Abstract
Monoclonal antibodies have proved to be highly specific tools for defining the antigenic epitopes of Pseudomonas aeruginosa outer membrane macromolecules. In this article we have highlighted the use of monoclonal antibodies in the study of lipopolysaccharide heterogeneity and in particular have demonstrated that single monoclonal antibodies can recognize epitopes on lipid A which are conserved in all Gram negative bacteria tested. Monoclonal antibodies against P. aeruginosa outer membrane proteins have been used to demonstrate the strong conservation of specific antigenic sites in all P. aeruginosa strains tested. In the case of one monoclonal antibody, specific for outer membrane lipoprotein H2, the antigenic site recognized by the antibody was also found to be conserved in all group 1 Pseudomonads. The implications of these monoclonal antibodies to bacterial taxonomy is discussed. Monoclonal antibodies against two separate conserved surface epitopes on outer membrane protein F were isolated and differentiated according to their reactions with 2 mercaptoethanol-reduced protein F and with proteolytic and cyanogen bromide peptide fragments of protein F.. One of these protein F-specific monoclonal antibodies has been demonstrated to have immunotherapeutic potential.
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References
Bradley, S.G. 1979. Cellular and molecular mechanisms of action of bacterial endotoxins. Annu. Rev. Microbiol. 33: 67.
Darveau, R.P., and Hancock, R.E.W. 1983. Procedure for the isolation of bacterial lipopolysaccharides from both smooth and rough Pseudomonas aeruginosa and Salmonella typhimurum strains. J. Bacteriol. 155: 831.
DeVos, P., and J. DeLey. 1983. Intra- and intergenic similarities of Pseudomonas and Xanthromonas ribosomal ribonucleic acid cistrons. Int. J. Systemat. Bacteriol. 33: 487.
Hancock, R.E.W., Mutharia, L.M., Chan, L., Darveau, R.P., Speert, D.P. and Pier, G.B. 1983. Pseudomonas aeruginosa isolates from patients with cystic fibrosis: A class of serum sensitive, nontypable strains deficient in lipopolysaccharide 0 side chains. Infect. Immun. 42, 170.
Hancock, R.E.W., Wieczorec, A.A., Mutharia, L.M., and Poole, K. 1982. Monoclonal antibodies against Pseudomonas aeruginosa outer membrane antigens: Isolation and characterization. Infect. Immun. 37: 166.
Lam, J.S., Mutharia, L.M., Hancock, R.E.W., Hoiby, N., Lam, K., Belk, L. and Costerton, J.W. 1983. Immunogenicity of Pseudomonas aeruginosa outer membrane antigens examined by crossed immunoelectrophoresis. Infect. Immun. 42: 88.
Moss, C.W., Samuels, S.B., and Weaver, R.E. 1972. Cellular fatty acid composition of selected Pseudomonas species. Appl. Microbiol. 24: 596.
Mutharia, L.M., Crockford, G., Bogard, W.C., and Hancock, R.E.W. 1984. Monoclonal antibodies specific for Escherichia coli J-5 lipopolysaccharide: Cross reaction with other Gram negative bacterial species. Infect. Immun., in press.
Mutharia, L.M. and Hancock, R.E.W. 1983. Surface localization of Pseudomonas aeruginosa outer membrane porin proten F by using monoclonal antibodies. Infect. Immun. 42: 1027.
Mutharia, L.M., Nicas, T.I., Hancock, R.E.W. 1982. Outer membrane proteins of Pseudomonas aeruginosa serotype strains. J. Infect. Dis. 146: 770.
Nikaido, H., and Nakae, T. 1979. The outer membrane of Gram negative bacteria. Adv. Microb. Physiol. 19: 163.
Palleroni, N.J., Ballard, R.W., Ralston, E., and Doudoroff, M. 1973. Nucleic acid homologies in the genus Pseudomonas. Int. J. Systemat. Bacteriol. 23: 333.
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© 1985 Plenum Press, New York
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Hancock, R.E.W., Mutharia, L.M. (1985). Monoclonal Antibodies Against Bacterial Outer Membrane Antigens. In: Atassi, M.Z., Bachrach, H.L. (eds) Immunobiology of Proteins and Peptides—III. Advances in Experimental Medicine and Biology, vol 185. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-7974-4_14
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DOI: https://doi.org/10.1007/978-1-4684-7974-4_14
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