Chlamydia trachomatis suppresses host cell store-operated Ca²⁺ entry and inhibits NFAT/calcineurin signaling.

ABSTRACT: The obligate intracellular bacterium, Chlamydia trachomatis, replicates within a parasitophorous vacuole termed an inclusion. During development, host proteins critical for regulating intracellular calcium (Ca²⁺) homeostasis interact with the inclusion membrane. The inclusion membrane protein, MrcA, interacts with the inositol-trisphosphate receptor (IP₃R), an ER cationic channel that conducts Ca²⁺. Stromal interaction molecule 1 (STIM1), an ER transmembrane protein important for regulating store-operated Ca²⁺ entry (SOCE), localizes to the inclusion membrane via an uncharacterized interaction. We therefore examined Ca²⁺ mobilization in C. trachomatis infected cells. Utilizing a variety of Ca²⁺ indicators to assess changes i

SUBMITTER: Chamberlain NB 

PROVIDER: S-EPMC9741641 | biostudies-literature | 2022 Dec

REPOSITORIES: biostudies-literature