ELECTROPHORETIC ANALYSIS OF THE MAJOR OUTER-MEMBRANE PROTEIN OF CHLAMYDIA-PSITTACI REVEALS MULTIMERS WHICH ARE RECOGNIZED BY PROTECTIVE MONOCLONAL-ANTIBODIES

Purified major outer membrane protein, detergent solubilized and reduced with dithiothreitol but not heated, gave an apparent molecular weight in sodium dodecyl sulfate (SDS)-polyacrylamide gels almost three times that observed for the heat-denatured SDS-treated peptide. This is similar to the behavior of porin trimers from gram-negative bacteria. Two protective monoclonal antibodies showed strong binding to the proposed trimer but not to denatured, monomeric major outer membrane protein.