A heat-labile protein of Chlamydia trachomatis binds to HeLa cells and inhibits the adherence of chlamydiae.

From highly purified elementary bodies (EBs) of Chlamydia trachomatis, we have identified a protein of 38 kDa that selectively binds to monolayer cultures of HeLa cells. This protein, which we have named the chlamydial cytadhesin (CCA), is present on the surface of the EBs of three C. trachomatis serovars (B, E, and L1) that were examined. Localization of the CCA at the surface was confirmed by its ability to be labeled when viable EBs were iodinated and by its absence in preparations from trypsin-treated EBs. Viable EBs, but not heated or trypsin-treated EBs, inhibited the binding of the CCA to HeLa cells, indicating competition for a common receptor on the host cell membrane. A dose-dependent inhibition of adherence of radioactive EBs to HeLa cells was effected by extracts containing the CCA. This inhibition occurred even with extracts prepared from the EB of heterologous serovars. However, no inhibition could be demonstrated with extracts prepared from heat-treated EBs. Heat treatment of the extract resulted in the loss of ability of the CCA to bind to the host cells. HeLa cells preincubated with CCA-containing chlamydial extract showed reduced ability to bind labeled EBs and to develop cytoplasmic inclusions after infection. This protective activity was lost after exposure of the extract to heat. These findings indicate that the CCA is a thermolabile surface-exposed chlamydial adhesin; it may be useful in the development of vaccines for diseases caused by the pathogenic bacterium.