Abstract

It is planned to produce hybridoma lines producing monoclonal antibodies to four gonococcal surface antigens of great importance in pathogenesis. The reactivity of a number of antibodies to pili will be related to the primary structure of this protein, and the ability to inhibit adhesive properties will be determined in order to locate the receptor site within the pilin molecule. Similarly, the determinants seen by monoclonal antibodies to proteins I will be correlated with the primary sequence, and their ability to mediate opsonization, complement dependent bacteriolysis and translocation to eukaryotic membranes. Antibodies will be developed to protein III, a constant antigen present in all gonococci, and their capacity to opsonize and to promote or block bacteriolysis determined. Lastly, antibodies to IgA proteases will be developed, with the particular intent to find clones inactivating the enzyme. Once these are available they will be used to determine if it is possible to identify the active site by immunochemical techniques. The goal is to design an immunizing agent favoring the production of inactivating antibodies.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Research Project (R01)
Project #
2R01AI019469-04
Application #
3128801
Study Section
Bacteriology and Mycology Subcommittee 1 (BM)
Project Start
1982-02-01
Project End
1988-08-31
Budget Start
1986-09-30
Budget End
1987-08-31
Support Year
4
Fiscal Year
1986
Total Cost
Indirect Cost

  Institution

Name
Rockefeller University
Department
Type
Graduate Schools
DUNS #
071037113
City
New York
State
NY
Country
United States
Zip Code
10065

  Publications

Apicella, M A; Ketterer, M; Lee, F K et al. (1996) The pathogenesis of gonococcal urethritis in men: confocal and immunoelectron microscopic analysis of urethral exudates from men infected with Neisseria gonorrhoeae. J Infect Dis 173:636-46
Porat, N; Apicella, M A; Blake, M S (1995) Neisseria gonorrhoeae utilizes and enhances the biosynthesis of the asialoglycoprotein receptor expressed on the surface of the hepatic HepG2 cell line. Infect Immun 63:1498-506
Porat, N; Apicella, M A; Blake, M S (1995) A lipooligosaccharide-binding site on HepG2 cells similar to the gonococcal opacity-associated surface protein Opa. Infect Immun 63:2164-72
Blake, M S; Blake, C M; Apicella, M A et al. (1995) Gonococcal opacity: lectin-like interactions between Opa proteins and lipooligosaccharide. Infect Immun 63:1434-9
Brooks, G F; Lammel, C J; Blake, M S et al. (1992) Antibodies against IgA1 protease are stimulated both by clinical disease and asymptomatic carriage of serogroup A Neisseria meningitidis. J Infect Dis 166:1316-21
Wetzler, L M; Blake, M S; Barry, K et al. (1992) Gonococcal porin vaccine evaluation: comparison of Por proteosomes, liposomes, and blebs isolated from rmp deletion mutants. J Infect Dis 166:551-5
Koomey, M; Bergstrom, S; Blake, M et al. (1991) Pilin expression and processing in pilus mutants of Neisseria gonorrhoeae: critical role of Gly-1 in assembly. Mol Microbiol 5:279-87
Butler, C A; Gotschlich, E C (1991) High-frequency mobilization of broad-host-range plasmids into Neisseria gonorrhoeae requires methylation in the donor. J Bacteriol 173:5793-9
Blake, M S; Eastby, C (1991) Studies on the gonococcal IgA1 protease II. Improved methods of enzyme purification and production of monoclonal antibodies to the enzyme. J Immunol Methods 144:215-21
Blake, M S; MacDonald, C M; Klugman, K P (1989) Colony morphology of piliated Neisseria meningitidis. J Exp Med 170:1727-36

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