{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T05:35:56Z","timestamp":1791178556569,"version":"4.1.0"},"reference-count":96,"publisher":"American Society for Microbiology","issue":"5","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Clin. Vaccine Immunol."],"published-print":{"date-parts":[[2015,5]]},"abstract":"<jats:title>ABSTRACT<\/jats:title><jats:p>Urgently needed species-specific enzyme-linked immunosorbent assays (ELISAs) for the detection of antibodies against<jats:named-content content-type=\"genus-species\">Chlamydia<\/jats:named-content>spp. have been elusive due to high cross-reactivity of chlamydial antigens. To identify<jats:named-content content-type=\"genus-species\">Chlamydia<\/jats:named-content>species-specific B cell epitopes for such assays, we ranked the potential epitopes of immunodominant chlamydial proteins that are polymorphic among all<jats:named-content content-type=\"genus-species\">Chlamydia<\/jats:named-content>species. High-scoring peptides were synthesized with N-terminal biotin, followed by a serine-glycine-serine-glycine spacer, immobilized onto streptavidin-coated microtiter plates, and tested with mono-specific mouse hyperimmune sera against each<jats:named-content content-type=\"genus-species\">Chlamydia<\/jats:named-content>species in chemiluminescent ELISAs. For each of nine<jats:named-content content-type=\"genus-species\">Chlamydia<\/jats:named-content>species, three to nine dominant polymorphic B cell epitope regions were identified on OmpA, CT618, PmpD, IncA, CT529, CT442, IncG, Omp2, TarP, and IncE proteins. Peptides corresponding to 16- to 40-amino-acid species-specific sequences of these epitopes reacted highly and with absolute specificity with homologous, but not heterologous,<jats:named-content content-type=\"genus-species\">Chlamydia<\/jats:named-content>monospecies-specific sera. Host-independent reactivity of such epitopes was confirmed by testing of six<jats:named-content content-type=\"genus-species\">C. pecorum<\/jats:named-content>-specific peptides from five proteins with<jats:named-content content-type=\"genus-species\">C. pecorum<\/jats:named-content>-reactive sera from cattle, the natural host of<jats:named-content content-type=\"genus-species\">C. pecorum<\/jats:named-content>. The probability of cross-reactivity of peptide antigens from closely related chlamydial species or strains correlated with percent sequence identity and declined to zero at &lt;50% sequence identity. Thus, phylograms of B cell epitope regions predict the specificity of peptide antigens for rational use in the genus-, species-, or serovar-specific molecular serology of<jats:named-content content-type=\"genus-species\">Chlamydia<\/jats:named-content>spp. We anticipate that these peptide antigens will improve chlamydial serology by providing easily accessible assays to nonspecialist laboratories. Our approach also lends itself to the identification of relevant epitopes of other microbial pathogens.<\/jats:p>","DOI":"10.1128\/cvi.00102-15","type":"journal-article","created":{"date-parts":[[2015,3,12]],"date-time":"2015-03-12T02:12:36Z","timestamp":1426126356000},"page":"539-552","source":"Crossref","is-referenced-by-count":31,"title":["Defining Species-Specific Immunodominant B Cell Epitopes for Molecular Serology of Chlamydia Species"],"prefix":"10.1128","volume":"22","author":[{"given":"K. 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