IRSp53 links the enterohemorrhagic E. coli effectors Tir and EspFU for actin pedestal formation.
Cell Host Microbe
; 5(3): 244-58, 2009 Mar 19.
Article
em En
| MEDLINE
| ID: mdl-19286134
ABSTRACT
Actin pedestal formation by pathogenic E. coli requires signaling by the bacterial intimin receptor Tir, which induces host cell actin polymerization mediated by N-WASP and the Arp2/3 complex. Whereas canonical enteropathogenic E. coli (EPEC) recruit these actin regulators through tyrosine kinase signaling cascades, enterohemorrhagic E. coli (EHEC) O157H7 employ the bacterial effector EspF(U) (TccP), a potent N-WASP activator. Here, we show that IRSp53 family members, key regulators of membrane and actin dynamics, directly interact with both Tir and EspF(U). IRSp53 colocalizes with EspF(U) and N-WASP in actin pedestals. In addition, targeting of IRSp53 is independent of EspF(U) and N-WASP but requires Tir residues 454-463, previously shown to be essential for EspF(U)-dependent actin assembly. Genetic and functional loss of IRSp53 abrogates actin assembly mediated by EHEC. Collectively, these data indentify IRSp53 family proteins as the missing host cell factors linking bacterial Tir and EspF(U) in EHEC pedestal formation.
Texto completo:
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Base de dados:
MEDLINE
Assunto principal:
Proteínas de Transporte
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Receptores de Superfície Celular
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Escherichia coli O157
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Proteínas de Escherichia coli
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Mapeamento de Interação de Proteínas
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Interações Hospedeiro-Patógeno
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Proteínas do Tecido Nervoso
Limite:
Humans
Idioma:
En
Ano de publicação:
2009
Tipo de documento:
Article