Initial characterization of a chlamydial receptor on mammalian cells.
We have examined characteristics of the binding of eukaryotic cells to chlamydial elementary body (EB)-specific proteins. A wide variety of eukaryotic cell lines bound to representatives of both Chlamydia trachomatis lymphogranuloma venereum (LGV) and trachoma biovars and a C. psittaci strain meningopneumonitis (Mn) suggesting the presence of a common host cell receptor. Neither tunicamycin nor neuraminidase treatment of HeLa cells impaired binding to C. trachomatis EB, implying that host cell N-linked carbohydrate domains and sialic acid moieties, respectively, are not involved in attachment. However, trypsinized HeLa cells do not bind to EB, suggestive of a proteinaceous host cell receptor. The trypsin sensitivity of two EB-specific binding proteins Mr = 18,000 and 31,000) was also examined, and the finding that 125I-labeled HeLa cells bind both the 18,000 and 31,000-dalton proteins after chlamydial trypsinization corroborates our earlier observation that these EB binding proteins mediate attachment.
Kaul
R
R
Department of Pediatrics, University of Alberta, Edmonton, Canada.
Chong
K L
KL
Wenman
W M
WM
D000818:Animals; D001422:Bacterial Adhesion; D001426:Bacterial Proteins / Q000378:metabolism*; D002352:Carrier Proteins / Q000378:metabolism; D002460:Cell Line; D002692:Chlamydia trachomatis / Q000378:metabolism*; D006801:Humans; D011971:Receptors, Immunologic / Q000378:metabolism*
D001426:Bacterial Proteins; D002352:Carrier Proteins; D011971:Receptors, Immunologic; C047105:bacterial adhesin receptor; C053998:chlanectin protein, Chlamydia trachomatis