Chlamydia trachomatis elementary bodies possess proteins which bind to eucaryotic cell membranes.
Chlamydia trachomatis proteins were electrophoresed and then transferred to nitrocellulose paper to detect chlamydial proteins which bind to eucaryotic cell membranes. Resolved polypeptides of C. trachomatis serovars J and L2 were reacted with iodinated HeLa cell membranes and autoradiographed. Infectious elementary bodies of both serovars possess 31,000- and 18,000-dalton proteins which bind to HeLa cells. In contrast, noninfectious reticulate bodies do not possess eucaryotic cell-binding proteins. Both proteins are antigenic when reacted with hyperimmune rabbit antisera in immunoblots and antisera raised against the 31,000- and 18,000-dalton proteins are inhibitory to chlamydia-host cell association. In addition, these antisera exhibit neutralizing activity. Our data suggest that these putative chlamydial adhesins play a key role in the early steps of chlamydia-host cell interaction and that antibody directed against them may be protective.
D000268:Adhesiveness; D001426:Bacterial Proteins / Q000032:analysis* / Q000276:immunology / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism*; D002692:Chlamydia trachomatis / Q000032:analysis* / Q000276:immunology; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006367:HeLa Cells; D006801:Humans; D007158:Immunologic Techniques; D066298:In Vitro Techniques; D008970:Molecular Weight; D009500:Neutralization Tests
D001426:Bacterial Proteins