Chlamydia Trachomatis Suppresses Host Cell Store-operated Ca Entry and Inhibits NFAT/calcineurin Signaling
Affiliations
The obligate intracellular bacterium, Chlamydia trachomatis, replicates within a parasitophorous vacuole termed an inclusion. During development, host proteins critical for regulating intracellular calcium (Ca) homeostasis interact with the inclusion membrane. The inclusion membrane protein, MrcA, interacts with the inositol-trisphosphate receptor (IPR), an ER cationic channel that conducts Ca. Stromal interaction molecule 1 (STIM1), an ER transmembrane protein important for regulating store-operated Ca entry (SOCE), localizes to the inclusion membrane via an uncharacterized interaction. We therefore examined Ca mobilization in C. trachomatis infected cells. Utilizing a variety of Ca indicators to assess changes in cytosolic Ca concentration, we demonstrate that C. trachomatis impairs host cell SOCE. Ca regulates many cellular signaling pathways. We find that the SOCE-dependent NFAT/calcineurin signaling pathway is impaired in C. trachomatis infected HeLa cells and likely has major implications on host cell physiology as it relates to C. trachomatis pathogenesis.
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