Activation of the unfolded protein response by Listeria monocytogenes.

摘要: Summary The endoplasmic reticulum (ER) responds to perturbation of homeostasis with stress. To maintain ER function, a signalling-circuitry has evolved which, when engaged, attempts reduce surplus unfolded proteins by triggering the protein response (UPR). Several studies have implicated UPR in viral infections, neurodegenerative disorders and metabolic diseases but not yet been widely linked bacterial infections. Here we demonstrate that facultative intracellular pathogen Listeria monocytogenes (Lm) induces expansion prior host cell entry. Lm activated kinase RNA-like (PERK) evidenced phosphorylation α-subunit eukaryotic translation initiation factor-2 (eIF2α), inositol-requiring protein-1 (IRE1) as shown detection spliced X-box binding (XBP1) activating transcription factor-6 (ATF6) demonstrated depletion its inactive form. A mutant LmΔhly strain did produce listeriolysin (LLO) lacked response. Conversely purified LLO UPR. Sustained infection resulted apoptosis. Induction stress thapsigargin or tunicamycin reduced number. Our findings suggest plays an important role autonomous defence responses infection.