Analysis of the humoral response elicited in mice by a chimeric peptide representing variable segments I and IV of the major outer membrane protein of Chlamydia trachomatis.

A synthetic chimeric peptide representing the variable segments I (VS I) and IV of the major outer membrane protein (MOMP) of Chlamydia trachomatis, serovars C and E respectively, was studied to determine its ability to elicit a neutralizing humoral response in mice. Antibody responses varied to the peptide in the five inbred strains of mice, A/J(H-2a), DBA/1(H-2q), C57BL/10(H-2b), CBA/J(H-2k), Balb/c(H-2d), that were immunized. There was a spectrum of antibody responses which ranged from high ELISA and IFA titres by the C57BL/10 mice to little or no response by Balb/c mice. Antisera from C57BL/10 mice recognized all 15 serovars of C. trachomatis in a dot blot assay. A pepscan of the antisera from C57BL/10 mice showed strong reactivity to both neutralizing epitopes VAGLQNDPT in VS I of serovar C and the species-conserved peptide, TLNPTIA, in the VS IV. This antiserum neutralized, in vitro, the infectivity of serovars representing the B complex (B, D and E), C complex (C and J), B-related (F) and C-related (L3) complexes. In an attempt to elicit a stronger response to the peptide in the weakly reactive Balb/c and the DBA/1 strains, the peptide was conjugated to the carrier, keyhole limpet haemocyanin (KLH). All mice immunized with the KLH-peptide produced high-titred antisera that recognized neutralizing epitopes in VS I and VS IV and strongly neutralized the infectivity of both serovars C and E.