Enteropathogenic
            <i>Escherichia coli</i>
            Activates Ezrin, Which Participates in Disruption of Tight Junction Barrier Function

Simonović, Ivana; Arpin, Monique; Koutsouris, Athanasia; Falk-Krzesinski, Holly J.; Hecht, Gail

doi:10.1128/iai.69.9.5679-5688.2001

Cited by 81 publications

(56 citation statements)

References 62 publications

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“…Upon infection by EPEC, the peripheral lining of ZO-1 began to disperse at 3 h postinfection and became discontinuous at 5 h or later. These changes are basically consistent with the observations made with T84 monolayers (10,37,43,48). In addition to these changes, we noticed the recruitment of ZO-1 to the sites of bacterial attachment (Fig.…”

Section: Resultssupporting

confidence: 81%

Enteropathogenic Escherichia coli , Shigella flexneri , and Listeria monocytogenes Recruit a Junctional Protein, Zonula Occludens-1, to Actin Tails and Pedestals

et al. 2007

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Enteropathogenic Escherichia coli, Shigella flexneri, and Listeria monocytogenes induce localized actin polymerization at the cytoplasmic face of the plasma membrane or within the host cytoplasm, creating unique actin-rich structures termed pedestals or actin tails. The process is known to be mediated by the actin-related protein 2 and 3 (Arp2/3) complex, which in these cases acts downstream of neural Wiskott-Aldrich syndrome protein (N-WASP) or of a listerial functional homolog of WASP family proteins. Here, we show that zonula occludens-1 (ZO-1), a protein in the tight junctions of polarized epithelial cells, is recruited to actin tails and pedestals. Immunocytochemical analysis revealed that ZO-1 was stained most in the distal part of the actin-rich structures, and the incorporation was mediated by the proline-rich region of the ZO-1 molecule. The direct clustering of membrane-targeted Nck, which is known to activate the N-WASP-Arp2/3 pathway, triggered the formation of the ZO-1-associated actin tails. The results suggest that the activation of the Arp2/3 complex downstream of N-WASP or a WASP-related molecule is a key to the formation of the particular actin-rich structures that bind with ZO-1. We propose that an analysis of the recruitment on a molecular basis will lead to an understanding of how ZO-1 recognizes a distinctive actin-rich structure under pathophysiological conditions.

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Section: Resultssupporting

confidence: 81%

Enteropathogenic Escherichia coli , Shigella flexneri , and Listeria monocytogenes Recruit a Junctional Protein, Zonula Occludens-1, to Actin Tails and Pedestals

et al. 2007

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“…Many pathogens disrupt tight junctions during invasion through activation of cytoskeletal components (Sears, 2000;Simonovic et al, 2001). Occludin is a major transmembrane protein that localizes at the tight junction.…”

Section: Effect Of Cryptococcus Cells On Solubility Of Hbmec Occludinmentioning

confidence: 99%

Cryptococcus neoformans induces alterations in the cytoskeleton of human brain microvascular endothelial cells

Chen

Stins

Huang

et al. 2003

Journal of Medical Microbiology

169

200

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The fungal pathogen Cryptococcus neoformans has a predilection for the central nervous system (CNS), resulting in devastating meningoencephalitis. At present, it is unclear how C. neoformans traverses the blood-brain barrier (BBB) and causes CNS infection. The present study has examined and characterized the interaction of C. neoformans with human brain microvascular endothelial cells (HBMEC), which constitute the BBB. Adhesion of and transcytosis of HBMEC by C. neoformans was inoculum-and time-dependent and occurred with both encapsulated and acapsulated strains. C. neoformans induced marked morphological changes in HBMEC, for example membrane ruffling, irregular nuclear morphology and swelling of the mitochondria and the ER. These findings suggest that C. neoformans induced actin cytoskeletal reorganization of the host cells. In addition, it was observed that the dephosphorylated form of cofilin was increased during cryptococcal adherence to HBMEC, concomitant with the actin rearrangement. Cryptococcal binding to HBMEC was increased in the presence of Y27632, a Rho kinase (ROCK)-specific inhibitor. Since ROCK activates LIM kinase (LIMK), which phosphorylates cofilin (inactive form), this suggests the involvement of the ROCK!LIMK!cofilin pathway. In contrast, the phosphatase inhibitor sodium orthovanadate decreased adherence of Cryptococcus to HBMEC, concomitant with the increase of phosphorylation of cofilin. Furthermore, the tight junction marker protein occludin became Tritonextractable, indicating alteration of tight junctions in brain endothelial cells. This is the first demonstration that C. neoformans is able to adhere to and transcytose across the HBMEC monolayer and alter the cytoskeleton morphology in HBMEC. Further characterization of the interactions between C. neoformans and HBMEC should help the development of novel strategies to prevent cryptococcal meningitis and its associated morbidity.

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“…47 Upon EPEC infection, ezrin is relocalized to the pedestal, where it gets phosphorylated and activated. 48 This effect is EspB and EspF dependent, and results in the redistribution of ZO-1 and a subsequent decrease in TER. 48 The adherens junctions do not escape the disruptive effects of EPEC.…”

Section: Disruption Of Epithelial Barrier Structure and Functionmentioning

confidence: 99%

“…48 This effect is EspB and EspF dependent, and results in the redistribution of ZO-1 and a subsequent decrease in TER. 48 The adherens junctions do not escape the disruptive effects of EPEC. EspB-mediated phosphorylation and subsequent activation of PKCa have been reported during EPEC infection, increasing its association with the transmembrane protein E-cadherin.…”

Section: Disruption Of Epithelial Barrier Structure and Functionmentioning

confidence: 99%

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The role of epithelial malfunction in the pathogenesis of enteropathogenic E. coli-induced diarrhea

Lapointe

O'Connor

Buret

2009

Laboratory Investigation

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The homeostatic balance of the gastrointestinal tract relies on a single layer of epithelial cells, which assumes both digestive and protective functions. Enteric pathogens, including enteropathogenic Escherichia coli (EPEC), have evolved numerous mechanisms to disrupt basic intestinal epithelial functions, promoting the development of gastrointestinal disorders. Despite its non-invasive nature, EPEC inflicts severe damage to the intestinal mucosa, including the dysregulation of water and solute transport and the disruption of epithelial barrier structure and function. Despite the high prevalence and morbidity of disease caused by EPEC infections, the etiology of its pathogenesis remains incompletely understood. This review integrates the newest findings on EPEC-epithelial interactions with established mechanisms of disease in an attempt to give a comprehensive understanding of the cellular processes whereby this common pathogen may cause diarrheal illness.

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Enteropathogenic Escherichia coli Activates Ezrin, Which Participates in Disruption of Tight Junction Barrier Function

Cited by 81 publications

References 62 publications

Enteropathogenic Escherichia coli , Shigella flexneri , and Listeria monocytogenes Recruit a Junctional Protein, Zonula Occludens-1, to Actin Tails and Pedestals

Enteropathogenic Escherichia coli , Shigella flexneri , and Listeria monocytogenes Recruit a Junctional Protein, Zonula Occludens-1, to Actin Tails and Pedestals

Cryptococcus neoformans induces alterations in the cytoskeleton of human brain microvascular endothelial cells

The role of epithelial malfunction in the pathogenesis of enteropathogenic E. coli-induced diarrhea

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