Abstract
cDNAs encoding the mRNAs for the fusion protein (F) and the hemagglutinin/neuraminidase protein (HN) of the paramyxovirus simian virus 5 have been inserted into a eukaryotic expression vector under the control of the simian virus 40 late promoter. The F and HN proteins synthesized in recombinant infected cells are indistinguishable in terms of electrophoretic mobility and glycosylation from the proteins synthesized in simian virus 5-infected cells. In addition, the expressed F and HN proteins have been shown to be anchored in the plasma membrane in a biologically active form by indirect live cell immunofluorescence, the F-mediated formation of syncytia, and the ability of HN to cause the hemadsorption of erythrocytes to the infected cell surface.
Full text
PDFImages in this article
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Blok J., Air G. M., Laver W. G., Ward C. W., Lilley G. G., Woods E. F., Roxburgh C. M., Inglis A. S. Studies on the size, chemical composition, and partial sequence of the neuraminidase (NA) from type A influenza viruses show that the N-terminal region of the NA is not processed and serves to anchor the NA in the viral membrane. Virology. 1982 May;119(1):109–121. doi: 10.1016/0042-6822(82)90069-1. [DOI] [PubMed] [Google Scholar]
- Blumberg B. M., Giorgi C., Rose K., Kolakofsky D. Sequence determination of the Sendai virus fusion protein gene. J Gen Virol. 1985 Feb;66(Pt 2):317–331. doi: 10.1099/0022-1317-66-2-317. [DOI] [PubMed] [Google Scholar]
- Blumberg B., Giorgi C., Roux L., Raju R., Dowling P., Chollet A., Kolakofsky D. Sequence determination of the Sendai virus HN gene and its comparison to the influenza virus glycoproteins. Cell. 1985 May;41(1):269–278. doi: 10.1016/0092-8674(85)90080-7. [DOI] [PubMed] [Google Scholar]
- Bosch F. X., Garten W., Klenk H. D., Rott R. Proteolytic cleavage of influenza virus hemagglutinins: primary structure of the connecting peptide between HA1 and HA2 determines proteolytic cleavability and pathogenicity of Avian influenza viruses. Virology. 1981 Sep;113(2):725–735. doi: 10.1016/0042-6822(81)90201-4. [DOI] [PubMed] [Google Scholar]
- Collins P. L., Huang Y. T., Wertz G. W. Nucleotide sequence of the gene encoding the fusion (F) glycoprotein of human respiratory syncytial virus. Proc Natl Acad Sci U S A. 1984 Dec;81(24):7683–7687. doi: 10.1073/pnas.81.24.7683. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Dreyfuss G., Choi Y. D., Adam S. A. Characterization of heterogeneous nuclear RNA-protein complexes in vivo with monoclonal antibodies. Mol Cell Biol. 1984 Jun;4(6):1104–1114. doi: 10.1128/mcb.4.6.1104. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Fields S., Winter G., Brownlee G. G. Structure of the neuraminidase gene in human influenza virus A/PR/8/34. Nature. 1981 Mar 19;290(5803):213–217. doi: 10.1038/290213a0. [DOI] [PubMed] [Google Scholar]
- Florkiewicz R. Z., Rose J. K. A cell line expressing vesicular stomatitis virus glycoprotein fuses at low pH. Science. 1984 Aug 17;225(4663):721–723. doi: 10.1126/science.6087454. [DOI] [PubMed] [Google Scholar]
- Garten W., Bosch F. X., Linder D., Rott R., Klenk H. D. Proteolytic activation of the influenza virus hemagglutinin: The structure of the cleavage site and the enzymes involved in cleavage. Virology. 1981 Dec;115(2):361–374. doi: 10.1016/0042-6822(81)90117-3. [DOI] [PubMed] [Google Scholar]
- Gething M. J., White J. M., Waterfield M. D. Purification of the fusion protein of Sendai virus: analysis of the NH2-terminal sequence generated during precursor activation. Proc Natl Acad Sci U S A. 1978 Jun;75(6):2737–2740. doi: 10.1073/pnas.75.6.2737. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hiebert S. W., Paterson R. G., Lamb R. A. Hemagglutinin-neuraminidase protein of the paramyxovirus simian virus 5: nucleotide sequence of the mRNA predicts an N-terminal membrane anchor. J Virol. 1985 Apr;54(1):1–6. doi: 10.1128/jvi.54.1.1-6.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hiebert S. W., Paterson R. G., Lamb R. A. Identification and predicted sequence of a previously unrecognized small hydrophobic protein, SH, of the paramyxovirus simian virus 5. J Virol. 1985 Sep;55(3):744–751. doi: 10.1128/jvi.55.3.744-751.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Homma M., Ouchi M. Trypsin action on the growth of Sendai virus in tissue culture cells. 3. Structural difference of Sendai viruses grown in eggs and tissue culture cells. J Virol. 1973 Dec;12(6):1457–1465. doi: 10.1128/jvi.12.6.1457-1465.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hsu M. C., Scheid A., Choppin P. W. Reconstitution of membranes with individual paramyxovirus glycoproteins and phospholipid in cholate solution. Virology. 1979 Jun;95(2):476–491. doi: 10.1016/0042-6822(79)90502-6. [DOI] [PubMed] [Google Scholar]
- Hsu M., Choppin P. W. Analysis of Sendai virus mRNAs with cDNA clones of viral genes and sequences of biologically important regions of the fusion protein. Proc Natl Acad Sci U S A. 1984 Dec;81(24):7732–7736. doi: 10.1073/pnas.81.24.7732. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hsu M., Scheid A., Choppin P. W. Activation of the Sendai virus fusion protein (f) involves a conformational change with exposure of a new hydrophobic region. J Biol Chem. 1981 Apr 10;256(7):3557–3563. [PubMed] [Google Scholar]
- Kondor-Koch C., Burke B., Garoff H. Expression of Semliki Forest virus proteins from cloned complementary DNA. I. The fusion activity of the spike glycoprotein. J Cell Biol. 1983 Sep;97(3):644–651. doi: 10.1083/jcb.97.3.644. [DOI] [PMC free article] [PubMed] [Google Scholar]
- König M., Lai C. J. A general approach to construct double deletion mutants of SV40. Virology. 1979 Jul 15;96(1):277–280. doi: 10.1016/0042-6822(79)90193-4. [DOI] [PubMed] [Google Scholar]
- Lamb R. A., Etkind P. R., Choppin P. W. Evidence for a ninth influenza viral polypeptide. Virology. 1978 Nov;91(1):60–78. doi: 10.1016/0042-6822(78)90355-0. [DOI] [PubMed] [Google Scholar]
- Lamb R. A., Lai C. J. Expression of unspliced NS1 mRNA, spliced NS2 mRNA, and a spliced chimera mRNA from cloned influenza virus NS DNA in an SV40 vector. Virology. 1984 May;135(1):139–147. doi: 10.1016/0042-6822(84)90124-7. [DOI] [PubMed] [Google Scholar]
- Lopata M. A., Cleveland D. W., Sollner-Webb B. High level transient expression of a chloramphenicol acetyl transferase gene by DEAE-dextran mediated DNA transfection coupled with a dimethyl sulfoxide or glycerol shock treatment. Nucleic Acids Res. 1984 Jul 25;12(14):5707–5717. doi: 10.1093/nar/12.14.5707. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Markoff L., Lin B. C., Sveda M. M., Lai C. J. Glycosylation and surface expression of the influenza virus neuraminidase requires the N-terminal hydrophobic region. Mol Cell Biol. 1984 Jan;4(1):8–16. doi: 10.1128/mcb.4.1.8. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Merz D. C., Scheid A., Choppin P. W. Immunological studies of the functions of paramyxovirus glycoproteins. Virology. 1981 Feb;109(1):94–105. doi: 10.1016/0042-6822(81)90474-8. [DOI] [PubMed] [Google Scholar]
- Merz D. C., Scheid A., Choppin P. W. Importance of antibodies to the fusion glycoprotein of paramyxoviruses in the prevention of spread of infection. J Exp Med. 1980 Feb 1;151(2):275–288. doi: 10.1084/jem.151.2.275. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Nagai Y., Klenk H. D., Rott R. Proteolytic cleavage of the viral glycoproteins and its significance for the virulence of Newcastle disease virus. Virology. 1976 Jul 15;72(2):494–508. doi: 10.1016/0042-6822(76)90178-1. [DOI] [PubMed] [Google Scholar]
- Paterson R. G., Harris T. J., Lamb R. A. Analysis and gene assignment of mRNAs of a paramyxovirus, simian virus 5. Virology. 1984 Oct 30;138(2):310–323. doi: 10.1016/0042-6822(84)90354-4. [DOI] [PubMed] [Google Scholar]
- Paterson R. G., Harris T. J., Lamb R. A. Fusion protein of the paramyxovirus simian virus 5: nucleotide sequence of mRNA predicts a highly hydrophobic glycoprotein. Proc Natl Acad Sci U S A. 1984 Nov;81(21):6706–6710. doi: 10.1073/pnas.81.21.6706. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Peluso R. W., Lamb R. A., Choppin P. W. Polypeptide synthesis in simian virus 5-infected cells. J Virol. 1977 Jul;23(1):177–187. doi: 10.1128/jvi.23.1.177-187.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Pipas J. M., Peden K. W., Nathans D. Mutational analysis of simian virus 40 T antigen: isolation and characterization of mutants with deletions in the T-antigen gene. Mol Cell Biol. 1983 Feb;3(2):203–213. doi: 10.1128/mcb.3.2.203. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Portner A. The HN glycoprotein of Sendai virus: analysis of site(s) involved in hemagglutinating and neuraminidase activities. Virology. 1981 Dec;115(2):375–384. doi: 10.1016/0042-6822(81)90118-5. [DOI] [PubMed] [Google Scholar]
- Richardson C. D., Choppin P. W. Oligopeptides that specifically inhibit membrane fusion by paramyxoviruses: studies on the site of action. Virology. 1983 Dec;131(2):518–532. doi: 10.1016/0042-6822(83)90517-2. [DOI] [PubMed] [Google Scholar]
- Richardson C. D., Scheid A., Choppin P. W. Specific inhibition of paramyxovirus and myxovirus replication by oligopeptides with amino acid sequences similar to those at the N-termini of the F1 or HA2 viral polypeptides. Virology. 1980 Aug;105(1):205–222. doi: 10.1016/0042-6822(80)90168-3. [DOI] [PubMed] [Google Scholar]
- Riedel H., Kondor-Koch C., Garoff H. Cell surface expression of fusogenic vesicular stomatitis virus G protein from cloned cDNA. EMBO J. 1984 Jul;3(7):1477–1483. doi: 10.1002/j.1460-2075.1984.tb01999.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Roux L., Beffy P., Portner A. Restriction of cell surface expression of Sendai virus hemagglutinin-neuraminidase glycoprotein correlates with its higher instability in persistently and standard plus defective interfering virus infected BHK-21 cells. Virology. 1984 Oct 15;138(1):118–128. doi: 10.1016/0042-6822(84)90152-1. [DOI] [PubMed] [Google Scholar]
- Roux L., Waldvogel F. A. Defective interfering particles of Sendai virus modulate HN expression at the surface of infected BHK cells. Virology. 1983 Oct 15;130(1):91–104. doi: 10.1016/0042-6822(83)90120-4. [DOI] [PubMed] [Google Scholar]
- Scheid A., Caliguiri L. A., Compans R. W., Choppin P. W. Isolation of paramyxovirus glycoproteins. Association of both hemagglutinating and neuraminidase activities with the larger SV5 glycoprotein. Virology. 1972 Dec;50(3):640–652. doi: 10.1016/0042-6822(72)90418-7. [DOI] [PubMed] [Google Scholar]
- Scheid A., Choppin P. W. Identification of biological activities of paramyxovirus glycoproteins. Activation of cell fusion, hemolysis, and infectivity of proteolytic cleavage of an inactive precursor protein of Sendai virus. Virology. 1974 Feb;57(2):475–490. doi: 10.1016/0042-6822(74)90187-1. [DOI] [PubMed] [Google Scholar]
- Scheid A., Choppin P. W. The hemagglutinating and neuraminidase protein of a paramyxovirus: interaction with neuraminic acid in affinity chromatography. Virology. 1974 Nov;62(1):125–133. doi: 10.1016/0042-6822(74)90308-0. [DOI] [PubMed] [Google Scholar]
- Scheid A., Choppin P. W. Two disulfide-linked polypeptide chains constitute the active F protein of paramyxoviruses. Virology. 1977 Jul 1;80(1):54–66. doi: 10.1016/0042-6822(77)90380-4. [DOI] [PubMed] [Google Scholar]
- White J., Helenius A., Gething M. J. Haemagglutinin of influenza virus expressed from a cloned gene promotes membrane fusion. Nature. 1982 Dec 16;300(5893):658–659. doi: 10.1038/300658a0. [DOI] [PubMed] [Google Scholar]
- White J., Kielian M., Helenius A. Membrane fusion proteins of enveloped animal viruses. Q Rev Biophys. 1983 May;16(2):151–195. doi: 10.1017/s0033583500005072. [DOI] [PubMed] [Google Scholar]