Skip to main content
PMC home page
Infection and Immunity logoLink to Infection and Immunity
. 1983 Oct;42(1):276–284. doi: 10.1128/iai.42.1.276-284.1983

Identification and characterization of Campylobacter jejuni outer membrane proteins.

M J Blaser, J A Hopkins, R M Berka, M L Vasil, W L Wang
PMCID: PMC264555  PMID: 6618667

Abstract

Outer membrane proteins from isolates of Campylobacter jejuni were examined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Sarcosinate-insoluble membrane preparations were outer membrane enriched based on increased ketodeoxyoctonate concentrations, the presence of surface-exposed 125I-labeled proteins that were hydrophobic, and similarity to membrane vesicle (bleb) sodium dodecyl sulfate-polyacrylamide gel electrophoresis profiles. Most isolates contained a single major band with molecular weight of 41,000 to 45,000. Profiles of C. jejuni and Campylobacter coli isolates were indistinguishable, but either could be easily differentiated from Campylobacter fetus and Campylobacter faecalis. The profiles were stable for strains under a variety of growth, incubation and passage conditions. We classified 110 isolates from patients with sporadic campylobacter enteritis into nine subtypes based on differences in outer membrane sodium dodecyl sulfate-polyacrylamide gel electrophoresis profiles. Two categories accounted for 76% of the isolates. Complete concordance was observed in subtypes of strains obtained from epidemiologically related cases. Thus, comparison of the major outer membrane proteins of C. jejuni is a useful technique for investigating the transmission of this organism and may provide a basis for immunological characterization of the outer membrane proteins.

Full text

PDF

Images in this article

278Image
on p.278
278Image
on p.278
279Image
on p.279
279Image
on p.279
280Image
on p.280
281Image
on p.281
281Image
on p.281
282Image
on p.282
282Image
on p.282

Selected References

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

  1. Alphen W. V., Lugtenberg B. Influence of osmolarity of the growth medium on the outer membrane protein pattern of Escherichia coli. J Bacteriol. 1977 Aug;131(2):623–630. doi: 10.1128/jb.131.2.623-630.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Ames G. F. Resolution of bacterial proteins by polyacrylamide gel electrophoresis on slabs. Membrane, soluble, and periplasmic fractions. J Biol Chem. 1974 Jan 25;249(2):634–644. [PubMed] [Google Scholar]
  3. Barenkamp S. J., Munson R. S., Jr, Granoff D. M. Subtyping isolates of Haemophilus influenzae type b by outer-membrane protein profiles. J Infect Dis. 1981 May;143(5):668–676. doi: 10.1093/infdis/143.5.668. [DOI] [PubMed] [Google Scholar]
  4. Blaser M. J., Checko P., Bopp C., Bruce A., Hughes J. M. Campylobacter enteritis associated with foodborne transmission. Am J Epidemiol. 1982 Dec;116(6):886–894. doi: 10.1093/oxfordjournals.aje.a113491. [DOI] [PubMed] [Google Scholar]
  5. Blaser M. J., Penner J. L., Wells J. G. Diversity of serotypes in outbreaks of enteritis due to Campylobacter jejuni. J Infect Dis. 1982 Dec;146(6):826–826. doi: 10.1093/infdis/146.6.826. [DOI] [PubMed] [Google Scholar]
  6. Blaser M. J., Reller L. B. Campylobacter enteritis. N Engl J Med. 1981 Dec 10;305(24):1444–1452. doi: 10.1056/NEJM198112103052404. [DOI] [PubMed] [Google Scholar]
  7. Blaser M. J., Reller L. B., Luechtefeld N. W., Wang W. L. Campylobacter enteritis in Denver. West J Med. 1982 Apr;136(4):287–290. [PMC free article] [PubMed] [Google Scholar]
  8. Buchanan T. M., Hildebrandt J. F. Antigen-specific serotyping of Neisseria gonorrhoeae: characterization based upon principal outer membrane protein. Infect Immun. 1981 Jun;32(3):985–994. doi: 10.1128/iai.32.3.985-994.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Devoe I. W., Gilchrist J. E. Release of endotoxin in the form of cell wall blebs during in vitro growth of Neisseria meningitidis. J Exp Med. 1973 Nov 1;138(5):1156–1167. doi: 10.1084/jem.138.5.1156. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. DiRienzo J. M., Nakamura K., Inouye M. The outer membrane proteins of Gram-negative bacteria: biosynthesis, assembly, and functions. Annu Rev Biochem. 1978;47:481–532. doi: 10.1146/annurev.bi.47.070178.002405. [DOI] [PubMed] [Google Scholar]
  11. Filip C., Fletcher G., Wulff J. L., Earhart C. F. Solubilization of the cytoplasmic membrane of Escherichia coli by the ionic detergent sodium-lauryl sarcosinate. J Bacteriol. 1973 Sep;115(3):717–722. doi: 10.1128/jb.115.3.717-722.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Hansen E. J., Frisch C. F., McDade R. L., Jr, Johnston K. H. Identification of immunogenic outer membrane proteins of Haemophilus influenzae type b in the infant rat model system. Infect Immun. 1981 Jun;32(3):1084–1092. doi: 10.1128/iai.32.3.1084-1092.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Hébert G. A., Hollis D. G., Weaver R. E., Lambert M. A., Blaser M. J., Moss C. W. 30 years of campylobacters: biochemical characteristics and a biotyping proposal for Campylobacter jejuni. J Clin Microbiol. 1982 Jun;15(6):1065–1073. doi: 10.1128/jcm.15.6.1065-1073.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Kelley J. T., Parker C. D. Identification and preliminary characterization of Vibrio cholerae outer membrane proteins. J Bacteriol. 1981 Feb;145(2):1018–1024. doi: 10.1128/jb.145.2.1018-1024.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Loeb M. R., Smith D. H. Outer membrane protein composition in disease isolates of Haemophilus influenzae: pathogenic and epidemiological implications. Infect Immun. 1980 Dec;30(3):709–717. doi: 10.1128/iai.30.3.709-717.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Logan S. M., Trust T. J. Outer membrane characteristics of Campylobacter jejuni. Infect Immun. 1982 Dec;38(3):898–906. doi: 10.1128/iai.38.3.898-906.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Markwell M. A., Haas S. M., Bieber L. L., Tolbert N. E. A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples. Anal Biochem. 1978 Jun 15;87(1):206–210. doi: 10.1016/0003-2697(78)90586-9. [DOI] [PubMed] [Google Scholar]
  18. Matsushita K., Adachi O., Shinagawa E., Ameyama M. Isolation and characterization of outer and inner membranes from Pseudomonas aeruginosa and effect of EDTA on the membranes. J Biochem. 1978 Jan;83(1):171–181. doi: 10.1093/oxfordjournals.jbchem.a131888. [DOI] [PubMed] [Google Scholar]
  19. McCoy E. C., Wiltberger H. A., Winter J. Major outer membrane protein of Campylobacter fetus: physical and immunological characterization. Infect Immun. 1976 Apr;13(4):1258–1265. doi: 10.1128/iai.13.4.1258-1265.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Mizuno T., Kageyama M. Separation and characterization of the outer membrane of Pseudomonas aeruginosa. J Biochem. 1978 Jul;84(1):179–191. doi: 10.1093/oxfordjournals.jbchem.a132106. [DOI] [PubMed] [Google Scholar]
  21. Mocca L. F., Frasch C. E. Sodium dodecyl sulfate-polyacrylamide gel typing system for characterization of Neisseria meningitidis isolates. J Clin Microbiol. 1982 Aug;16(2):240–244. doi: 10.1128/jcm.16.2.240-244.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Munford R. S., Hall C. L., Rick P. D. Size heterogeneity of Salmonella typhimurium lipopolysaccharides in outer membranes and culture supernatant membrane fragments. J Bacteriol. 1980 Nov;144(2):630–640. doi: 10.1128/jb.144.2.630-640.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Munford R. S., Patton C. M., Gorman G. W. Epidemiologic studies of serotype antigens common to groups B and C Neisseria meningitidis. J Infect Dis. 1975 Mar;131(3):286–290. doi: 10.1093/infdis/131.3.286. [DOI] [PubMed] [Google Scholar]
  24. Oakley B. R., Kirsch D. R., Morris N. R. A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels. Anal Biochem. 1980 Jul 1;105(2):361–363. doi: 10.1016/0003-2697(80)90470-4. [DOI] [PubMed] [Google Scholar]
  25. Ohman D. E., Sadoff J. C., Iglewski B. H. Toxin A-deficient mutants of Pseudomonas aeruginosa PA103: isolation and characterization. Infect Immun. 1980 Jun;28(3):899–908. doi: 10.1128/iai.28.3.899-908.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Osborn M. J., Gander J. E., Parisi E., Carson J. Mechanism of assembly of the outer membrane of Salmonella typhimurium. Isolation and characterization of cytoplasmic and outer membrane. J Biol Chem. 1972 Jun 25;247(12):3962–3972. [PubMed] [Google Scholar]
  27. Penner J. L., Hennessy J. N. Passive hemagglutination technique for serotyping Campylobacter fetus subsp. jejuni on the basis of soluble heat-stable antigens. J Clin Microbiol. 1980 Dec;12(6):732–737. doi: 10.1128/jcm.12.6.732-737.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Pike R. M., Chandler C. H. Partial purification and properties of somatic antigen spontaneously released from Vibrio cholerae. Infect Immun. 1975 Jul;12(1):187–192. doi: 10.1128/iai.12.1.187-192.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Swanson J. Surface-exposed protein antigens of the gonococcal outer membrane. Infect Immun. 1981 Dec;34(3):804–816. doi: 10.1128/iai.34.3.804-816.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Tsai C. M., Frasch C. E. A sensitive silver stain for detecting lipopolysaccharides in polyacrylamide gels. Anal Biochem. 1982 Jan 1;119(1):115–119. doi: 10.1016/0003-2697(82)90673-x. [DOI] [PubMed] [Google Scholar]

Articles from Infection and Immunity are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES