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IDENTIFICATION AND BIOCHEMICAL CHARACTERIZATION OF THE CHLAMYDIA TRACHOMA TIS TYPE III SECRETION CHAPERONE, SLCl, AND ITS ROLE IN THE TRANSLOCATION OF THE INVASIONASSOCIATED EFFECTOR T ARP Amanda Brinkworth May 2011 Chlamydia trachomatis is an obligate intracellular pathogen that utilizes a type III secretion system to enter mammalian cells and establish an intracellular niche. TARP, the translocated ~ctin recruitment 12rotein, is a chlamydial invasion protein known to be type III secreted by the metabolically inert elementary body upon docking to the mammalian cell surface. Because immediate secretion of TARP into host cells is necessary for entry, I hypothesized that a chlamydial chaperone binds to TARP and facilitates its translocation through the type III secretion apparatus. Most effectorbinding type III secretion chaperones are small (14-18 kDa), have an acidic pI, and share a specific secondary structure of alternating alpha-helices (a) and beta-sheets (~). Typically, type III secretion chaperones dimerize and interact with their effectors as a complex of two molecules of chaperone to one effector molecule. Only 3 Chlamydia trachomatis proteins have been identified in EB' s that are predicted to be putative chlamydial type III effector chaperones. These are CT043, CT663, and CT088, which I have designated as SIc 1, SIc2, and Scc 1, respectively. These chaperones were tested for their interaction with the N-terminal200 amino acids ofTARP (HIS6_TARpl-200) by co-

Identification and biochemical characterization of the CHLAMYDIA TRACHOMATIS type III secretion chaperone, SLC1, and its role in the translocation of the invasion-associated effector TARP.