Official websites use. Share sensitive information only on official, secure websites. The use, distribution or reproduction in other forums is permitted, provided the original author s and the copyright owner are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. Invasion of epithelial cells by the obligate intracellular bacterium Chlamydia trachomatis results in its enclosure inside a membrane-bound compartment termed an inclusion.
The bacterium quickly begins manipulating interactions between host intracellular trafficking and the inclusion interface, diverging from the endocytic pathway and escaping lysosomal fusion. We have identified a previously uncharacterized protein, CT, unique to the Chlamydiaceae , in the absence of which most bacteria failed to establish a successful infection.
CT is abundant in the infectious form of the bacteria, in which it associates with CT, a putative novel chaperone protein. We show that CT is translocated into the host cytoplasm via type three secretion throughout the developmental cycle of the bacteria. Two separate domains of roughly equal size have been identified within CT and a 1.
Genetic disruption of ct expression resulted in a strong bacterial growth defect, which was due to deficiencies in proliferation and in the generation of infectious bacteria. Our results converge to identify CT as a secreted protein that plays multiple and crucial roles in the initiation and support of the C. They reveal that genetic disruption of a single effector can deeply affect bacterial fitness.
Keywords: host-pathogen interactions, effector proteins, genetic manipulation, Chlamydia trachomatis , chaperone proteins, structural biology, prenylation. Chlamydia trachomatis is the most common sexually transmitted bacterial pathogen.
