Architecture of the Helicobacter pylori Cag-type IV secretion system

Authors


L. Terradot, Institut de Biologie et Chimie des Protéines, Biologie Structurale des Complexes Macromoléculaires Bactériens, UMR 5086 CNRS Université de Lyon, IFR128, 7 Passage du Vercors, F-69367 Lyon Cedex 07, France
Fax: +33 472 722604
Tel: +33 472 722652
E-mail: laurent.terradot@ibcp.fr and
G. Waksman, Institute of Structural and Molecular Biology, UCL and Birkbeck, Malet Street, London, WC1E 7HX, UK
Fax: +44 (0)207 631 6803
Tel: +44 (0)207 631 6833
E-mail: g.waksman@bbk.ac.uk or g.waksman@ucl.ac.uk

Abstract

Type IV secretion systems (T4SS) are macromolecular assemblies used by bacteria to transport material across their membranes. T4SS are generally composed of a set of twelve proteins (VirB1–11 and VirD4). This represents a dynamic machine powered by three ATPases. T4SS are widespread in pathogenic bacteria where they are often used to deliver effectors into host cells. For example, the human pathogen Helicobacter pylori encodes a T4SS, the Cag-T4SS, which mediates the injection of the toxin CagA. We review the progress made in the past decade in our understanding of T4SS architecture. We translate this new knowledge to derive an understanding of the structure of the H. pylori Cag system, and use recent protein–protein interaction data to refine this model.

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