Abstract
The structure and biological properties of solubilized envelope proteins of Bordetella pertussis have been examined. Several envelope proteins were found to be specific for phase I strains of B. pertussis and could be isolated by selective detergent extraction. These proteins had molecular weights of 90,000, 86,000, 81,000, 33,000, 31,000, and 30,000 and were reduced or absent in envelope preparations from Bordetella bronchiseptica, Bordetella parapertussis, or phase IV strains of B. pertussis. When the envelope preparations from phase I B. pertussis were assayed in the mouse intracerebral protection test they were found to be highly protective, and there was a strong correlation between the protective potency and the lymphocytosis-promoting factor (LPF) content of different preparations. Treatment with glutaraldehyde reduced the LPF activity, toxicity, and protective potency of the envelope extracts. Similarly affinity chromatography of envelope proteins on columns of haptoglobin coupled to Sepharose 4B reduced both the LPF content and the protective potency. The addition of a small amount of purified LPF to the haptoglobin-treated proteins restored the protective potency. The LPF by itself was nonprotective, indicating a potentiating role of LPF in the mouse intracerebral challenge test.
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Selected References
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- Arai H., Munoz J. J. Fimbrial hemagglutinin in stationary and shake cultures of Bordetella pertussis. Infect Immun. 1979 Aug;25(2):764–767. doi: 10.1128/iai.25.2.764-767.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Arai H., Sato Y. Separation and characterization of two distinct hemagglutinins contained in purified leukocytosis-promoting factor from Bordetella pertussis. Biochim Biophys Acta. 1976 Oct 22;444(3):765–782. doi: 10.1016/0304-4165(76)90323-8. [DOI] [PubMed] [Google Scholar]
- Ashworth L. A., Fitzgeorge R. B., Irons L. I., Morgan C. P., Robinson A. Rabbit nasopharyngeal colonization by Bordetella pertussis: the effects of immunization on clearance and on serum and nasal antibody levels. J Hyg (Lond) 1982 Jun;88(3):475–486. doi: 10.1017/s0022172400070339. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 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]
- Beher M. G., Schnaitman C. A., Pugsley A. P. Major heat-modifiable outer membrane protein in gram-negative bacteria: comparison with the ompA protein of Escherichia coli. J Bacteriol. 1980 Aug;143(2):906–913. doi: 10.1128/jb.143.2.906-913.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ezzell J. W., Dobrogosz W. J., Kloos W. E., Manclark C. R. Phase-shift markers in Bordetella: alterations in envelope proteins. J Infect Dis. 1981 Apr;143(4):562–569. doi: 10.1093/infdis/143.4.562. [DOI] [PubMed] [Google Scholar]
- Fairbanks G., Steck T. L., Wallach D. F. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry. 1971 Jun 22;10(13):2606–2617. doi: 10.1021/bi00789a030. [DOI] [PubMed] [Google Scholar]
- 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]
- Guymon L. F., Walstad D. L., Sparling P. F. Cell envelope alterations in antibiotic-sensitive and-resistant strains of Neisseria gonorrhoeae. J Bacteriol. 1978 Oct;136(1):391–401. doi: 10.1128/jb.136.1.391-401.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Irons L. I., MacLennan A. P. Isolation of the lymphocytosis promoting factor-haemagglutinin of Bordetella pertussis by affinity chromatography. Biochim Biophys Acta. 1979 Sep 29;580(1):175–185. doi: 10.1016/0005-2795(79)90208-3. [DOI] [PubMed] [Google Scholar]
- Kendrick P. L., Eldering G., Dixon M. K., Misner J. Mouse Protection Tests in the Study of Pertussis Vaccine: A Comparative Series Using the Intracerebral Route for Challenge. Am J Public Health Nations Health. 1947 Jul;37(7):803–810. [PMC free article] [PubMed] [Google Scholar]
- Lambden P. R., Heckels J. E., James L. T., Watt P. J. Variations in surface protein composition associated with virulence properties in opacity types of Neisseria gonorrhoeae. J Gen Microbiol. 1979 Oct;114(2):305–312. doi: 10.1099/00221287-114-2-305. [DOI] [PubMed] [Google Scholar]
- Lane A. G. Use of glutamic acid to supplement fluid medium for cultivation of Bordetella pertussis. Appl Microbiol. 1970 Mar;19(3):512–520. doi: 10.1128/am.19.3.512-520.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Morse S. I., Morse J. H. Isolation and properties of the leukocytosis- and lymphocytosis-promoting factor of Bordetella pertussis. J Exp Med. 1976 Jun 1;143(6):1483–1502. doi: 10.1084/jem.143.6.1483. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Munoz J. J., Arai H., Bergman R. K., Sadowski P. L. Biological activities of crystalline pertussigen from Bordetella pertussis. Infect Immun. 1981 Sep;33(3):820–826. doi: 10.1128/iai.33.3.820-826.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Munoz J. J., Arai H., Cole R. L. Mouse-protecting and histamine-sensitizing activities of pertussigen and fimbrial hemagglutinin from Bordetella pertussis. Infect Immun. 1981 Apr;32(1):243–250. doi: 10.1128/iai.32.1.243-250.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Osborn M. J., Wu H. C. Proteins of the outer membrane of gram-negative bacteria. Annu Rev Microbiol. 1980;34:369–422. doi: 10.1146/annurev.mi.34.100180.002101. [DOI] [PubMed] [Google Scholar]
- Parton R., Wardlaw A. C. Cell-envelope proteins of Bordetella pertussis. J Med Microbiol. 1975 Feb;8(1):47–57. doi: 10.1099/00222615-8-1-47. [DOI] [PubMed] [Google Scholar]
- Sato Y., Arai H., Suzuki K. Leukocytosis-promoting factor of Bordetella pertussis. 3. Its identity with protective antigen. Infect Immun. 1974 May;9(5):801–810. doi: 10.1128/iai.9.5.801-810.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tsai C. M., Frasch C. E. Chemical analysis of major outer membrane proteins of Neisseria meningitidis: comparison of serotypes 2 and 11. J Bacteriol. 1980 Jan;141(1):169–176. doi: 10.1128/jb.141.1.169-176.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]