Identifier to cite or link to this item: http://hdl.handle.net/20.500.13003/15829
TccP2-mediated subversion of actin dynamics by EPEC 2 - a distinct evolutionary lineage of enteropathogenic Escherichia coli
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ISSN: 1350-0872
eISSN: 1465-2080
WOS ID: 000247304900007
Scopus EID: 2-s2.0-34247847571
PMID: 17526832
Embase PUI: L46952505
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2007-06Document type
research articleCitation
Whale AD, Hernandes RT, Ooka T, Beutin L, Schuller S, Garmendia J, et al. TccP2-mediated subversion of actin dynamics by EPEC 2 - a distinct evolutionary lineage of enteropathogenic Escherichia coli. Microbiology-(UK). 2007 Jun;153:1743-55.Abstract
Enteropathogenic Escherichia coli (EPEC) is a major cause of infantile diarrhoea in developing countries. While colonizing the gut mucosa, EPEC triggers extensive actin-polymerization activity at the site of intimate bacterial attachment, which is mediated by avid interaction between the outer-membrane adhesin intimin and the type III secretion system (T3SS) effector Tir. The prevailing dogma is that actin polymerization by EPEC is achieved following tyrosine phosphorylation of Tir, recruitment of Nck and activation of neuronal Wiskott-Aldrich syndrome protein (N-WASP). In closely related enterohaemorrhagic E. coli (EHEC) O157 : H7, actin polymerization is triggered following recruitment of the T3SS effector TccP/EspF(U) (instead of Nck) and local activation of N-WASP. In addition to tccP, typical EHEC O157 : H7 harbour a pseudogene (tccP2). However, it has recently been found that atypical, sorbitol-fermenting EHEC O157 carries functional tccP and tccP2 alleles. Interestingly, intact tccP2 has been identified in the incomplete genome sequence of the prototype EPEC strain B171 (serotype O111 : H-), but it is missing from another prototype EPEC strain E2348/69 (O127 : H7). E2348/69 and B171 belong to two distinct evolutionary lineages of EPEC, termed EPEC 1 and EPEC 2, respectively. Here, it is reported that while both EPEC 1 and EPEC 2 triggered actin polymerization via the Nck pathway, tccP2 was found in 26 of 27 (96.2%) strains belonging to EPEC 2, and in none of the 34 strains belonging to EPEC 1. It was shown that TccP2 was: (i) translocated by the locus of enterocyte effacement-encoded T3SS; (ii) localized at the tip of the EPEC 2-induced actin-rich pedestals in infected HeLa cells and human intestinal in vitro organ cultures ex vivo; and (iii) essential for actin polymerization in infected Nck-/- cells. Therefore, unlike strains belonging to EPEC 1, strains belonging to EPEC 2 can trigger actin polymerization using both Nck and TccP2 actin-polymerization signalling cascades.
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https://dx.doi.org/10.1099/mic.0.2006/004325-0MeSH
Escherichia coli ProteinsGene Deletion
Protein Transport
Molecular Sequence Data
DNA, Bacterial
Humans
Organ Culture Techniques
Microscopy, Electron, Scanning
HeLa Cells
Adaptor Proteins, Signal Transducing
Actins
Amino Acid Sequence
Intestine, Small
Microscopy, Confocal
Sequence Alignment
Oncogene Proteins
Polymerase Chain Reaction
Sequence Analysis, DNA
DeCS
Análisis de Secuencia de ADNProteínas Adaptadoras Transductoras de Señales
Microscopía Confocal
Proteínas Oncogénicas
Alineación de Secuencia
Intestino Delgado
Transporte de Proteínas
Técnicas de Cultivo de Órganos
Células HeLa
Datos de Secuencia Molecular
Actinas
Secuencia de Aminoácidos
Humanos
ADN Bacteriano
Proteínas de Escherichia coli
Microscopía Electrónica de Rastreo
Eliminación de Gen
Reacción en Cadena de la Polimerasa