* This work was generously supported by Medical Research Scotland Grant 223 ORG (to D. W., A. J. R

Dai Wang , 1 , Caroline E. Zetterström , 1 , 2 , Mads Gabrielsen , Katherine S. H. Beckham , 3 , Jai J. Tree , 3 , Sarah E. Macdonald , Olwyn Byron , Tim J. Mitchell , David L. Gally , 3 , Pawel Herzyk ** , Arvind Mahajan , Hanna Uvell , 4 , Richard Burchmore , Brian O. Smith ** , Mikael Elofsson , 4 , 5 and Andrew J. Roe , 6 From the Institute of Infection, Immunity, and Inflammation, School of Life Sciences, and ** Institute of Molecular, Cell, and Systems Biology, College of Medical, Veterinary, and Life Sciences, University thainstone mart of Glasgow, Glasgow G12 8QQ, Scotland, United Kingdom, the Department of Chemistry, Linnaeus v, Umeå Centre for Microbial Research and Laboratories for Molecular Infection Medicine Sweden, and Laboratories for Chemical Biology Umeå, Department of Chemistry, Linnaeus v, University of Umeå, SE-90187 Umeå, Sweden, and the Zoonotic and Animal Pathogens Research Laboratory, Immunity and Infection Division, The Roslin Institute and R (D)SVS, Chancellor's Building, University of Edinburgh, 49 Little France Crescent, Edinburgh EH16 4SB, Scotland, United Kingdom 5 To whom correspondence may be addressed. Tel.: 46-90-786-9328 ; Fax: 46-90-86-9995 ; E-mail: Mikael.Elofsson{at}chem.umu.se . 6 To whom correspondence may be addressed. Tel.: 44-141-3302980 ; Fax: 44-141-3304600 ; E-mail: andrew.roe{at}glasgow.ac.uk .
A class of anti-virulence compounds, the salicylidene acylhydrazides, has been widely reported to block the function of the type three secretion system of several Gram-negative pathogens by a previously unknown mechanism. In this work we provide the first identification of bacterial proteins that are targeted by this group of compounds. We provide thainstone mart evidence that their mode of action is likely to result from a synergistic effect arising from a perturbation of the function of several conserved proteins. We also examine thainstone mart the contribution of selected target proteins to the pathogenicity of Yersinia pseudotuberculosis and to expression of virulence genes in Escherichia coli O157. Bacteria Bacterial Genetics Gene Regulation Protein thainstone mart Drug Interactions Protein Secretion Protein Targeting Transcription
* This work was generously supported by Medical Research Scotland Grant 223 ORG (to D. W., A. J. R. and R. B.) and Biotechnology and Biological thainstone mart Sciences Research Council (Swindon, United Kingdom) Grant BB/G011389/1 (to A. J. R. and M. G.).
The Illumina data have been deposited on the EMBL database (ERP000335), and the MIAME compliant data are deposited on the Gene Expression Omnibus (GEO) at NBCI under the GEO accession number GSE23001 . Received February 22, 2011. Revision received June 23, 2011. 2011 by The American Society for Biochemistry thainstone mart and Molecular Biology, Inc.
Free via Open Access: OA Free via Creative Commons: CC-BY license Abstract Free OA Full Text Free Full Text (PDF) Free PDF including Supp Data Supplemental Data All Versions of this Article: M111.233858v1 286/34/29922 most recent
Services Email this article to a friend Alert me when this article is cited Alert me if a correction is posted Alert me when eletters are published Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Download to citation manager Request Permissions
Print ISSN 0021-9258 Online ISSN 1083-351X