Skip to main content
NCBI home page
Journal of Virology logoLink to Journal of Virology
. 1988 Nov;62(11):4259–4264. doi: 10.1128/jvi.62.11.4259-4264.1988

Translocation of rubella virus glycoprotein E1 into the endoplasmic reticulum.

T C Hobman 1, R Shukin 1, S Gillam 1
PMCID: PMC253859  PMID: 2845137

Abstract

Rubella virus (RV) contains four structural proteins, C (capsid), E2a, E2b, and E1, which are derived from posttranslational processing of a single polyprotein precursor, p110. C protein is nonglycosylated and is thought to interact with RV RNA to form a nucleocapsid. E1 and E2 are membrane glycoproteins that form the spike complexes located on the virion exterior. Two different E1 cDNAs were used to analyze the requirements for translocation of E1 into the endoplasmic reticulum. Analysis of expression of these cDNAs both in vivo and in vitro showed that RV E1 was stably expressed and glycosylated in COS cells and correctly targeted into microsomes in the absence of E2 glycoprotein. The results provide experimental evidence that translocation of RV E1 glycoprotein into the endoplasmic reticulum is mediated by a signal peptide contained within the 69 carboxyl-terminal residues of E2.

Full text

PDF
4259

Images in this article

4262Image
on p.4262
4262Image
on p.4262
4263Image
on p.4263

Selected References

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

  1. Abdul Jabbar M., Nayak D. P. Signal processing, glycosylation, and secretion of mutant hemagglutinins of a human influenza virus by Saccharomyces cerevisiae. Mol Cell Biol. 1987 Apr;7(4):1476–1485. doi: 10.1128/mcb.7.4.1476. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Adams G. A., Rose J. K. Structural requirements of a membrane-spanning domain for protein anchoring and cell surface transport. Cell. 1985 Jul;41(3):1007–1015. doi: 10.1016/s0092-8674(85)80081-7. [DOI] [PubMed] [Google Scholar]
  3. Beverley S. M., Wilson A. C. Ancient origin for Hawaiian Drosophilinae inferred from protein comparisons. Proc Natl Acad Sci U S A. 1985 Jul;82(14):4753–4757. doi: 10.1073/pnas.82.14.4753. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Blobel G., Dobberstein B. Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma. J Cell Biol. 1975 Dec;67(3):835–851. doi: 10.1083/jcb.67.3.835. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Clarke D. M., Loo T. W., Hui I., Chong P., Gillam S. Nucleotide sequence and in vitro expression of rubella virus 24S subgenomic messenger RNA encoding the structural proteins E1, E2 and C. Nucleic Acids Res. 1987 Apr 10;15(7):3041–3057. doi: 10.1093/nar/15.7.3041. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Favaloro J., Treisman R., Kamen R. Transcription maps of polyoma virus-specific RNA: analysis by two-dimensional nuclease S1 gel mapping. Methods Enzymol. 1980;65(1):718–749. doi: 10.1016/s0076-6879(80)65070-8. [DOI] [PubMed] [Google Scholar]
  7. Frey T. K., Marr L. D., Hemphill M. L., Dominguez G. Molecular cloning and sequencing of the region of the rubella virus genome coding for glycoprotein E1. Virology. 1986 Oct 15;154(1):228–232. doi: 10.1016/0042-6822(86)90446-0. [DOI] [PubMed] [Google Scholar]
  8. Garoff H., Kondor-Koch C., Riedel H. Structure and assembly of alphaviruses. Curr Top Microbiol Immunol. 1982;99:1–50. doi: 10.1007/978-3-642-68528-6_1. [DOI] [PubMed] [Google Scholar]
  9. Gething M. J., Sambrook J. Construction of influenza haemagglutinin genes that code for intracellular and secreted forms of the protein. Nature. 1982 Dec 16;300(5893):598–603. doi: 10.1038/300598a0. [DOI] [PubMed] [Google Scholar]
  10. Kalkkinen N., Oker-Blom C., Pettersson R. F. Three genes code for rubella virus structural proteins E1, E2a, E2b and C. J Gen Virol. 1984 Sep;65(Pt 9):1549–1557. doi: 10.1099/0022-1317-65-9-1549. [DOI] [PubMed] [Google Scholar]
  11. Kornfeld R., Kornfeld S. Assembly of asparagine-linked oligosaccharides. Annu Rev Biochem. 1985;54:631–664. doi: 10.1146/annurev.bi.54.070185.003215. [DOI] [PubMed] [Google Scholar]
  12. Kozak M. An analysis of 5'-noncoding sequences from 699 vertebrate messenger RNAs. Nucleic Acids Res. 1987 Oct 26;15(20):8125–8148. doi: 10.1093/nar/15.20.8125. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  14. Melancon P., Garoff H. Reinitiation of translocation in the Semliki Forest virus structural polyprotein: identification of the signal for the E1 glycoprotein. EMBO J. 1986 Jul;5(7):1551–1560. doi: 10.1002/j.1460-2075.1986.tb04396.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Nakhasi H. L., Meyer B. C., Liu T. Y. Rubella virus cDNA. Sequence and expression of E1 envelope protein. J Biol Chem. 1986 Dec 15;261(35):16616–16621. [PubMed] [Google Scholar]
  16. Oker-Blom C., Kalkkinen N., Käriäinen L., Pettersson R. F. Rubella virus contains one capsid protein and three envelope glycoproteins, E1, E2a, and E2b. J Virol. 1983 Jun;46(3):964–973. doi: 10.1128/jvi.46.3.964-973.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Oker-Blom C. The gene order for rubella virus structural proteins is NH2-C-E2-E1-COOH. J Virol. 1984 Aug;51(2):354–358. doi: 10.1128/jvi.51.2.354-358.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Oker-Blom C., Ulmanen I., Käriäinen L., Pettersson R. F. Rubella virus 40S genome RNA specifies a 24S subgenomic mRNA that codes for a precursor to structural proteins. J Virol. 1984 Feb;49(2):403–408. doi: 10.1128/jvi.49.2.403-408.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Sekikawa K., Lai C. J. Defects in functional expression of an influenza virus hemagglutinin lacking the signal peptide sequences. Proc Natl Acad Sci U S A. 1983 Jun;80(12):3563–3567. doi: 10.1073/pnas.80.12.3563. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Singer S. J., Maher P. A., Yaffe M. P. On the transfer of integral proteins into membranes. Proc Natl Acad Sci U S A. 1987 Apr;84(7):1960–1964. doi: 10.1073/pnas.84.7.1960. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Vidgren G., Takkinen K., Kalkkinen N., Käriäinen L., Pettersson R. F. Nucleotide sequence of the genes coding for the membrane glycoproteins E1 and E2 of rubella virus. J Gen Virol. 1987 Sep;68(Pt 9):2347–2357. doi: 10.1099/0022-1317-68-9-2347. [DOI] [PubMed] [Google Scholar]
  23. Walter P., Blobel G. Preparation of microsomal membranes for cotranslational protein translocation. Methods Enzymol. 1983;96:84–93. doi: 10.1016/s0076-6879(83)96010-x. [DOI] [PubMed] [Google Scholar]
  24. von Heijne G. How signal sequences maintain cleavage specificity. J Mol Biol. 1984 Feb 25;173(2):243–251. doi: 10.1016/0022-2836(84)90192-x. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Virology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES