Skip to main content
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1981 Apr;78(4):2062–2066. doi: 10.1073/pnas.78.4.2062

Nucleotide sequence of the 26S mRNA of Sindbis virus and deduced sequence of the encoded virus structural proteins.

C M Rice, J H Strauss
PMCID: PMC319283  PMID: 6941270

Abstract

The nucleotide sequence of intracellular 26S mRNA of Sindbis virus has been determined by direct sequence analysis of the cDNA made to this RNA with reverse transcriptase. From this, the amino acid sequences of the encoded virus structural proteins, which include a basic capsid protein and two integral membrane glycoproteins, have been deduced. The features of these proteins as related to their functions are discussed. We suggest that three proteases are required to produce these proteins from their polyprotein precursor: a viral protease, which functions in the cytosol to release the capsid protein, signalase, which makes two cleavages to separate the glycoproteins; and a protease of the Golgi complex that cleaves after double basic residues, to process the precursor form of one of the glycoproteins.

Full text

PDF

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Aliperti G., Schlesinger M. J. Evidence for an autoprotease activity of sindbis virus capsid protein. Virology. 1978 Oct 15;90(2):366–369. doi: 10.1016/0042-6822(78)90321-5. [DOI] [PubMed] [Google Scholar]
  2. Bell J. R., Hunkapiller M. W., Hood L. E., Strauss J. H. Amino-terminal sequence analysis of the structural proteins of Sindbis virus. Proc Natl Acad Sci U S A. 1978 Jun;75(6):2722–2726. doi: 10.1073/pnas.75.6.2722. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bell J. R., Strauss E. G., Strauss J. H. Purification and amino acid compositions of the structural proteins of sindbis virus. Virology. 1979 Sep;97(2):287–294. doi: 10.1016/0042-6822(79)90340-4. [DOI] [PubMed] [Google Scholar]
  4. Bhatti A. R., Weber J. Protease of adenovirus type 2: partial characterization. Virology. 1979 Jul 30;96(2):478–485. doi: 10.1016/0042-6822(79)90105-3. [DOI] [PubMed] [Google Scholar]
  5. Blobel G., Walter P., Chang C. N., Goldman B. M., Erickson A. H., Lingappa V. R. Translocation of proteins across membranes: the signal hypothesis and beyond. Symp Soc Exp Biol. 1979;33:9–36. [PubMed] [Google Scholar]
  6. Boege U., Wengler G., Wengler G., Wittmann-Liebold B. Partial amino acid sequences of Sindbis and Semliki Forest virus-specific core proteins. Virology. 1980 May;103(1):178–190. doi: 10.1016/0042-6822(80)90136-1. [DOI] [PubMed] [Google Scholar]
  7. Bonatti S., Blobel G. Absence of a cleavable signal sequence in Sindbis virus glycoprotein PE2. J Biol Chem. 1979 Dec 25;254(24):12261–12264. [PubMed] [Google Scholar]
  8. Burke D. J., Keegstra K. Purification and composition of the proteins from Sindbis virus grown in chick and BHK cells. J Virol. 1976 Dec;20(3):676–686. doi: 10.1128/jvi.20.3.676-686.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Burke D., Keegstra K. Carbohydrate structure of Sindbis virus glycoprotein E2 from virus grown in hamster and chicken cells. J Virol. 1979 Feb;29(2):546–554. doi: 10.1128/jvi.29.2.546-554.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Dalrymple J. M., Schlesinger S., Russell P. K. Antigenic characterization of two sindbis envelope glycoproteins separated by isoelectric focusing. Virology. 1976 Jan;69(1):93–103. doi: 10.1016/0042-6822(76)90197-5. [DOI] [PubMed] [Google Scholar]
  11. Fiers W., Contreras R., Haegemann G., Rogiers R., Van de Voorde A., Van Heuverswyn H., Van Herreweghe J., Volckaert G., Ysebaert M. Complete nucleotide sequence of SV40 DNA. Nature. 1978 May 11;273(5658):113–120. doi: 10.1038/273113a0. [DOI] [PubMed] [Google Scholar]
  12. Garoff H., Frischauf A. M., Simons K., Lehrach H., Delius H. Nucleotide sequence of cdna coding for Semliki Forest virus membrane glycoproteins. Nature. 1980 Nov 20;288(5788):236–241. doi: 10.1038/288236a0. [DOI] [PubMed] [Google Scholar]
  13. Garoff H., Frischauf A. M., Simons K., Lehrach H., Delius H. The capsid protein of Semliki Forest virus has clusters of basic amino acids and prolines in its amino-terminal region. Proc Natl Acad Sci U S A. 1980 Nov;77(11):6376–6380. doi: 10.1073/pnas.77.11.6376. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Garoff H., Simons K., Renkonen O. Isolation and characterization of the membrane proteins of Semliki Forest virus. Virology. 1974 Oct;61(2):493–504. doi: 10.1016/0042-6822(74)90285-2. [DOI] [PubMed] [Google Scholar]
  15. Ghosh P. K., Reddy V. B., Swinscoe J., Choudary P. V., Lebowitz P., Weissman S. M. The 5'-terminal leader sequence of late 16 S mRNA from cells infected with simian virus 40. J Biol Chem. 1978 May 25;253(10):3643–3647. [PubMed] [Google Scholar]
  16. Maxam A. M., Gilbert W. Sequencing end-labeled DNA with base-specific chemical cleavages. Methods Enzymol. 1980;65(1):499–560. doi: 10.1016/s0076-6879(80)65059-9. [DOI] [PubMed] [Google Scholar]
  17. Palmenberg A. C., Pallansch M. A., Rueckert R. R. Protease required for processing picornaviral coat protein resides in the viral replicase gene. J Virol. 1979 Dec;32(3):770–778. doi: 10.1128/jvi.32.3.770-778.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Porter A. G., Barber C., Carey N. H., Hallewell R. A., Threlfall G., Emtage J. S. Complete nucleotide sequence of an influenza virus haemagglutinin gene from cloned DNA. Nature. 1979 Nov 29;282(5738):471–477. doi: 10.1038/282471a0. [DOI] [PubMed] [Google Scholar]
  19. Schmidt M. F., Bracha M., Schlesinger M. J. Evidence for covalent attachment of fatty acids to Sindbis virus glycoproteins. Proc Natl Acad Sci U S A. 1979 Apr;76(4):1687–1691. doi: 10.1073/pnas.76.4.1687. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Schupham R. K., Jones K. J., Sagik B. P., Bose H. R., Jr Virus-directed post-translational cleavage in Sindbus virus-infected cells. J Virol. 1977 May;22(2):568–571. doi: 10.1128/jvi.22.2.568-571.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Sefton B. M., Keegstra K. Glycoproteins of Sindbis virus: priliminary characterization of the oligosaccharides. J Virol. 1974 Sep;14(3):522–530. doi: 10.1128/jvi.14.3.522-530.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Simmons D. T., Strauss J. H. Translation of Sindbis virus 26 S RNA and 49 S RNA in lysates of rabbit reticulocytes. J Mol Biol. 1974 Jun 25;86(2):397–409. doi: 10.1016/0022-2836(74)90027-8. [DOI] [PubMed] [Google Scholar]
  23. Smith D. R., Calvo J. M. Nucleotide sequence of the E coli gene coding for dihydrofolate reductase. Nucleic Acids Res. 1980 May 24;8(10):2255–2274. doi: 10.1093/nar/8.10.2255. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Strauss E. G. Mutants of Sindbis virus. III. Host polypeptides present in purified HR and ts103 virus particles. J Virol. 1978 Nov;28(2):466–474. doi: 10.1128/jvi.28.2.466-474.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Welch W. J., Sefton B. M. Two small virus-specific polypeptides are produced during infection with Sindbis virus. J Virol. 1979 Mar;29(3):1186–1195. doi: 10.1128/jvi.29.3.1186-1195.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Wirth D. F., Katz F., Small B., Lodish H. F. How a single Sindbis virus mRNA directs the synthesis of one soluble protein and two integral membrane glycoproteins. Cell. 1977 Feb;10(2):253–263. doi: 10.1016/0092-8674(77)90219-7. [DOI] [PubMed] [Google Scholar]
  27. Wirth D. F., Lodish H. F., Robbins P. W. Requirements for the insertion of the Sindbis envelope glycoproteins into the endoplasmic reticulum membrane. J Cell Biol. 1979 Apr;81(1):154–162. doi: 10.1083/jcb.81.1.154. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. von der Helm K. Cleavage of Rous sarcoma viral polypeptide precursor into internal structural proteins in vitro involves viral protein p15. Proc Natl Acad Sci U S A. 1977 Mar;74(3):911–915. doi: 10.1073/pnas.74.3.911. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES