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. 1982 Feb;35(2):515–522. doi: 10.1128/iai.35.2.515-522.1982

Polypeptides and functions of antigens from human coronaviruses 229E and OC43.

O W Schmidt, G E Kenny
PMCID: PMC351070  PMID: 6173324

Abstract

Coronaviruses possess three major size classes of polypeptides as judged by molecular weight: approximately 180,000, approximately 50,000, and approximately 23,000. Human coronaviruses 229E and OC43 possess not only three similar size classes of polypeptides but also three distinct antigens, none of which cross-react with the heterologous strain. Polypeptides separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis were reacted in rocket immunoelectrophoresis with antiserum monospecific to each of the three strain-specific antigens (excised precipitin lines from crossed immunoelectrophoresis profiles were used for immunogens). Monospecific antiserum with neutralizing ability reacted with a polypeptide of 186,000 daltons for 229E and a polypeptide of 190,000 daltons for OC43. The antigen which elicited neutralizing antibody response was located at the surface, associated with the corona of the virion, glycosylated, and bound by concanavalin A. Another less prominent surface antigen was represented by size classes of 23,000 daltons for 229E and 24,000 for OC43. The core antigens of the viruses had molecular weights of 49,000 and 229E and 52,000 and OC43 virus. Thus, the molecular weights and functions of the antigens of human coronaviruses are similar to those of animal coronaviruses. The polypeptides of coronaviruses 229E and OC43 are nearly identical as judged by molecular weight, but the similar polypeptides of the two viruses represent different immunological specificities.

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Selected References

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

  1. Alexander A. G., Kenny G. E. Application of charge shift electrophoresis to antigenic analysis of mycoplasmic membranes by two-dimensional (crossed) immunoelectrophoresis. Infect Immun. 1978 Jun;20(3):861–863. doi: 10.1128/iai.20.3.861-863.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Alexander A. G., Kenny G. E. Characterization of membrane and cytoplasmic antigens of Mycoplasma arginini by two-dimensional (crossed) immunoelectrophoresis. Infect Immun. 1977 Jan;15(1):313–321. doi: 10.1128/iai.15.1.313-321.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bhakdi S., Bhakdi-Lehnen B., Bjerrum O. J. Detection of amphiphilic proteins and peptides in complex mixtures. Charge-shift crossed immunoelectrophoresis and two-dimensional charge-shift electrophoresis. Biochim Biophys Acta. 1977 Oct 3;470(1):35–44. doi: 10.1016/0005-2736(77)90059-1. [DOI] [PubMed] [Google Scholar]
  4. Bohac J., Derbyshire J. B. The demonstration of transmissible gastroenteritis viral antigens by immunoelectrophoresis and counterimmunoelectrophoresis. Can J Microbiol. 1975 Jun;21(6):750–753. doi: 10.1139/m75-111. [DOI] [PubMed] [Google Scholar]
  5. Bradburne A. F. Antigenic relationships amongst coronaviruses. Arch Gesamte Virusforsch. 1970;31(3):352–364. doi: 10.1007/BF01253769. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Caldwell H. D., Kuo C. C. Purification of a Chlamydia trachomatis-specific antigen by immunoadsorption with monospecific antibody. J Immunol. 1977 Feb;118(2):437–441. [PubMed] [Google Scholar]
  7. Compans R. W., Klenk H. D., Caliguiri L. A., Choppin P. W. Influenza virus proteins. I. Analysis of polypeptides of the virion and identification of spike glycoproteins. Virology. 1970 Dec;42(4):880–889. doi: 10.1016/0042-6822(70)90337-5. [DOI] [PubMed] [Google Scholar]
  8. Garwes D. J., Pocock D. H., Pike B. V. Isolation of subviral components from transmissible gastroenteritis virus. J Gen Virol. 1976 Aug;32(2):283–294. doi: 10.1099/0022-1317-32-2-283. [DOI] [PubMed] [Google Scholar]
  9. Garwes D. J., Pocock D. H. The polypeptide structure of transmissible gastroenteritis virus. J Gen Virol. 1975 Oct;29(1):25–34. doi: 10.1099/0022-1317-29-1-25. [DOI] [PubMed] [Google Scholar]
  10. Helenius A., Simons K. Charge shift electrophoresis: simple method for distinguishing between amphiphilic and hydrophilic proteins in detergent solution. Proc Natl Acad Sci U S A. 1977 Feb;74(2):529–532. doi: 10.1073/pnas.74.2.529. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Hierholzer J. C., Palmer E. L., Whitfield S. G., Kaye H. S., Dowdle W. R. Protein composition of coronavirus OC 43. Virology. 1972 May;48(2):516–527. doi: 10.1016/0042-6822(72)90062-1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Hierholzer J. C. Purification and biophysical properties of human coronavirus 229E. Virology. 1976 Nov;75(1):155–165. doi: 10.1016/0042-6822(76)90014-3. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  14. 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]
  15. Macnaughton M. R., Madge M. H. The polypeptide composition of avain infectious bronchitis virus particles. Arch Virol. 1977;55(1-2):47–54. doi: 10.1007/BF01314478. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Macnaughton M. R. The polypeptides of human and mouse coronaviruses. Brief report. Arch Virol. 1980;63(1):75–80. doi: 10.1007/BF01320763. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. McIntosh K., Kapikian A. Z., Hardison K. A., Hartley J. W., Chanock R. M. Antigenic relationships among the coronaviruses of man and between human and animal coronaviruses. J Immunol. 1969 May;102(5):1109–1118. [PubMed] [Google Scholar]
  18. Schmidt O. W., Cooney M. K., Kenny G. E. Plaque assay and improved yield of human coronaviruses in a human rhabdomyosarcoma cell line. J Clin Microbiol. 1979 Jun;9(6):722–728. doi: 10.1128/jcm.9.6.722-728.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Schmidt O. W., Kenny G. E. Immunogenicity and antigenicity of human coronaviruses 229E and OC43. Infect Immun. 1981 Jun;32(3):1000–1006. doi: 10.1128/iai.32.3.1000-1006.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. 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]
  21. Sturman L. S., Holmes K. V., Behnke J. Isolation of coronavirus envelope glycoproteins and interaction with the viral nucleocapsid. J Virol. 1980 Jan;33(1):449–462. doi: 10.1128/jvi.33.1.449-462.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Sturman L. S., Holmes K. V. Characterization of coronavirus II. Glycoproteins of the viral envelope: tryptic peptide analysis. Virology. 1977 Apr;77(2):650–660. doi: 10.1016/0042-6822(77)90489-5. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Sturman L. S. I. Structural proteins: effects of preparative conditions on the migration of protein in polyacrylamide gels. Virology. 1977 Apr;77(2):637–649. doi: 10.1016/0042-6822(77)90488-3. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Tyrrell D. A., Alexander D. J., Almeida J. D., Cunningham C. H., Easterday B. C., Garwes D. J., Hierholzer J. C., Kapikian A., Macnaughton M. R., McIntosh K. Coronaviridae: second report. Intervirology. 1978;10(6):321–328. doi: 10.1159/000148996. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Wardi A. H., Michos G. A. Alcian blue staining of glycoproteins in acrylamide disc electrophoresis. Anal Biochem. 1972 Oct;49(2):607–609. doi: 10.1016/0003-2697(72)90472-1. [DOI] [PubMed] [Google Scholar]

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