ArticleInfection and immunity2001
Chlamydia pneumoniae major outer membrane protein is a surface-exposed antigen that elicits antibodies primarily directed against conformation-dependent determinants.
Article in Infection and immunity, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 68 citations in OpenAlex.
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- Low-Dose Aspirin May Prevent Trophoblast Dysfunction in Women With Chlamydia Pneumoniae Infection.Reproductive sciences (Thousand Oaks, Calif.) · 2019Article
- AP-1 Transcription Factor Serves as a Molecular Switch between Chlamydia pneumoniae Replication and Persistence.Infection and immunity · 2015Article
- Biochemical and localization analyses of putative type III secretion translocator proteins CopB and CopB2 of Chlamydia trachomatis reveal significant distinctions.Infection and immunity · 2011Article
- Serodiagnosis of Chlamydia pneumoniae infection using three inclusion membrane proteins.Journal of clinical laboratory analysis · 2010Article
- Assessment of cell-surface exposure and vaccinogenic potentials of Treponema pallidum candidate outer membrane proteins.Microbes and infection · 2007Article
- Characterization of hypothetical proteins Cpn0146, 0147, 0284 & 0285 that are predicted to be in the Chlamydia pneumoniae inclusion membrane.BMC microbiology · 2007Article
- Antigenic variation of TprK V regions abrogates specific antibody binding in syphilis.Infection and immunity · 2006Article
- Analysis of putative Chlamydia trachomatis chaperones Scc2 and Scc3 and their use in the identification of type III secretion substrates.Journal of bacteriology · 2005Article
- Degradation of Chlamydia pneumoniae by peripheral blood monocytic cells.Infection and immunity · 2005Article
- Predominant outer membrane antigens of Bartonella henselae.Infection and immunity · 2004Article
- Functional reconstitution, gene isolation and topology modelling of porins from Burkholderia pseudomallei and Burkholderia thailandensis.The Biochemical journal · 2004Article
- Production of Chlamydia pneumoniae proteins in Bacillus subtilis and their use in characterizing immune responses in the experimental infection model.Clinical and diagnostic laboratory immunology · 2003Article
- Detection of Chlamydia pneumoniae-specific antibodies binding to the VD2 and VD3 regions of the major outer membrane protein.Journal of clinical microbiology · 2003Article
- Adjuvant modulation of the immune responses and the outcome of infection with Chlamydia pneumoniae.Clinical and experimental immunology · 2002Article
- Isolation of Chlamydia pneumoniae clonal variants by a focus-forming assay.Infection and immunity · 2002Article
- Prediction of the membrane-spanning beta-strands of the major outer membrane protein of Chlamydia.Protein science : a publication of the Protein Society · 2002Article
- Inclusion fluorescent-antibody test as a screening assay for detection of antibodies to Chlamydia pneumoniae.Clinical and diagnostic laboratory immunology · 2002Article
- Genomic approach for analysis of surface proteins in Chlamydia pneumoniae.Infection and immunity · 2002Article
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
The major outer membrane protein (MOMP) of Chlamydia trachomatis serovariants is known to be an immunodominant surface antigen. Moreover, it is known that the C. trachomatis MOMP elicits antibodies that recognize both linear and conformational antigenic determinants. In contrast, it has been reported that the MOMP of Chlamydia pneumoniae is not surface exposed and is immunorecessive. We hypothesized that the discrepancies between C. trachomatis and C. pneumoniae MOMP exposure on intact chlamydiae and immunogenic properties might be because the focus of the host's immune response is directed to conformational epitopes of the C. pneumoniae MOMP. We therefore conducted studies aimed at defining the surface exposure of MOMP and the conformational dominance of MOMP antibodies. We present here a description of C. pneumoniae species-specific monoclonal antibody (MAb), GZD1E8, which recognizes a conformational epitope on the surface of C. pneumoniae. This MAb is potent in the neutralization of C. pneumoniae infectivity in vitro. Another previously described C. pneumoniae species-specific monoclonal antibody, RR-402, displayed very similar characteristics. However, the antigenic determinant recognized by RR-402 has yet to be identified. We show by immunoprecipitation of C. pneumoniae with GZD1E8 and RR-402 MAbs and by mass spectrometry analysis of immunoprecipitated proteins that both antibodies GZD1E8 and RR-402 recognize the MOMP of C. pneumoniae and that this protein is localized on the surface of the organism. We also show that human sera from C. pneumoniae-positive donors consistently recognize the MOMP by immunoprecipitation, indicating that the MOMP of C. pneumoniae is an immunogenic protein. These findings have potential implications for both C. pneumoniae vaccine and diagnostic assay development.
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