Role of bundle-forming pilus of enteropathogenic<i>Escherichia coli</i>in host cell adherence and in microcolony development

Tobe, Toru; Sasakawa, Chihiro

doi:10.1046/j.1462-5822.2001.00136.x

Cited by 62 publications

(56 citation statements)

References 26 publications

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“…Bundle forming pili (BFP) are responsible for promoting the initial attachment of EPEC to epithelial cells (35). EHEC does not express BFP proteins.…”

Section: Resultsmentioning

confidence: 99%

Comparative Analysis of EspF from Enteropathogenic and Enterohemorrhagic Escherichia coli in Alteration of Epithelial Barrier Function

et al. 2004

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Enteropathogenic Escherichia coli (EPEC) and enterohemorrhagic E. coli (EHEC) are related intestinal pathogens that harbor highly similar pathogenicity islands known as the locus of enterocyte effacement (LEE). Despite their genetic similarity, these two pathogens disrupt epithelial tight junction barrier function with distinct kinetics. EHEC-induced reduction in transepithelial electrical resistance (TER), a measure of barrier function disruption, is significantly slower and more modest in comparison to that induced by EPEC. The variation in bacterial adherence only partially accounted for these differences. The LEE-encoded effector protein EspF has been shown to be critical for EPEC-induced alterations in TER. EspF from both EPEC and EHEC is expressed and secreted upon growth in tissue culture medium. The mutation of EHEC cesF suggested that the optimal expression and secretion of EHEC EspF required its chaperone CesF, as has been shown for EPEC. In contrast to EPEC espF and cesF, mutation of the corresponding EHEC homologs did not dramatically alter the decrease in TER. These differences could possibly be explained by the presence of additional espF-like sequences (designated U-and M-espF, where the letter designations refer to the specific cryptic prophage sequences on the EHEC chromosome closest to the respective genes) in EHEC. Reverse transcription-PCR analyses revealed coordinate regulation of EHEC U-espF and the LEE-encoded espF, with enhanced expression in bacteria grown in Dulbecco-Vogt modified Eagle's medium compared to bacteria grown in Luria broth. Both EHEC espF and U-espF complemented an EPEC espF deletion strain for barrier function alteration. The overexpression of U-espF, but not espF, in wild-type EHEC potentiated the TER response. These studies reveal further similarities and differences in the pathogenesis of EPEC and EHEC.

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“…Bundle forming pili (BFP) are responsible for promoting the initial attachment of EPEC to epithelial cells (35). EHEC does not express BFP proteins.…”

Section: Resultsmentioning

confidence: 99%

Comparative Analysis of EspF from Enteropathogenic and Enterohemorrhagic Escherichia coli in Alteration of Epithelial Barrier Function

et al. 2004

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“…The initial studies of Giron et al (1991) demonstrated a significant reduction in localized adherence of EPEC in the presence of BFP antibodies; residual adherence can now be explained by EspA filament and intimin-Tir adherence. Tobe & Sasakawa (2001) implicated BFP in host cell attachment by demonstrating preferential binding of BFP, producing EPEC to the Caco-2 cell surface rather than to existing EPEC microcolonies formed during an earlier infection. These authors also concluded that differential EPEC adherence to cells of different species origin was due to BFP (Tobe & Sasakawa, 2002).…”

Section: Discussionmentioning

confidence: 99%

“…Several studies have also implicated BFP in initial binding of EPEC to host epithelial cells (Donnenberg et al, 1992;Giron et al, 1991;Tobe & Sasakawa, 2001 although other studies which used human intestinal organ culture suggested that BFP were not involved in initial EPEC adherence but only at a later stage to promote microcolony formation (Hicks et al, 1998).…”

Section: Introductionmentioning

confidence: 99%

Enteropathogenic Escherichia coli (EPEC) adhesion to intestinal epithelial cells: role of bundle-forming pili (BFP), EspA filaments and intimin

et al. 2004

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Enteropathogenic Escherichia coli (EPEC), an important paediatric diarrhoeal pathogen, employs multiple adhesins to colonize the small bowel and produces characteristic 'attaching and effacing' (A/E) lesions on small intestinal enterocytes. EPEC adhesins that have been associated with A/E adhesion and intestinal colonization include bundle-forming pili (BFP), EspA filaments and intimin. BFP are involved in bacteria-bacteria interaction and microcolony formation but their role in cell adhesion remains unclear; EspA filaments are components of the EPEC type III secretion system but since they interact directly with host cells they may also function as adhesins; intimin is the well characterized intimate EPEC adhesin which binds the translocated intimin receptor, Tir. However, other uncharacterized host cell receptors have been implicated in intimin-mediated adhesion. In this study, the role of BFP, EspA filaments and intimin in EPEC adhesion to intestinal brush border cells was assessed by observing adhesion of wild-type EPEC strain E2348/69 and a set of isogenic single, double and triple mutants in bfpA, espA and eae (intimin gene) to differentiated human intestinal Caco-2 cells. E2348/69 (bfpA + espA + eae + ) adhered rapidly (<10 min) to the brush border of Caco-2 cells and subsequently produced microcolonies and typical A/E lesions. Non-intimate brush border adhesion of double mutant strain UMD880 (bfpA + espA " eae " ) also occurred rapidly, whereas adhesion of strain UMD886 (bfpA " espA + eae " ) occurred later in the infection (>1 h) and with much lower efficiency; confocal microscopy indicated BFP and EspA-mediated adhesion, respectively. Strain UMD883 (bfpA " espA " eae + ), which is unable to translocate Tir, was non-adherent although this strain was able to form intimate attachment and A/E lesions when co-cultured with strain CVD206 (bfpA + espA + eae " ) which supplied Tir to the membrane. Single mutant strains CVD206 (bfpA) and UMD872 (bfpA + espA " eae + ) showed adherence characteristics of strain UMD880 (bfpA + espA " eae " ), whilst triple mutant strain UMD888 (bfpA " espA " eae " ) was totally non-adherent. These results support an adhesive role for BFP and EspA in initial brush border cell attachment, and in typical EPEC which express both BFP and EspA filaments suggest a predominant role for BFP; EspA filaments, however, could serve as initial attachment factors in atypical EPEC which lacks BFP. The study found no evidence for an independent host cell intimin receptor or for other adhesive factors able to support bacterial adherence.Abbreviations: A/E, attaching and effacing; BFP, bundle-forming pilus/pili; EPEC, enteropathogenic Escherichia coli ; LEE, locus of enterocyte effacement; RBC, red blood cell; SEM, scanning electron microscopy; TTSS, type III secretion system; WGA, wheat germ agglutinin.

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“…The most commonly reported function of T4 pili is adherence to a diverse range of surfaces, from metal, glass, plastics, and rocks to plants and various host tissues (48,51,123,156,164,209,217,313,341,391,393,419,431). T4P have repeatedly been shown to contribute to the infectivity of pathogens-even intracellular pathogens such as Francisella tularensis (344)-firmly establishing them as important virulence factors.…”

Section: Adherence and Aggregationmentioning

confidence: 99%

Type IV Pilin Proteins: Versatile Molecular Modules

Giltner

Nguyen

Burrows

2012

Microbiol Mol Biol Rev

410

519

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SUMMARYType IV pili (T4P) are multifunctional protein fibers produced on the surfaces of a wide variety of bacteria and archaea. The major subunit of T4P is the type IV pilin, and structurally related proteins are found as components of the type II secretion (T2S) system, where they are called pseudopilins; of DNA uptake/competence systems in both Gram-negative and Gram-positive species; and of flagella, pili, and sugar-binding systems in the archaea. This broad distribution of a single protein family implies both a common evolutionary origin and a highly adaptable functional plan. The type IV pilin is a remarkably versatile architectural module that has been adopted widely for a variety of functions, including motility, attachment to chemically diverse surfaces, electrical conductance, acquisition of DNA, and secretion of a broad range of structurally distinct protein substrates. In this review, we consider recent advances in this research area, from structural revelations to insights into diversity, posttranslational modifications, regulation, and function.

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Role of bundle-forming pilus of enteropathogenicEscherichia coliin host cell adherence and in microcolony development

Cited by 62 publications

References 26 publications

Comparative Analysis of EspF from Enteropathogenic and Enterohemorrhagic Escherichia coli in Alteration of Epithelial Barrier Function

Comparative Analysis of EspF from Enteropathogenic and Enterohemorrhagic Escherichia coli in Alteration of Epithelial Barrier Function

Enteropathogenic Escherichia coli (EPEC) adhesion to intestinal epithelial cells: role of bundle-forming pili (BFP), EspA filaments and intimin

Type IV Pilin Proteins: Versatile Molecular Modules

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