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

Abstract

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.

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Item Type:	Article
Authors/Creators:	Wilson, JS Churchill-Angus, AM Davies, SP Sedelnikova, SE Tzokov, SB Rafferty, JB Bullough, PA Bisson, C Baker, PJ
Copyright, Publisher and Additional Information:	© Crown 2019. This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
Dates:	Published: 1 July 2019 Published (online): 1 July 2019 Accepted: 29 May 2019
Institution:	The University of Leeds
Academic Units:	The University of Leeds > Faculty of Biological Sciences (Leeds)
Depositing User:	Symplectic Publications
Date Deposited:	09 Jul 2019 12:56
Last Modified:	09 Jul 2019 12:56
Status:	Published
Publisher:	Nature Publishing Group
Identification Number:	10.1038/s41467-019-10777-x
Related URLs:	PubMed URL
Open Archives Initiative ID (OAI ID):	oai:eprints.whiterose.ac.uk:148265

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

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