Skip to main content
NCBI home page
Elsevier - PMC COVID-19 Collection logoLink to Elsevier - PMC COVID-19 Collection
. 2002 Nov 12;18(2):99–107. doi: 10.1016/0168-1702(91)90011-J

Localization of major neutralizing epitopes on the S1 polypeptide of the murine coronavirus peplomer glycoprotein

Takase-Yoden Sayaka 1, Kikuchi Tateki 1, Stuart G Siddell 2, Taguchi Fumihiro 1,∗
PMCID: PMC7133859  PMID: 1645909

Abstract

A recombinant baculovirus system has been used to express the amino terminal half of the murine coronavirus (JHMV) peplomer glycoprotein in insect cells. The expressed polypeptide is glycosylated and is recognized by a set of monoclonal antibodies (mAbs) specific for JHMV S protein. Three of these mAbs have a very high neutralizing activity for JHMV but not for other MHV strains. These results indicate that JHMV-specific, major neutralizing epitopes reside in the amino terminal S1 subunit of the peplomer glycoprotein.

Keywords: Murine coronavirus, Peplomer, Monoclonal antibody

References

  1. Banner L.R., Keck J.G., Lai M.M.C. A clustering of RNA recombination sites adjacent to a hypervariable region of the peplomer gene of murine coronavirus. Virology. 1990;175:548–555. doi: 10.1016/0042-6822(90)90439-X. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Cavanagh D., Davis P.J., Darbyshire J.H., Peter R.W. Coronavirus IBV: virus retaining spike glycopolypeptide S2 but not S1 is unable to induce virus-neutralizing or hemagglutination-in- hibiting antibody, or induce chicken tracheal protection. J. Gen. Virol. 1986;67:1435–1442. doi: 10.1099/0022-1317-67-7-1435. [DOI] [PubMed] [Google Scholar]
  3. Collins A.R., Knobler R.L., Powell H., Buchmeier M.J. Monoclonal antibodies to murine hepatitis virus-4 (strain JHM) define the viral glycoprotein responsible for attachment and cell-cell fusion. Virology. 1982;119:358–371. doi: 10.1016/0042-6822(82)90095-2. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Dalziel R.G., Lampert P.W., Talbot P.J., Buchmeier M.J. Site specific alteration of murine hepatitis virus type-4 (MHV-4) peplomer glycoprotein E2 results in reduced neurovirulence. J. Virol. 1986;59:463–471. doi: 10.1128/jvi.59.2.463-471.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Delmas B., Rasschaert D., Godet M., Gelfi J., Laude H. Four major antigenic sites of the coronavirus transmissible gastroenteritis virus are located on the amino-terminal half of spike glycoprotein S. J. Gen. Virol. 1990;71:1313–1323. doi: 10.1099/0022-1317-71-6-1313. [DOI] [PubMed] [Google Scholar]
  6. Frana M.F., Benhke J.N., Sturman L.S., Holmes K.V. Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: host-dependent differences in proteolytic cleavage and cell fusion. J.Virol. 1985;56:912–920. doi: 10.1128/jvi.56.3.912-920.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Fleming J.O., Trousdale M.D., El-Zaatari F.A., Stohlman S.A., Weiner L.P. Pathogenicity of antigenic variants of murine coronavirus JHM selected with monoclonal antibodies. J. Virol. 1986;58:869–875. doi: 10.1128/jvi.58.3.869-875.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Fleming J.O., Stohlman S.A., Harmon R.C., Lai M.M.C., Frelinger J.A., Weiner L.P. Antigenic relationships of murine coronaviruses: analysis using monoclonal antibodies to JHM(MHV-4) virus. Virology. 1983;131:296–307. doi: 10.1016/0042-6822(83)90498-1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Luytjes W., Geerts D., Posthumus W., Meloen R., Spaan W. Amino acid sequence of a conserved neutralizing epitope of murine coronaviruses. J. Virol. 1989;63:1408–1412. doi: 10.1128/jvi.63.3.1408-1412.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Luytjes W., Sturman L.S., Bredenbeek P.J., Charite J., Van der Zeijst B.A., Horzinek M.C., Spaan W.J. Primary structure of the glycoprotein E2 of coronavirus MHV-A59 and identification of the trypsin cleavage site. Virology. 1987;161:156–164. doi: 10.1016/0042-6822(87)90142-5. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Makino S., Fleming J.O., Keck J.G., Stohlman S.T., Lai M.M.C. Vol. 84. 1987. RNA recombination of coronaviruses: localization of neutralizing epitopes and neuropathogenic determinants on the carboxyl terminus of peplomers; pp. 6567–6571. (Proc. Natl. Acad. Sci.). [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Matsuura Y., Possee R.D., Bishop D.H.L. Expression of S-coded genes of lymphocytic choriomeningitis arenavirus using baculovirus vector. J. Gen. Virol. 1987;68:1233–1250. doi: 10.1099/0022-1317-67-8-1515. [DOI] [PubMed] [Google Scholar]
  13. Parker S.E., Gallagher T.M., Buchmeier M.J. Sequence analysis reveals extensive polymorphism and evidence of deletions within E2 glycoprotein gene of several strains of murine hepatitis virus. Virology. 1989;173:664–673. doi: 10.1016/0042-6822(89)90579-5. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Schmidt I., Skinner M., Siddell S.G. Nucleotide sequence of the gene encoding the surface projection glycoprotein of coronavirus MHV-JHM. J. Gen. Virol. 1987;68:47–56. doi: 10.1099/0022-1317-68-1-47. [DOI] [PubMed] [Google Scholar]
  15. Siddell S.G., Stauber R., Routledge E., Pfleiderer M. Functional analysis of coronavirus MHV-JHM surface glycoproteins. In: Brinton M.A., Heinz F.X., editors. New Aspects of Positive Strand RNA Viruses. ASM Press; Washington: 1990. pp. 287–293. [Google Scholar]
  16. Sturman L.S., Ricard C.S., Holmes K.V. Proteolytic cleavage of the E2 glycoprotein of murine coronavirus: activation of cell-fusion activity of virions by trypsin and separation of two different 90 K cleavage fragments. J. Virol. 1985;56:904–911. doi: 10.1128/jvi.56.3.904-911.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Taguchi F., Fleming J.O. Comparison of six different coronavirus JHM variants by monoclonal antibodies against the E2 glycoprotein. Virology. 1989;169:233–235. doi: 10.1016/0042-6822(89)90061-5. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Taguchi F., Makino S., Fujiwara K. Antigenic differentiation of mouse hepatitis viruses by neutralization test. Microbiol. Immunol. 1982;26:741–745. doi: 10.1111/j.1348-0421.1982.tb00218.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Taguchi F., Siddell S.G., Wege H., ter Meulen V. Characterization of a variant virus selected in rat brains after infection by coronavirus mouse hepatitis virus JHM. J. Virol. 1985;54:429–435. doi: 10.1128/jvi.54.2.429-435.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Taguchi F., Yamada A., Fujiwara K. Resistance to highly virulent mouse hepatitis virus acquired by mice after low-virulence infection: enhanced antiviral activity of macrophages. Infect. Immun. 1980;29:42–49. doi: 10.1128/iai.29.1.42-49.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Vennema H., Heijenen L., Zijderveld A., Horzinek M.C., Spaan W.J.M. Intracellular transport of recombinant coronavirus spike proteins: implication for virus assembly. J. Virol. 1990;64:339–346. doi: 10.1128/jvi.64.1.339-346.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Wege H., Dorries R., Wege H. Hybridoma antibodies to the murine coronavirus JHM: Characterization of epitopes on the peplomer protein (E2) J. Gen. Virol. 1984;65:1931–1942. doi: 10.1099/0022-1317-65-11-1931. [DOI] [PubMed] [Google Scholar]
  23. Wege H., Winter J., Meyermann R. The peplomer glycoprotein E2 of coronavirus JHM as a determinant of neurovirulence: definition of critical epitopes by variant analysis. J. Gen. Virol. 1988;69:87–98. doi: 10.1099/0022-1317-69-1-87. [DOI] [PubMed] [Google Scholar]
  24. Weismiller D.G., Sturman L.S., Buchmeier M.J., Fleming J.O., Holmes K.V. Monoclonal antibodies to the peplomer glycoprotein of coronavirus mouse hepatitis virus identify two subunits and detect a conformational change in the subunit released under mild alkaline conditions. J. Virol. 1990;64:3051–3055. doi: 10.1128/jvi.64.6.3051-3055.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Yoden S., Kikuchi T., Siddell S.G., Taguchi F. Expression of the peplomer glycoprotein of murine coronavirus JHM using a baculovirus vector. Virology. 1989;173:615–623. doi: 10.1016/0042-6822(89)90573-4. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Virus Research are provided here courtesy of Elsevier

RESOURCES