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    Identification and structural analysis of the tripartite α-pore forming toxin of Aeromonas hydrophila

    Wilson, J.S. and Churchill-Angus, A.M. and Davies, S.P. and Sedelnikova, S.E. and Tzokov, S.B. and Rafferty, J.B. and Bullough, P.A. and Bisson, Claudine and Baker, P.J. (2019) Identification and structural analysis of the tripartite α-pore forming toxin of Aeromonas hydrophila. Nature Communications 10 (1), p. 2900. ISSN 2041-1723.

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    The alpha helical CytolysinA family of pore forming toxins (α-PFT) contains single, two, and three component members. Structures of the single component Eschericia coli ClyA and the two component Yersinia enterolytica YaxAB show both undergo conformational changes from soluble to pore forms, and oligomerization to produce the active pore. Here we identify tripartite α-PFTs in pathogenic Gram negative bacteria, including Aeromonas hydrophila (AhlABC). We show that the AhlABC toxin requires all three components for maximal cell lysis. We present structures of pore components which describe a bi-fold hinge mechanism for soluble to pore transition in AhlB and a contrasting tetrameric assembly employed by soluble AhlC to hide their hydrophobic membrane associated residues. We propose a model of pore assembly where the AhlC tetramer dissociates, binds a single membrane leaflet, recruits AhlB promoting soluble to pore transition, prior to AhlA binding to form the active hydrophilic lined pore.


    Item Type: Article
    School: Birkbeck Faculties and Schools > Faculty of Science > School of Natural Sciences
    SWORD Depositor: Mr Joe Tenant
    Depositing User: Mr Joe Tenant
    Date Deposited: 05 Aug 2019 10:06
    Last Modified: 02 Aug 2023 17:52


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