Skip to main content
NCBI home page
Springer Nature - PMC COVID-19 Collection logoLink to Springer Nature - PMC COVID-19 Collection
. 1980;63(3):239–251. doi: 10.1007/BF01315030

Avian infectious bronchitis virus structural polypeptides: Effect of different conditions of disruption and comparison of different strains and isolates

M S Collins 1, D J Alexander 1
PMCID: PMC7086687  PMID: 6243925

Summary

Variations in the conditions used for disruption of purified virus involving differences in heat treatment and reducing agent concentration produced little affect on the polypeptide profiles of the Massachusetts 41 (M41) strain of avian infectious bronchitis virus obtained by polyacrylamide gel electrophoresis.

Comparisons of the structural polypeptides of 12 IBV isolates, consisting of M41, six serologically related viruses and representatives of five other serotypes, showed that the viruses could be placed in three groups on the molecular weights of the major glycopolypeptides. These were 31,000 and 86,000 for M41, the six related viruses and the serologically distinct SE17; 27,000 and 89,000 for Iowa 97 and Holte and 27,000 and 91,000 for Connecticut and T strain.

Keywords: Molecular Weight, Infectious Disease, Polypeptide, Polyacrylamide, Heat Treatment

Footnotes

With 7 Figures

References

  • 1.Alexander D. J. Comparison of the structural polypeptides of four avian paramyxoviruses. Arch. ges. Virusforsch. 1974;46:291–301. doi: 10.1007/BF01240071. [DOI] [PubMed] [Google Scholar]
  • 2.Alexander D. J., Collins M. S. The purification and polypeptide composition of avian infectious bronchitis virus. Microbios. 1977;18:87–98. [PubMed] [Google Scholar]
  • 3.Alexander D. J., Shortridge K. F., Collins M. S., Chettle N. J. Properties of a newly isolated, serologically distinct avian paramyxovirus. Arch. Virol. 1979;60:105–113. doi: 10.1007/BF01348026. [DOI] [PubMed] [Google Scholar]
  • 4.Bingham R. W. The polypeptide composition of avian infectious bronchitis virus. Arch. Virol. 1975;49:207–216. doi: 10.1007/BF01317539. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 5.Bracewell, C. D.: Antigenic relationships between strains of infectious bronchitis virus as shown by plaque reduction test in chick kidney cells. Proceedings Vth World Congress of the World Veterinary Poultry Association, Munich, 1973. 1975.
  • 6.Bracewell, C. D.: Serological studies of avian infectious bronchitis virus. Ph. D thesis, University of London, 1976.
  • 7.Collins M. S., Alexander D. J., Harkness J. W. Heterogeneity of infectious bronchitis virus grown in eggs. Arch. Virol. 1976;50:55–72. doi: 10.1007/BF01318001. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 8.Cowen B. S., Hitchner S. B. Serotyping of avian infectious bronchitis viruses by the virus-neutralization test. Avian Dis. 1975;19:583–595. [PubMed] [Google Scholar]
  • 9.Garwes D. J., Pocock D. H. The polypeptide structure of transmissible gastroenteritis virus. J. gen. Virol. 1975;29:25–34. doi: 10.1099/0022-1317-29-1-25. [DOI] [PubMed] [Google Scholar]
  • 10.Harkness J. W., Bracewell C. D. Morphological variation among avian infectious bronchitis virus strains. Res. vet. Sci. 1974;16:128–131. [PubMed] [Google Scholar]
  • 11.Hierholzer J. C. Purification and biophysical properties of human coronavirus 229E. Virology. 1976;75:155–165. doi: 10.1016/0042-6822(76)90014-3. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 12.Hierholzer J. C., Palmer E. L., Whitfield S. G., Kaye H. S., Dowdle W. R. Protein composition of coronavirus OC 43. Virology. 1972;48:516–527. doi: 10.1016/0042-6822(72)90062-1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 13.Hopkins S. R. Serological comparisons of strains of infectious bronchitis virus using plaque-purified isolants. Avian Dis. 1974;18:231–239. [PubMed] [Google Scholar]
  • 14.Lowry O. H., Rosebrough N. J., Farr A. L., Randall R. J. Protein measurement with the folin phenol reagent. J. biol. Chem. 1951;193:265–275. [PubMed] [Google Scholar]
  • 15.Macnaughton M. R., Madge M. H. The polypeptide composition of avian infectious bronchitis virus particles. Arch. Virol. 1977;55:47–54. doi: 10.1007/BF01314478. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 16.Macnaughton M. R., Madge M. H., Davies H. A., Dourmashkin R. R. Polypeptides of the surface projections and the ribonucleoprotein of avian infectious bronchitis virus. J. Virol. 1977;24:821–825. doi: 10.1128/jvi.24.3.821-825.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 17.Moore N. F., Burke C. D. Characterization of the strctural proteins of different strains of Newcastle disease virus. J. gen. Virol. 1974;25:275–289. doi: 10.1099/0022-1317-25-2-275. [DOI] [PubMed] [Google Scholar]
  • 18.Pocock D. H., Garwes D. J. The polypeptides of haemagglutinating encephalomyelitis virus and isolated subviral particles. J. gen. Virol. 1977;37:487–499. [Google Scholar]
  • 19.Robb, J. A., Bond, C. W.: Coronaviridae Comprehensive Virology14 (in press).
  • 20.Sturman L. S. Characterization of a coronavirus. 1. Structural proteins: Effects of preparative conditions on the migration of protein on polyacrylamide gels. Virology. 1977;77:637–649. doi: 10.1016/0042-6822(77)90488-3. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Archives of Virology are provided here courtesy of Nature Publishing Group

RESOURCES