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- W2136910633 endingPage "e1000942" @default.
- W2136910633 startingPage "e1000942" @default.
- W2136910633 abstract "Large bacterial protein toxins autotranslocate functional effector domains to the eukaryotic cell cytosol, resulting in alterations to cellular functions that ultimately benefit the infecting pathogen. Among these toxins, the clostridial glucosylating toxins (CGTs) produced by Gram-positive bacteria and the multifunctional-autoprocessing RTX (MARTX) toxins of Gram-negative bacteria have distinct mechanisms for effector translocation, but a shared mechanism of post-translocation autoprocessing that releases these functional domains from the large holotoxins. These toxins carry an embedded cysteine protease domain (CPD) that is activated for autoprocessing by binding inositol hexakisphosphate (InsP6), a molecule found exclusively in eukaryotic cells. Thus, InsP6-induced autoprocessing represents a unique mechanism for toxin effector delivery specifically within the target cell. This review summarizes recent studies of the structural and molecular events for activation of autoprocessing for both CGT and MARTX toxins, demonstrating both similar and potentially distinct aspects of autoprocessing among the toxins that utilize this method of activation and effector delivery." @default.
- W2136910633 created "2016-06-24" @default.
- W2136910633 creator A5015554938 @default.
- W2136910633 creator A5021165682 @default.
- W2136910633 date "2010-07-08" @default.
- W2136910633 modified "2023-09-26" @default.
- W2136910633 title "Inositol Hexakisphosphate-Induced Autoprocessing of Large Bacterial Protein Toxins" @default.
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- W2136910633 doi "https://doi.org/10.1371/journal.ppat.1000942" @default.
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