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Infect. Immun. doi:10.1128/IAI.01491-06
Copyright (c) 2006, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

TccP2 of O157:H7 and non-O157 enterohemorrhagic Escherichia coli (EHEC): challenging the dogma of EHEC-induced actin polymerization

Division of Bioenvironmental Science, Frontier Science Research Center, University of Miyazaki, 5200 Kiyotake, Miyazaki 889-1692, Japan; Division of Cell and Molecular Biology, Imperial College London, London SW7 2AZ, UK; Nationales Referenzlabor für Escherichia coli, Bundesinstitut für Risikobewertung, Diedersdorfer Weg 1, D-12277 Berlin, Germany; Department of Microbiology and Immunology, University of Melbourne, Victoria, Australia; Dipartimento di Sanità Alimentare e Animale Istituto Superiore di Sanità, 00161 Rome, Italy; Instituto Nacional de Enfermedades Infecciosas, 1281 Buenos Aires, Argentina; and Graduate School of Medicine, Osaka University, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan

^* To whom correspondence should be addressed. Email: g.frankel{at}imperial.ac.uk.

	Abstract

Enterohemorrhagic Escherichia coli (EHEC) O157:H7 and enteropathogenic E. coli (EPEC), trigger actin polymerization at the site of bacterial adhesion by inducing different signaling pathways. Actin assembly by EPEC requires tyrosine phosphorylation of Tir, which subsequently binds the host adaptor protein Nck. In contrast, Tir_EHECO157 is not tyrosine phosphorylated and instead of Nck utilizes the bacterially encoded Tir-cytoskeleton coupling protein (TccP)/EspF_U, which mimics the function of Nck. tccP is carried on prophage CP-933U/Sp14 (TccP). Typical isolates of EHEC O157:H7 harbor a pseudo-tccP gene that is carried on prophage CP-933M/Sp4 (tccP2). Here we report that atypical, -glucuronidase-positive and sorbitol fermenting, strains of EHEC O157 harbor intact tccP and tccP2 genes, both of which are secreted by the LEE-encoded type III secretion system. Non-O157 EHEC strains, including O26, O103, O111 and O145, are typically tccP negative and translocate Tir that encompasses an Nck binding site. Unexpectedly, we found that most clinical non-O157 EHEC isolates carry a functional tccP2 that encodes a secreted protein which can complement an EHEC O157:H7tccP mutant. Using discriminatory, allele-specific, PCR we demonstrated that over 90% of the tccP2-positive non-O157 EHEC contain Tir that can be tyrosine phosphorylated. These results suggest that the TccP pathway can be used by both O157 and non-O157 EHEC and that non-O157 EHEC can also trigger actin polymerization via the Nck pathway.

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