Crystal structure of enteropathogenic Escherichia coli intimin–receptor complex

Luo, Yu; Frey, Elizabeth A.; Pfuetzner, Richard A.; Creagh, A. Louise; Knoechel, D.G.; Haynes, Chad; Finlay, B. Brett; Strynadka, N.C.J.

doi:10.1038/35016618

Cited by 307 publications

(334 citation statements)

References 27 publications

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“…Different types of Tir proteins have also been described. Since the interaction between intimin and Tir is located in the 280 carboxy terminal amino-acids of the intimin adhesin, the different intimin types specifically interact with their cognate Tir receptor Hartland et al, 1999;Luo et al, 2000;Karmali et al, 2010;Schmidt, 2010). Alternative host receptors for the intimin adhesin are ␤1 integrins and nucleolin (Garmendia et al, 2005).…”

Section: Outer Membrane Proteins (Omps)mentioning

confidence: 99%

Escherichia coli virulence factors

Mainil

2013

Veterinary Immunology and Immunopathology

123

104

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a b s t r a c t Escherichia coli was described in 1885 by a German pediatrician, Theodor Escherich, in the faeces of a child suffering diarrhoea. In 1893, a Danish veterinarian postulated that the E. coli species comprises different strains, some being pathogens, others not. Today the E. coli species is subdivided into several pathogenic strains causing different intestinal, urinary tract or internal infections and pathologies, in animal species and in humans. Since this congress topic is the interaction between E. coli and the mucosal immune system, the purpose of this manuscript is to present different classes of adhesins (fimbrial adhesins, afimbrial adhesins and outer membrane proteins), the type 3 secretion system, and some toxins (oligopeptide, AB, and RTX pore-forming toxins) produced by E. coli, that can directly interact with the epithelial cells of the intestinal, respiratory and urinary tracts.

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Section: Outer Membrane Proteins (Omps)mentioning

confidence: 99%

Escherichia coli virulence factors

Mainil

2013

Veterinary Immunology and Immunopathology

123

104

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“…The solution (Kelly et al , 1999) and crystal (Luo et al , 2000) 3D structure of Int280 α revealed that the polypeptide comprises a series of three globular modules with a distinct organization. The two domains (D1–2) closest to the bacterial cell surface comprise β -sheet sandwiches and structurally resemble immunoglobulin (Ig)-like folds.…”

Section: Introductionmentioning

confidence: 99%

Functional studies of intimin in vivo and ex vivo: implications for host specificity and tissue tropism

et al. 2007

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Intimin is an outer-membrane adhesin that is essential for colonization of the host gastrointestinal tract by attaching and effacing pathogens including enteropathogenic Escherichia coli (EPEC), enterohaemorrhagic E. coli (EHEC) and Citrobacter rodentium (CR). The N-terminus of intimin from the different strains is highly conserved while the C-terminus, which harnesses the active receptor-binding site, shows sequence and antigenic polymorphism. This diversity was used to define a number of distinct intimin types, the most common of which are α, β and γ. Intimin binds the type III secretion system effector protein Tir. However, a large body of evidence suggests that intimin also binds a host-cell-encoded receptor(s) (Hir), and interaction of different intimin types with Hir contributes to tissue and host specificity. The aims of this study were to compare the activity of the major intimin types (α, β and γ) in vivo and ex vivo, using the CR mouse model and in vitro organ culture (IVOC), and to determine their exchangeability. The results confirm that intimin γ is not functional in the CR mouse model. In the pig, intimin β can substitute for EPEC intimin α but when placed in an EHEC O157 : H7 background it does not produce an intimin α-like tropism, although some adhesion to the small and large intestine was observed. In contrast, in human IVOC, intimin β in an EHEC background produces small intestinal colonization in a similar manner to intimin α.

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“…Tir is one of the virulence factors termed "effectors," which are delivered directly into the host cytoplasm through bacterial secretion machinery termed the type III secretion system (TTSS) (24,46). The secreted Tir is in turn integrated into the plasma membrane and binds with a bacterial outer membrane protein, intimin (31). The binding induces the clustering of the membrane-associated Tir beneath the bacteria, which activates an Nck adaptor molecule at the cytoplasmic face of the plasma membrane and finally results in activation of neural Wiskott-Aldrich syndrome protein (N-WASP) and the downstream actin-nucleating Arp2/3 complex (19,23).…”

mentioning

confidence: 99%

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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Crystal structure of enteropathogenic Escherichia coli intimin–receptor complex

Cited by 307 publications

References 27 publications

Escherichia coli virulence factors

Escherichia coli virulence factors

Functional studies of intimin in vivo and ex vivo: implications for host specificity and tissue tropism

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

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