Abstract
Variants of an ilp (invasin-like protein) gene have been identified previously in Chlamydia caviae and in Chlamydia suis. The C. caviae ilp gene is interrupted by two frame shift mutations while the C. suis gene is intact. Characterization of the ilp gene in C. caviae passaged minimally in vitro showed that the two frameshift mutations were present in the original isolates. The gentamicin protection assay was used to determine if E. coli bacteria expressing the intact C. suis ilp could adhere to or invade HEp-2 cells. While inv+ clones showed increased adherence and invasion, no increase in adherence or invasion was observed for ilp+ clones. However, these clones were found to produce detectable amounts of ilp transcript. In a 48 h time course of C. suis culture, ilp transcript was initially detected at 8 h, peaked at 16 h, and declined subsequently. Antibodies specifically recognizing the putative functional domain of Ilp failed to detect any ilp-specific gene product in either E. coli or C. suis cultures. These data suggest that ilp does not encode a functional protein and raise questions about how ilp was introduced and maintained in Chlamydia.