Enterohaemorrhagic and enteropathogenic <i>Escherichia coli</i> use a different Tir‐based mechanism for pedestal formation

DeVinney, Rebekah; Puente, José L.; Gauthier, Annick; Goosney, Danika L.; Finlay, B. Brett

doi:10.1046/j.1365-2958.2001.02617.x

Cited by 103 publications

(110 citation statements)

References 64 publications

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“…Los mecanismos fisiopatológicos que originan el cuadro diarreico se relacionan principalmente con la alteración de la célula intestinal debido a la lesión de adhesión y borrado (A/E: attaching/effacing) y a la formación de pedestales 15,16 .…”

Section: Escherichia Coli Enteropatógenaunclassified

Mecanismos de virulencia de Escherichia coli enteropatógena

Farfán-García¹,

Ariza-Rojas²,

Vargas-Cárdenas³

et al. 2016

Rev. chil. infectol.

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Section: Escherichia Coli Enteropatógenaunclassified

Mecanismos de virulencia de Escherichia coli enteropatógena

Farfán-García¹,

Ariza-Rojas²,

Vargas-Cárdenas³

et al. 2016

Rev. chil. infectol.

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“…61 EPEC strains Dtir, 9 Deae (Intimin) CVD206 62 and polyclonal Abs anti-Tir, 9 anti-EspB 63 and anti-EspF. 64 EPEC strains Deae and Dtir are nalidixic acidresistant (25 mg/ml).…”

Section: Cells Bacteria and Antibodiesmentioning

confidence: 99%

Nck adaptors, besides promoting N-WASP mediated actin-nucleation activity at pedestals, influence the cellular levels of enteropathogenicEscherichia coliTir effector

Nieto-Pelegrín

Kenny

Martı́nez-Quiles

2014

Cell Adhesion & Migration

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Enteropathogenic Escherichia coli (EPEC) binding to human intestinal cells triggers the formation of diseaseassociated actin rich structures called pedestals. The latter process requires the delivery, via a Type 3 secretion system, of the translocated Intimin receptor (Tir) protein into the host plasma membrane where binding of a host kinasemodified form to the bacterial surface protein Intimin triggers pedestal formation. Tir-Intimin interaction recruits the Nck adaptor to a Tir tyrosine phosphorylated residue where it activates neural Wiskott-Aldrich syndrome protein (N-WASP); initiating the major pathway to actin polymerization mediated by the actin-related protein (Arp) 2/3 complex. Previous studies with Nck-deficient mouse embryonic fibroblasts (MEFs) identified a key role for Nck in pedestal formation, presumed to reflect a lack of N-WASP activation. Here, we show the defect relates to reduced amounts of Tir within Nck-deficient cells. Indeed, Tir delivery and, thus, pedestal formation defects were much greater for MEFs than HeLa (human epithelial) cells. Crucially, the levels of two other effectors (EspB/EspF) within Nck-deficient MEFs were not reduced unlike that of Map (Mitochondrial associated protein) which, like Tir, requires CesT chaperone function for efficient delivery. Interestingly, drugs blocking various host protein degradation pathways failed to increase Tir cellular levels unlike an inhibitor of deacetylase activity (Trichostatin A; TSA). Treatments with TSA resulted in significant recovery of Tir levels, potentiation of actin polymerization and improvement in bacterial attachment to cells. Our findings have important implications for the current model of Tir-mediated actin polymerization and opens new lines of research in this area.

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“…75,2011 VARIATIONS IN MECHANISMS OF EPSILONPROTEOBACTERIA 111 phosphorylate tyrosine, serine, and threonine residues of Tir, which results in blockage of inhibitory pathways for actin polymerization (198,227,630). As a result, EHEC and EPEC manipulate actin polymerization to form the pedestals necessary to initiate and maintain intimate adherence (133,227). The Tir proteins of EPEC and EHEC are not interchangeable and use different pathways to alter actin polymerization (133,321).…”

Section: Alteration Of Host Cells To Create An Extracellular Nichementioning

confidence: 99%

“…As a result, EHEC and EPEC manipulate actin polymerization to form the pedestals necessary to initiate and maintain intimate adherence (133,227). The Tir proteins of EPEC and EHEC are not interchangeable and use different pathways to alter actin polymerization (133,321). Phosphorylation of EPEC Tir allows for the formation of a docking site for Nck adaptor proteins (227).…”

Section: Alteration Of Host Cells To Create An Extracellular Nichementioning

confidence: 99%

“…This binding of Nck proteins results in the loss of autoinhibition of N-WASP, which culminates in activation of Arp2/3 and in actin polymerization (227). However, EHEC strains use an Nck-independent pathway by injecting a non-LEE-encoded effector, EspF u , into host cells (75,133,198). EspF u directly relieves N-WASP from autoinhibition, which begins a cascade of events leading to actin polymerization (75).…”

Section: Alteration Of Host Cells To Create An Extracellular Nichementioning

confidence: 99%

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Change Is Good: Variations in Common Biological Mechanisms in the Epsilonproteobacterial GeneraCampylobacterandHelicobacter

Gilbreath

Cody

Merrell

et al. 2011

Microbiol Mol Biol Rev

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SUMMARY Microbial evolution and subsequent species diversification enable bacterial organisms to perform common biological processes by a variety of means. The epsilonproteobacteria are a diverse class of prokaryotes that thrive in diverse habitats. Many of these environmental niches are labeled as extreme, whereas other niches include various sites within human, animal, and insect hosts. Some epsilonproteobacteria, such as Campylobacter jejuni and Helicobacter pylori , are common pathogens of humans that inhabit specific regions of the gastrointestinal tract. As such, the biological processes of pathogenic Campylobacter and Helicobacter spp. are often modeled after those of common enteric pathogens such as Salmonella spp. and Escherichia coli . While many exquisite biological mechanisms involving biochemical processes, genetic regulatory pathways, and pathogenesis of disease have been elucidated from studies of Salmonella spp. and E. coli , these paradigms often do not apply to the same processes in the epsilonproteobacteria. Instead, these bacteria often display extensive variation in common biological mechanisms relative to those of other prototypical bacteria. In this review, five biological processes of commonly studied model bacterial species are compared to those of the epsilonproteobacteria C. jejuni and H. pylori . Distinct differences in the processes of flagellar biosynthesis, DNA uptake and recombination, iron homeostasis, interaction with epithelial cells, and protein glycosylation are highlighted. Collectively, these studies support a broader view of the vast repertoire of biological mechanisms employed by bacteria and suggest that future studies of the epsilonproteobacteria will continue to provide novel and interesting information regarding prokaryotic cellular biology.

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Enterohaemorrhagic and enteropathogenic Escherichia coli use a different Tir‐based mechanism for pedestal formation

Cited by 103 publications

References 64 publications

Mecanismos de virulencia de Escherichia coli enteropatógena

Mecanismos de virulencia de Escherichia coli enteropatógena

Nck adaptors, besides promoting N-WASP mediated actin-nucleation activity at pedestals, influence the cellular levels of enteropathogenicEscherichia coliTir effector

Change Is Good: Variations in Common Biological Mechanisms in the Epsilonproteobacterial GeneraCampylobacterandHelicobacter

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