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The first 25 N-terminal amino acids of the major outer membrane protein of Chlamydia trachomatis serovar L2 were determined. The amino acid sequence was used to construct an oligonucleotide probe specific for the major outer membrane protein gene. Using this oligonucleotide as a hybridization major outer membrane protein gene. Using this oligonucleotide as a hybridization probe, we discovered one recombinant clone that produced a 15-kilodalton polypeptide which reacted with a monoclonal antibody directed against the major outer membrane protein type-specific epitope. In a separate set of experiments, we uncovered another recombinant clone that produced a 51-kilodalton polypeptide which was reactive with an anti-major outer membrane protein subspecies-specific monoclonal antibody. The expression of these recombinant DNA plasmids in Escherichia coli is discussed.

Partial amino acid sequence and molecular cloning of the encoding gene for the major outer membrane protein of Chlamydia trachomatis