Abstract

Biological Significance of Treponema pallidum Surface Antigens. The goal of this work is to define and purify individual T. pallidum molecules of relevance to the pathogenesis of syphilis. We have expressed in E. coli a 190 kilodalton T. pallidum antigen which is remarkably resistant to proteolytic degradation. Twenty-five milligram amounts of this antigen, designated """"""""4D"""""""" have been purified to homogeneity. Immunization of rabbits with the 4D antigen induces a complement dependent serum activity which immobilizes T. pallidum in vitro. We will present plans to develop an optimal immunization protocol for maintenance of high levels of immobilizing activity and then test the relationship between immobilizing activity (TPI), immunity to dermal challenge with virulent T. pallidum, and the ability of the organism to attach to host surfaces. We plan use of immunoelectronmicroscopy (IEM) to localilze the 4D antigen and other cloned antigens after thin sectioning of T. pallidum. Cloned T. pallidum antigens with IEM demonstrated surface location will be studied for activity in systems to assess attachment and immunity in experimental syphilis.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Research Project (R01)
Project #
5R01AI021352-03
Application #
3131372
Study Section
Bacteriology and Mycology Subcommittee 1 (BM)
Project Start
1984-09-30
Project End
1987-08-31
Budget Start
1986-09-01
Budget End
1987-08-31
Support Year
3
Fiscal Year
1986
Total Cost
Indirect Cost

  Institution

Name
University of California Los Angeles
Department
Type
Schools of Medicine
DUNS #
119132785
City
Los Angeles
State
CA
Country
United States
Zip Code
90095

  Publications

Champion, Cheryl I; Blanco, David R; Lovett, Michael A (2005) Quantitative assessment of protection in experimental syphilis. Infect Immun 73:5923-7
Blanco, David R; Champion, Cheryl I; Dooley, Alek et al. (2005) A monoclonal antibody that conveys in vitro killing and partial protection in experimental syphilis binds a phosphorylcholine surface epitope of Treponema pallidum. Infect Immun 73:3083-95
Blanco, David R; Champion, Cheryl I; Lovett, Michael A (2005) Use of the skin protection assay in experimental syphilis to assess protective immunity against a specific Treponema pallidum surface epitope. FEMS Microbiol Lett 249:171-5
Blanco, D R; Whitelegge, J P; Miller, J N et al. (1999) Demonstration by mass spectrometry that purified native Treponema pallidum rare outer membrane protein 1 (Tromp1) has a cleaved signal peptide. J Bacteriol 181:5094-8
Zhang, H H; Blanco, D R; Exner, M M et al. (1999) Renaturation of recombinant Treponema pallidum rare outer membrane protein 1 into a trimeric, hydrophobic, and porin-active conformation. J Bacteriol 181:7168-75
Lewinski, M A; Miller, J N; Lovett, M A et al. (1999) Correlation of immunity in experimental syphilis with serum-mediated aggregation of Treponema pallidum rare outer membrane proteins. Infect Immun 67:3631-6
Blanco, D R; Champion, C I; Lewinski, M A et al. (1999) Immunization with Treponema pallidum outer membrane vesicles induces high-titer complement-dependent treponemicidal activity and aggregation of T. pallidum rare outer membrane proteins (TROMPs). J Immunol 163:2741-6
Skare, J T; Foley, D M; Hernandez, S R et al. (1999) Cloning and molecular characterization of plasmid-encoded antigens of Borrelia burgdorferi. Infect Immun 67:4407-17
Shang, E S; Skare, J T; Exner, M M et al. (1998) Isolation and characterization of the outer membrane of Borrelia hermsii. Infect Immun 66:1082-91
Champion, C I; Blanco, D R; Exner, M M et al. (1997) Sequence analysis and recombinant expression of a 28-kilodalton Treponema pallidum subsp. pallidum rare outer membrane protein (Tromp2). J Bacteriol 179:1230-8

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