| Chlamydia trachomatis, an obligate intracellular pathogen, grows inside of a vacuole, termed the inclusion. One strategy for Chlamydia to obtain necessary nutrients and metabolites from the host is to intercept host vesicular trafficking pathways. In this study we demonstrate that a trans-Golgi soluble N-ethylmaleimide--sensitive factor attachment protein (SNARE), syntaxin 10, colocalizes with specific Golgi structural proteins at the chlamydial inclusion. Further, syntaxin 10 and Golgi subunits remain stably localized with the inclusion after the Golgi is chemically disrupted with brefeldin A (BFA) or nocodazole. We demonstrate that siRNA knockdown of syntaxin 10 results in major defects in normal chlamydial maturation including: variable inclusion size with fewer chlamydial organisms per inclusion, fewer infectious progeny, and delayed or halted RB-EB differentiation. These defects in chlamydial development correlate with an overabundance of NBD-lipid retained by inclusions cultured in syntaxin 10 knockdown cells. We hypothesize that Chlamydia utilize syntaxin 10 at the inclusion membrane to maintain an optimal growth environment for the organisms. Overall, loss of syntaxin 10 at the inclusion membrane negatively affects Chlamydia. Defining the relationship between syntaxin 10 and the inclusion membrane will increase our understanding of SNARE-mediated Golgi-inclusion interactions that impact chlamydial development. |
