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We recently developed a consensus computational framework that employs a battery of cellular localization and topological prediction tools to generate ranked clusters of candidate rare OMPs (D. L. Cox et al., Infect. Immun. 78:5178\u20135194, 2010). TP0117\/TP0131 (TprC\/D), a member of the<jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">T. pallidum<\/jats:named-content>repeat (Tpr) family, was a highly ranked candidate. Circular dichroism, heat modifiability by SDS-PAGE, Triton X-114 phase partitioning, and liposome incorporation confirmed that full-length, recombinant TprC (TprC<jats:sup>Fl<\/jats:sup>) forms a \u03b2-barrel capable of integrating into lipid bilayers. Moreover, TprC<jats:sup>Fl<\/jats:sup>increased efflux of terbium-dipicolinic acid complex from large unilamellar vesicles and migrated as a trimer by blue-native PAGE. We found that in<jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">T. pallidum<\/jats:named-content>, TprC is heat modifiable, trimeric, expressed in low abundance, and, based on proteinase K accessibility and opsonophagocytosis assays, surface exposed. From these collective data, we conclude that TprC is a bona fide rare OMP as well as a functional ortholog of<jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Escherichia coli<\/jats:named-content>OmpF. We also discovered that TprC has a bipartite architecture consisting of a soluble N-terminal portion (TprC<jats:sup>N<\/jats:sup>), presumably periplasmic and bound directly or indirectly to peptidoglycan, and a C-terminal \u03b2-barrel (TprC<jats:sup>C<\/jats:sup>). Syphilitic rabbits generate antibodies exclusively against TprC<jats:sup>C<\/jats:sup>, while secondary syphilis patients fail to mount a detectable antibody response against either domain. The syphilis spirochete appears to have resolved a fundamental dilemma arising from its extracellular lifestyle, namely, how to enhance OM permeability without increasing its vulnerability to the antibody-mediated defenses of its natural human host.<\/jats:p>","DOI":"10.1128\/jb.00101-12","type":"journal-article","created":{"date-parts":[[2012,3,5]],"date-time":"2012-03-05T14:50:32Z","timestamp":1330959032000},"page":"2321-2333","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":49,"title":["TprC\/D (Tp0117\/131), a Trimeric, Pore-Forming Rare Outer Membrane Protein of Treponema pallidum, Has a Bipartite Domain Structure"],"prefix":"10.1128","volume":"194","author":[{"given":"Arvind","family":"Anand","sequence":"first","affiliation":[{"name":"Departments of Medicine, University of Connecticut Health Center, Farmington, Connecticut, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Amit","family":"Luthra","sequence":"additional","affiliation":[{"name":"Departments of Medicine, University of Connecticut Health Center, Farmington, Connecticut, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Star","family":"Dunham-Ems","sequence":"additional","affiliation":[{"name":"Departments of Medicine, University of Connecticut Health Center, Farmington, Connecticut, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Melissa J.","family":"Caimano","sequence":"additional","affiliation":[{"name":"Departments of Medicine, University of Connecticut Health Center, Farmington, Connecticut, USA"},{"name":"Department of Pediatrics, Connecticut Children's Medical Center, Division of Pediatric Infectious Diseases, Hartford, Connecticut, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Carson","family":"Karanian","sequence":"additional","affiliation":[{"name":"Department of Pediatrics, Connecticut Children's Medical Center, Division of Pediatric Infectious Diseases, Hartford, Connecticut, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Morgan","family":"LeDoyt","sequence":"additional","affiliation":[{"name":"Departments of Medicine, University of Connecticut Health Center, Farmington, Connecticut, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Adriana R.","family":"Cruz","sequence":"additional","affiliation":[{"name":"Centro Internacional de Entrenamiento e Investigaciones M\u00e9dicas (CIDEIM), Cali, Colombia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Juan C.","family":"Salazar","sequence":"additional","affiliation":[{"name":"Immunology, University of Connecticut Health Center, Farmington, Connecticut, USA"},{"name":"Department of Pediatrics, Connecticut Children's Medical Center, Division of Pediatric Infectious Diseases, Hartford, Connecticut, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Justin D.","family":"Radolf","sequence":"additional","affiliation":[{"name":"Departments of Medicine, University of Connecticut Health Center, Farmington, Connecticut, USA"},{"name":"Genetics and Developmental Biology, University of Connecticut Health Center, Farmington, Connecticut, USA"},{"name":"Immunology, University of Connecticut Health Center, Farmington, Connecticut, USA"},{"name":"Department of Pediatrics, Connecticut Children's Medical Center, Division of Pediatric Infectious Diseases, Hartford, Connecticut, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","reference":[{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.179.16.5076-5086.1997"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1128\/jb.143.2.906-913.1980"},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.2010.07280.x"},{"key":"e_1_3_3_5_2","doi-asserted-by":"crossref","first-page":"1882","DOI":"10.1074\/jbc.M609598200","article-title":"Functional and phylogenetic properties of the pore-forming beta-barrel transporters of the Omp85 family","volume":"282","author":"Bredemeier R","year":"2007","unstructured":"BredemeierR. 2007. 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