Abstract
An enzymatically deficient recombinant S1 subunit, in which Arg-9 was replaced by Lys, was combined with native B oligomer to form a mutant holotoxin molecule. This molecule exhibited decreased leukocytosis-promoting and histamine-sensitizing activities compared with those of the native toxin, supporting the view that the B oligomer is not responsible for these activities. The protective activity of this genetically attenuated pertussis toxin was compared with that of B oligomer alone. The mutant pertussis toxin and B oligomer were similarly capable of protecting mice against a respiratory infection with Bordetella pertussis, suggesting that the B oligomer makes a significant contribution to the protection afforded by the genetically attenuated holotoxin.
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- Arciniega J. L., Burns D. L., Garcia-Ortigoza E., Manclark C. R. Immune response to the B oligomer of pertussis toxin. Infect Immun. 1987 May;55(5):1132–1136. doi: 10.1128/iai.55.5.1132-1136.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bartley T. D., Whiteley D. W., Mar V. L., Burns D. L., Burnette W. N. Pertussis holotoxoid formed in vitro with a genetically deactivated S1 subunit. Proc Natl Acad Sci U S A. 1989 Nov;86(21):8353–8357. doi: 10.1073/pnas.86.21.8353. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1006/abio.1976.9999. [DOI] [PubMed] [Google Scholar]
- Burnette W. N., Cieplak W., Mar V. L., Kaljot K. T., Sato H., Keith J. M. Pertussis toxin S1 mutant with reduced enzyme activity and a conserved protective epitope. Science. 1988 Oct 7;242(4875):72–74. doi: 10.1126/science.2459776. [DOI] [PubMed] [Google Scholar]
- Burnette W. N. The advent of recombinant pertussis vaccines. Biotechnology (N Y) 1990 Nov;8(11):1002–1005. doi: 10.1038/nbt1190-1002. [DOI] [PubMed] [Google Scholar]
- Burns D. L., Hausman S. Z., Lindner W., Robey F. A., Manclark C. R. Structural characterization of pertussis toxin A subunit. J Biol Chem. 1987 Dec 25;262(36):17677–17682. [PubMed] [Google Scholar]
- Gilman A. G. G proteins: transducers of receptor-generated signals. Annu Rev Biochem. 1987;56:615–649. doi: 10.1146/annurev.bi.56.070187.003151. [DOI] [PubMed] [Google Scholar]
- Hewlett E. L., Sauer K. T., Myers G. A., Cowell J. L., Guerrant R. L. Induction of a novel morphological response in Chinese hamster ovary cells by pertussis toxin. Infect Immun. 1983 Jun;40(3):1198–1203. doi: 10.1128/iai.40.3.1198-1203.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Katada T., Ui M. Direct modification of the membrane adenylate cyclase system by islet-activating protein due to ADP-ribosylation of a membrane protein. Proc Natl Acad Sci U S A. 1982 May;79(10):3129–3133. doi: 10.1073/pnas.79.10.3129. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kimura A., Mountzouros K. T., Schad P. A., Cieplak W., Cowell J. L. Pertussis toxin analog with reduced enzymatic and biological activities is a protective immunogen. Infect Immun. 1990 Oct;58(10):3337–3347. doi: 10.1128/iai.58.10.3337-3347.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 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]
- Nencioni L., Pizza M., Bugnoli M., De Magistris T., Di Tommaso A., Giovannoni F., Manetti R., Marsili I., Matteucci G., Nucci D. Characterization of genetically inactivated pertussis toxin mutants: candidates for a new vaccine against whooping cough. Infect Immun. 1990 May;58(5):1308–1315. doi: 10.1128/iai.58.5.1308-1315.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Nicosia A., Bartoloni A., Perugini M., Rappuoli R. Expression and immunological properties of the five subunits of pertussis toxin. Infect Immun. 1987 Apr;55(4):963–967. doi: 10.1128/iai.55.4.963-967.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Nogimori K., Tamura M., Yajima M., Ito K., Nakamura T., Kajikawa N., Maruyama Y., Ui M. Dual mechanisms involved in development of diverse biological activities of islet-activating protein, pertussis toxin, as revealed by chemical modification of lysine residues in the toxin molecule. Biochim Biophys Acta. 1984 Sep 28;801(2):232–243. doi: 10.1016/0304-4165(84)90072-2. [DOI] [PubMed] [Google Scholar]
- Oda M., Cowell J. L., Burstyn D. G., Manclark C. R. Protective activities of the filamentous hemagglutinin and the lymphocytosis-promoting factor of Bordetella pertussis in mice. J Infect Dis. 1984 Dec;150(6):823–833. doi: 10.1093/infdis/150.6.823. [DOI] [PubMed] [Google Scholar]
- Sato H., Ito A., Chiba J., Sato Y. Monoclonal antibody against pertussis toxin: effect on toxin activity and pertussis infections. Infect Immun. 1984 Nov;46(2):422–428. doi: 10.1128/iai.46.2.422-428.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sato Y., Izumiya K., Sato H., Cowell J. L., Manclark C. R. Role of antibody to leukocytosis-promoting factor hemagglutinin and to filamentous hemagglutinin in immunity to pertussis. Infect Immun. 1981 Mar;31(3):1223–1231. doi: 10.1128/iai.31.3.1223-1231.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Shahin R. D., Witvliet M. H., Manclark C. R. Mechanism of pertussis toxin B oligomer-mediated protection against Bordetella pertussis respiratory infection. Infect Immun. 1990 Dec;58(12):4063–4068. doi: 10.1128/iai.58.12.4063-4068.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tamura M., Nogimori K., Murai S., Yajima M., Ito K., Katada T., Ui M., Ishii S. Subunit structure of islet-activating protein, pertussis toxin, in conformity with the A-B model. Biochemistry. 1982 Oct 26;21(22):5516–5522. doi: 10.1021/bi00265a021. [DOI] [PubMed] [Google Scholar]
- Thomas M. G., Redhead K., Lambert H. P. Human serum antibody responses to Bordetella pertussis infection and pertussis vaccination. J Infect Dis. 1989 Feb;159(2):211–218. doi: 10.1093/infdis/159.2.211. [DOI] [PubMed] [Google Scholar]