Chlamydia trachomatis major outer membrane protein epitopes expressed as fusions with LamB in an attenuated aro A strain of Salmonella typhimurium; their application as potential immunogens.

The difference in amino acid sequence designation is due to the presence of the signal peptide in the database sequence. Two overlapping C. trachomatis MOMP peptides (aa 288-298, and aa 298-308) linked by two amino acids (Asp-Pro) were expressed as a fusion protein inserted in E. coli lamB at aa position 153, with one extra amino acid at each end introduced by cloning. Antisera raised against a synthetic peptide version of the epitope (aa 288-298) reacted with the fusion protein which was found in outer membrane fractions of either E. coli or S. typhimurium aroA.