AI Article Synopsis
- S. Typhimurium, EPEC, and EHEC bacteria hijack host cell actin to enhance their infection process by injecting effectors that alter cell signaling and actin rearrangements.
- Cyclophilin A (CypA) is identified as a key player in managing bacterial invasion, as its depletion leads to increased bacterial loads in host cells.
- CypA interacts with the EPEC effector Tir and is involved in the formation of actin-rich structures called pedestals during infections, highlighting its role in dynamic cellular responses to bacterial invasions.
Article Abstract
Salmonella enterica serovar Typhimurium (S. Typhimurium), enteropathogenic Escherichia coli (EPEC) and enterohemorrhagic E. coli (EHEC) commandeer the actin cytoskeleton of their host cells as a crucial step in their infectious processes. These pathogens depend on the injection of their own effectors directly into target host cells in order to usurp cellular signaling pathways that lead to morphological actin rearrangements in those cells. Here we show that the PPIase Cyclophilin A (CypA) is a novel component of S. Typhimurium-induced membrane ruffles and functions to restrict bacterial invasion levels, as in cells depleted of CypA, bacterial loads increase. We also demonstrate that CypA requires the EPEC effector Tir as well as pedestal formation for its recruitment to bacterial attachment sites and that its presence at pedestals also holds during EHEC infections. Finally, we demonstrate that CypA is found at lamellipodia; actin-rich structures at the leading edge of motile cells. Our findings further establish CypA as a component of dynamic actin-rich structures formed during bacterial infections and within cells in general. Anat Rec, 301:2086-2094, 2018. © 2018 Wiley Periodicals, Inc.
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