TccP2-mediated subversion of actin dynamics by EPEC 2 - a distinct evolutionary lineage of enteropathogenic Escherichia coli
Autor(a) principal: | |
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Data de Publicação: | 2007 |
Outros Autores: | , , , , , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNIFESP |
Texto Completo: | http://repositorio.unifesp.br/handle/11600/29767 http://dx.doi.org/10.1099/mic.0.2006/004325-0 |
Resumo: | 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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Whale, Andrew D.Hernandes, Rodrigo T. [UNIFESP]Ooka, TadasukeBeutin, LotharSchuller, StephanieGarmendia, JunkalCrowther, LynetteVieira, Mônica Aparecida Midolli [UNIFESP]Ogura, YoshitoshiKrause, GladysIllips, Alan D. PhGomes, Tania A. T.Hayashi, TetsuyaFrankel, GadUniv London Imperial Coll Sci Technol & MedUniversidade Federal de São Paulo (UNIFESP)Miyazaki UnivBundesinst RisikobewertungUCL Royal Free & Univ Coll Med SchRecinto Hosp Joan March2016-01-24T13:48:45Z2016-01-24T13:48:45Z2007-06-01Microbiology-sgm. Reading: Soc General Microbiology, v. 153, p. 1743-1755, 2007.1350-0872http://repositorio.unifesp.br/handle/11600/29767http://dx.doi.org/10.1099/mic.0.2006/004325-0WOS000247304900007.pdf10.1099/mic.0.2006/004325-0WOS:000247304900007Enteropathogenic 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.Univ London Imperial Coll Sci Technol & Med, Div Cell & Mol Biol, London SW7 2AZ, EnglandUniversidade Federal de São Paulo, Dept Microbiol Imunol & Parasitol, São Paulo, BrazilMiyazaki Univ, Frontier Sci Res Ctr, Div Bioenvironm Sci, Miyazaki 8891692, JapanBundesinst Risikobewertung, Natl Referenzlab Escherichia Coli, D-12277 Berlin, GermanyUCL Royal Free & Univ Coll Med Sch, Ctr Paediat Gastroenterol, London, EnglandRecinto Hosp Joan March, Fdn Caubet Cimera, Bunyola, Mallorca, SpainUniversidade Federal de São Paulo, Dept Microbiol Imunol & Parasitol, São Paulo, BrazilWeb of Science1743-1755engSoc General MicrobiologyMicrobiology-sgmTccP2-mediated subversion of actin dynamics by EPEC 2 - a distinct evolutionary lineage of enteropathogenic Escherichia coliinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleinfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESPORIGINALWOS000247304900007.pdfapplication/pdf1098590${dspace.ui.url}/bitstream/11600/29767/1/WOS000247304900007.pdf51584de4b821f60f006da244155cd29dMD51open accessTEXTWOS000247304900007.pdf.txtWOS000247304900007.pdf.txtExtracted texttext/plain58744${dspace.ui.url}/bitstream/11600/29767/2/WOS000247304900007.pdf.txtc6aa8d64e9644e068e503177b7f26df8MD52open access11600/297672022-11-03 10:40:49.222open accessoai:repositorio.unifesp.br:11600/29767Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestopendoar:34652023-05-25T12:27:42.945724Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false |
dc.title.en.fl_str_mv |
TccP2-mediated subversion of actin dynamics by EPEC 2 - a distinct evolutionary lineage of enteropathogenic Escherichia coli |
title |
TccP2-mediated subversion of actin dynamics by EPEC 2 - a distinct evolutionary lineage of enteropathogenic Escherichia coli |
spellingShingle |
TccP2-mediated subversion of actin dynamics by EPEC 2 - a distinct evolutionary lineage of enteropathogenic Escherichia coli Whale, Andrew D. |
title_short |
TccP2-mediated subversion of actin dynamics by EPEC 2 - a distinct evolutionary lineage of enteropathogenic Escherichia coli |
title_full |
TccP2-mediated subversion of actin dynamics by EPEC 2 - a distinct evolutionary lineage of enteropathogenic Escherichia coli |
title_fullStr |
TccP2-mediated subversion of actin dynamics by EPEC 2 - a distinct evolutionary lineage of enteropathogenic Escherichia coli |
title_full_unstemmed |
TccP2-mediated subversion of actin dynamics by EPEC 2 - a distinct evolutionary lineage of enteropathogenic Escherichia coli |
title_sort |
TccP2-mediated subversion of actin dynamics by EPEC 2 - a distinct evolutionary lineage of enteropathogenic Escherichia coli |
author |
Whale, Andrew D. |
author_facet |
Whale, Andrew D. Hernandes, Rodrigo T. [UNIFESP] Ooka, Tadasuke Beutin, Lothar Schuller, Stephanie Garmendia, Junkal Crowther, Lynette Vieira, Mônica Aparecida Midolli [UNIFESP] Ogura, Yoshitoshi Krause, Gladys Illips, Alan D. Ph Gomes, Tania A. T. Hayashi, Tetsuya Frankel, Gad |
author_role |
author |
author2 |
Hernandes, Rodrigo T. [UNIFESP] Ooka, Tadasuke Beutin, Lothar Schuller, Stephanie Garmendia, Junkal Crowther, Lynette Vieira, Mônica Aparecida Midolli [UNIFESP] Ogura, Yoshitoshi Krause, Gladys Illips, Alan D. Ph Gomes, Tania A. T. Hayashi, Tetsuya Frankel, Gad |
author2_role |
author author author author author author author author author author author author author |
dc.contributor.institution.none.fl_str_mv |
Univ London Imperial Coll Sci Technol & Med Universidade Federal de São Paulo (UNIFESP) Miyazaki Univ Bundesinst Risikobewertung UCL Royal Free & Univ Coll Med Sch Recinto Hosp Joan March |
dc.contributor.author.fl_str_mv |
Whale, Andrew D. Hernandes, Rodrigo T. [UNIFESP] Ooka, Tadasuke Beutin, Lothar Schuller, Stephanie Garmendia, Junkal Crowther, Lynette Vieira, Mônica Aparecida Midolli [UNIFESP] Ogura, Yoshitoshi Krause, Gladys Illips, Alan D. Ph Gomes, Tania A. T. Hayashi, Tetsuya Frankel, Gad |
description |
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. |
publishDate |
2007 |
dc.date.issued.fl_str_mv |
2007-06-01 |
dc.date.accessioned.fl_str_mv |
2016-01-24T13:48:45Z |
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2016-01-24T13:48:45Z |
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info:eu-repo/semantics/publishedVersion |
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info:eu-repo/semantics/article |
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article |
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publishedVersion |
dc.identifier.citation.fl_str_mv |
Microbiology-sgm. Reading: Soc General Microbiology, v. 153, p. 1743-1755, 2007. |
dc.identifier.uri.fl_str_mv |
http://repositorio.unifesp.br/handle/11600/29767 http://dx.doi.org/10.1099/mic.0.2006/004325-0 |
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1350-0872 |
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WOS000247304900007.pdf |
dc.identifier.doi.none.fl_str_mv |
10.1099/mic.0.2006/004325-0 |
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WOS:000247304900007 |
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Microbiology-sgm. Reading: Soc General Microbiology, v. 153, p. 1743-1755, 2007. 1350-0872 WOS000247304900007.pdf 10.1099/mic.0.2006/004325-0 WOS:000247304900007 |
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http://repositorio.unifesp.br/handle/11600/29767 http://dx.doi.org/10.1099/mic.0.2006/004325-0 |
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Soc General Microbiology |
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Soc General Microbiology |
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