| Both B cell and T cell antigenicities of the major outer membrane protein (MOMP) of Chlamydia trachomatis were comprehensively analyzed. The B cell antigenicity of chalmydial MOMPs from 7 different serovars was systemically evaluated by using overlapping hexapeptides and polyclonal as well as monoclonal antibodies (mAb) in a peptide enzyme-lined immunosorbent assay (ELISA). Serovar B and C MOMPs were most extensively analyzed since these two serovars are the senior representatives in their serogroups respectively. Based on the binding titer and binding frequency, all four variable domains (VDs) of B MOMP are antigenic, but only VDIV is immunodominant among immunized rabbits. The specificity and surface accessibility of the epitopes were characterized by preabsorbing the peptide-reactive antibodies with acetone-permeabilized or native organisms prior to the peptide-ELISA. Four neutralizing species specific mAbs from different sources were located within S3 region and were able to bind to native organisms from 8 different serovars. We concluded that a sequence covering ST cell antigenicity of serovar B MOMP was also evaluated. Multiple Th cell sites were found in TWe synthesized a colinear 30-mer peptide (designated as HIn general, antibody responses to epitopes in both B and C MOMP VDII regions and in C MOMP VDIV C-terminal region are most intensely restricted by H-2. Therefore, the epitopes in these regions are not suitable for vaccine development. |
