Journal
MICROBES AND INFECTION
Volume 12, Issue 12-13, Pages 956-966Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.micinf.2010.06.006
Keywords
Shigella; IcsB; Autophagy; Cholesterol binding
Categories
Funding
- FNRS [3 4623 06]
- E Defay
- A Van Buuren foundation
- D Van Buuren foundation
- Canadian Association of Gastroenterology/Crohn's and Colitis Foundation of Canada/the Canadian Institutes of Health Research
- Canadian Institutes of Health Research and the Howard Hughes Medical Institute
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Type III secretion systems are present in many pathogenic bacteria and mediate the translocation of bacterial effectors into host cells Identification of host targets of these effectors is crucial for understanding bacterial virulence IcsB a type III secretion effector helps Shigella to evade the host autophagy defense system by binding to the autophagy protein Atg5 Here we show that IcsB is able to interact specifically with cholesterol The cholesterol binding domain (CBD) of IcsB is located between residues 288 and 351 Specific mutations of single tyrosine residues Y297 or Y340 of IcsB by phenylalanine (F) slightly reduced cholesterol binding whereas deletion of the entire CBD or double mutation Y297F Y340F strongly abolished interactions with cholesterol To determine whether Shigella expressing IcsB variants could evade autophagy as effectively as the wild type Shigella we infected MDAMC cells stably expressing the autophagy marker LC3 fused to GFP and bacterial autophagosome formation was quantified using fluorescence microscopy Mutation Y297F or Y340F slightly impaired IcsB function whereas complete removal of CBD or mutation Y297F-Y340F significantly impaired autophagy evasion Furthermore we report that BopA the counterpart of IcsB in Burkholderia pseudomallei with similar autophagy evading properties, contains the CBD domain and is also able to bind cholesterol (C) 2010 Institut Pasteur Published by Elsevier Masson SAS All rights reserved
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