Abstract
Immunoglobulin G in human serum neutralizes chlamydial infectivity in vitro. Complement-intact, C5-depleted, and C8-depleted human serum all have significantly more neutralizing activity than serum heated to inactivate early components of complement. Cobra venom factor, an analog of human C3b, enhances neutralization of antichlamydial immunoglobulin G in the absence of early complement components.
Full text
PDF



Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Barnes R. C., Wang S. P., Kuo C. C., Stamm W. E. Rapid immunotyping of Chlamydia trachomatis with monoclonal antibodies in a solid-phase enzyme immunoassay. J Clin Microbiol. 1985 Oct;22(4):609–613. doi: 10.1128/jcm.22.4.609-613.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Becherer J. D., Alsenz J., Lambris J. D. Molecular aspects of C3 interactions and structural/functional analysis of C3 from different species. Curr Top Microbiol Immunol. 1990;153:45–72. doi: 10.1007/978-3-642-74977-3_3. [DOI] [PubMed] [Google Scholar]
- Caldwell H. D., Perry L. J. Neutralization of Chlamydia trachomatis infectivity with antibodies to the major outer membrane protein. Infect Immun. 1982 Nov;38(2):745–754. doi: 10.1128/iai.38.2.745-754.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Johnson A. P., Osborn M. F., Rowntree S., Thomas B. J., Taylor-Robinson D. A study of inactivation of Chlamydia trachomatis by normal human serum. Br J Vener Dis. 1983 Dec;59(6):369–372. doi: 10.1136/sti.59.6.369. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Joiner K. A. Complement evasion by bacteria and parasites. Annu Rev Microbiol. 1988;42:201–230. doi: 10.1146/annurev.mi.42.100188.001221. [DOI] [PubMed] [Google Scholar]
- Joiner K. A., Hawiger A., Gelfand J. A. A study of optimal reaction conditions for an assay of the human alternative complement pathway. Am J Clin Pathol. 1983 Jan;79(1):65–72. doi: 10.1093/ajcp/79.1.65. [DOI] [PubMed] [Google Scholar]
- Megran D. W., Stiver H. G., Peeling R., Maclean I. W., Brunham R. C. Complement enhancement of neutralizing antibody to the structural proteins of Chlamydia trachomatis. J Infect Dis. 1988 Sep;158(3):661–663. doi: 10.1093/infdis/158.3.661. [DOI] [PubMed] [Google Scholar]
- Newhall W. J., Batteiger B., Jones R. B. Analysis of the human serological response to proteins of Chlamydia trachomatis. Infect Immun. 1982 Dec;38(3):1181–1189. doi: 10.1128/iai.38.3.1181-1189.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Osborn M. F., Johnson A. P., Taylor-Robinson D. Susceptibility of different serovars of Chlamydia trachomatis to inactivation by normal human serum. Genitourin Med. 1985 Aug;61(4):244–246. doi: 10.1136/sti.61.4.244. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Peeling R. W., Peeling J., Brunham R. C. High-resolution 31P nuclear magnetic resonance study of Chlamydia trachomatis: induction of ATPase activity in elementary bodies. Infect Immun. 1989 Nov;57(11):3338–3344. doi: 10.1128/iai.57.11.3338-3344.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Peeling R., Maclean I. W., Brunham R. C. In vitro neutralization of Chlamydia trachomatis with monoclonal antibody to an epitope on the major outer membrane protein. Infect Immun. 1984 Nov;46(2):484–488. doi: 10.1128/iai.46.2.484-488.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Peterson E. M., Hoshiko M., Markoff B. A., Lauermann M. W., de la Maza L. M. Differences in susceptibilities of the lymphogranuloma venereum and trachoma biovars of Chlamydia trachomatis to neutralization by immune sera. Infect Immun. 1990 Apr;58(4):938–943. doi: 10.1128/iai.58.4.938-943.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ratnoff W. D., Fearon D. T., Austen K. F. The role of antibody in the activation of the alternative complement pathway. Springer Semin Immunopathol. 1983;6(4):361–371. doi: 10.1007/BF02116280. [DOI] [PubMed] [Google Scholar]
- Su H., Watkins N. G., Zhang Y. X., Caldwell H. D. Chlamydia trachomatis-host cell interactions: role of the chlamydial major outer membrane protein as an adhesin. Infect Immun. 1990 Apr;58(4):1017–1025. doi: 10.1128/iai.58.4.1017-1025.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tauber A. I., Pavlotsky N., Lin J. S., Rice P. A. Inhibition of human neutrophil NADPH oxidase by Chlamydia serovars E, K, and L2. Infect Immun. 1989 Apr;57(4):1108–1112. doi: 10.1128/iai.57.4.1108-1112.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Taylor P. W. Bactericidal and bacteriolytic activity of serum against gram-negative bacteria. Microbiol Rev. 1983 Mar;47(1):46–83. doi: 10.1128/mr.47.1.46-83.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Volanakis J. E. Participation of C3 and its ligands in complement activation. Curr Top Microbiol Immunol. 1990;153:1–21. doi: 10.1007/978-3-642-74977-3_1. [DOI] [PubMed] [Google Scholar]
- Williams D. M., Schachter J., Weiner M. H., Grubbs B. Antibody in host defense against mouse pneumonitis agent (murine Chlamydia trachomatis). Infect Immun. 1984 Sep;45(3):674–678. doi: 10.1128/iai.45.3.674-678.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
