M. F., Baltimore D. Polypeptide cleavages in the formation of poliovirus proteins. Proc Natl Acad Sci U S A. 1968 Sep;61(1):77–84. doi: 10.1073/pnas.61.1.77. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kennedy S. I. Isolation and identification of the virus-specified RNA species found on membrane-bound polyribosomes of chick embryo cells infected with Semliki Forest virus. Biochem Biophys Res Commun. 1972 Sep 5;48(5):1254–1258. doi: 10.1016/0006-291x(72)90846-7. [DOI] [PubMed] [Google Scholar]
- Kiehn E. D., Holland J. J. Synthesis and cleavage of enterovirus polypeptides in mammalian cells. J Virol. 1970 Mar;5(3):358–367. doi: 10.1128/jvi.5.3.358-367.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Levin J. G., Friedman R. M. Analysis of arbovirus ribonucleic acid forms by polyacrylamide gel electrophoresis. J Virol. 1971 Apr;7(4):504–514. doi: 10.1128/jvi.7.4.504-514.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Loening U. E. Molecular weights of ribosomal RNA in relation to evolution. J Mol Biol. 1968 Dec;38(3):355–365. doi: 10.1016/0022-2836(68)90391-4. [DOI] [PubMed] [Google Scholar]
- Pfefferkorn E. R., Boyle M. K. Selective inhibition of the synthesis of Sindbis virion proteins by an inhibitor of chymotrypsin. J Virol. 1972 Jan;9(1):187–188. doi: 10.1128/jvi.9.1.187-188.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Scheele C. M., Pfefferkorn E. R. Inhibition of interjacent ribonucleic acid (26S) synthesis in cells infected by Sindbis virus. J Virol. 1969 Aug;4(2):117–122. doi: 10.1128/jvi.4.2.117-122.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Scheele C. M., Pfefferkorn E. R. Kinetics of incorporation of structural proteins into Sindbis virions. J Virol. 1969 Apr;3(4):369–375. doi: 10.1128/jvi.3.4.369-375.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Scheele C. M., Pfefferkorn E. R. Virus-specific proteins synthesized in cells infected with RNA+ temperature-sensitive mutants of Sindbis virus. J Virol. 1970 Mar;5(3):329–337. doi: 10.1128/jvi.5.3.329-337.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Schlesinger M. J., Schlesinger S., Burge B. W. Identification of a second glycoprotein in Sindbis virus. Virology. 1972 Feb;47(2):539–541. doi: 10.1016/0042-6822(72)90298-x. [DOI] [PubMed] [Google Scholar]
- Shapiro A. L., Viñuela E., Maizel J. V., Jr Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels. Biochem Biophys Res Commun. 1967 Sep 7;28(5):815–820. doi: 10.1016/0006-291x(67)90391-9. [DOI] [PubMed] [Google Scholar]
- Strauss J. H., Jr, Burge B. W., Darnell J. E. Sindbis virus infection of chick and hamster cells: synthesis of virus-specific proteins. Virology. 1969 Mar;37(3):367–376. doi: 10.1016/0042-6822(69)90220-7. [DOI] [PubMed] [Google Scholar]
- Strauss J. H., Jr, Burge B. W., Pfefferkorn E. R., Darnell J. E., Jr Identification of the membrane protein and "core" protein of Sindbis virus. Proc Natl Acad Sci U S A. 1968 Feb;59(2):533–537. doi: 10.1073/pnas.59.2.533. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Waite M. R., Pfefferkorn E. R. Phospholipid synthesis in Sindbis virus-infected cells. J Virol. 1970 Nov;6(5):637–643. doi: 10.1128/jvi.6.5.637-643.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed] [Google Scholar]