Indications that the erythrocyte receptor involved in enterotoxigenic Escherichia coli attachment is a sialoglycoconjugate

Bartus, H F; Actor, Paul; Snipes, E; Sedlock, David M.; Zajac, Ian

doi:10.1128/jcm.21.6.951-954.1985

Cited by 19 publications

(10 citation statements)

References 19 publications

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“…We used only the ETEC ATCC 31705 for further studies, because it is the most characterized of the three strains. ATCC 31705 is also referred to as H 10407 and is well known to have CFA-I adhesin, which has been reported to bind to sialic acid-containing glycoconjugates (Bartus et al 1985;Pieroni et al 1988;Wennera Ês et al 1990). Enterotoxigenic E. coli is a major cause of infant diarrhoea in developing countries and is a principal agent of diarrhoea among travellers from developed to developing countries.…”

Section: Discussionmentioning

confidence: 99%

Inhibition of the adherence of Escherichia coli strains to basement membrane by Lactobacillus crispatus expressing an S-layer

et al. 2002

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Aims: This study aimed to evaluate the efficiency with which Lactobacillus crispatus JCM 5810 inhibited the adhesion of enteric pathogens to a synthetic basement membrane and to elucidate the mechanism underlying the inhibition. Methods and Results: Lactobacillus crispatus JCM 5810 inhibited the adhesion of three diarrhoeagenic Escherichia coli strains to a reconstituted basement membrane preparation called Matrigel, used as a model of a damaged intestinal tissue site. Inhibition was also observed with the use of immobilized laminin, a major component of Matrigel, but diminished after the removal of S‐layer protein (CbsA) from JCM 5810 cells. The isolated CbsA inhibited the adhesion of E. coli to both Matrigel and immobilized laminin. Lactobacillus crispatus JCM 5810 and CbsA seem to inhibit pathogenic E. coli from adhering to basement membrane via competition with laminin molecules for binding sites. Conclusions: These results suggested that not only Lact. crispatus JCM 5810 cells but CbsA alone might prevent pathogens from colonizing damaged intestinal tissues. Significance and Impact of the Study: This is the first study to show the applied aspect of Lactobacillus S‐layer protein.

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Section: Discussionmentioning

confidence: 99%

Inhibition of the adherence of Escherichia coli strains to basement membrane by Lactobacillus crispatus expressing an S-layer

et al. 2002

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“…The role of the spatial structure and the integrity of the pili in the recognition of hemagglutination receptors has been demonstrated (1,16,17). The maintenance of integrity of bacterial adhesins was studied here, on whole bacteria, by using dissociating chemicals.…”

Section: Fems Symposium On Molecular Biology Of Microbialmentioning

confidence: 99%

Pilus-mediated binding of bovine enterotoxigenic Escherichia coli to calf small intestinal mucins

Mouricout¹,

Julien²

1987

Infect Immun

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In this study we show that the adhesion to mucus of the enterotoxigenic Escherichia coli strains responsible for diarrhea in calves involves a bacterium-mucin recognition phenomenon in which the bacterial pii and specific mucus receptors carried by the glycoproteins (2,000 to 400 kilodalton) play a major role. An adhesion maximum was observed at a pH of less than 6 (4.75 to 5.25). The sialic acids and galactose appeared to be at least partly responsible for the attachment of K99 pili, whereas F41 pili preferentially recognized desialylated receptors. The attachment of different strains of E. coli characterized by the presence of the three main pili, K99, F41, and FY, known to be responsible for the binding of enterotoxigenic E. coli to the intestinal epithelium of the calf, was studied using Scatchard and Hill analyses. The attachment mechanism of bacteria carrying K99 pili showed positive cooperativity. FY and F41 pili recognized independent receptor sites, the first on sialylated mucus and the second on sialidase-treated mucus. Moreover, F41 pili were found to bind to native mucus according to a negative cooperativity phenomenon. Finally, the recognition sites carried by bacterial pilins may be saturated by some animal glycoprotein glycans which are therefore adhesion inhibitors.

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“…Demonstration that CFA/I also induces mannose‐resistant haemagglutination (MRHA) of human, bovine and chicken erythrocytes led to the adoption of this assay as a proxy model for the study of CFA/I adhesion (Evans et al ., 1979). Evidence suggests that a sialylated glycoprotein serves as the eukaryotic receptor, although a specific enterocyte or red cell receptor remains to be identified (Evans et al ., 1979; Bartus et al ., 1985). The minor, tip‐associated subunit CfaE has been clearly ascribed a direct role in both erythrocyte and human enterocyte adherence and, thus, is viewed as the key fimbrial adhesive subunit (Li et al ., 2007; Poole et al ., 2007; Baker et al ., 2009).…”

Section: Introductionmentioning

confidence: 99%

Shear‐enhanced binding of intestinal colonization factor antigen I of enterotoxigenic Escherichia coli

Tchesnokova¹,

McVeigh

Kidd

et al. 2010

Molecular Microbiology

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SummaryIn the intestine, enterotoxigenic Escherichia coli works against peristaltic forces, adhering to the epithelium via the colonization factor antigen I (CFA/I) fimbrial adhesin CfaE. The CfaE adhesin is similar in localization and tertiary (but not primary) structure to FimH, the type 1 fimbrial adhesin of uropathogenic E. coli, which shows shear-dependent binding to epithelial receptors by an allosteric catch-bond mechanism. Thus, we speculated that CfaE is also capable of shear-enhanced binding. Indeed, bovine erythrocytes coursing over immobilized CFA/I fimbriae in flow chambers exhibited low accumulation levels and fast rolling at low shear, but an 80-fold increase in accumulation and threefold decrease in rolling velocity at elevated shear. This effect was reversible and abolished by pre-incubation of fimbriae with anti-CfaE antibody. Erythrocytes bound to whole CfaE in the same shear-enhanced manner, but to CfaE adhesin domain in a shear-inhibitable fashion. Residue replacements designed to disrupt CfaE interdomain interaction decreased the shear dependency of adhesion and increased binding under static conditions to human intestinal epithelial cells. These findings indicate that close interaction between adhesive and anchoring pilin domains of CfaE keeps the former in a low-affinity state that toggles into a high-affinity state upon separation of two domains, all consistent with an allosteric catch-bond mechanism of CfaE binding.

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Indications that the erythrocyte receptor involved in enterotoxigenic Escherichia coli attachment is a sialoglycoconjugate

Cited by 19 publications

References 19 publications

Inhibition of the adherence of Escherichia coli strains to basement membrane by Lactobacillus crispatus expressing an S-layer

Inhibition of the adherence of Escherichia coli strains to basement membrane by Lactobacillus crispatus expressing an S-layer

Pilus-mediated binding of bovine enterotoxigenic Escherichia coli to calf small intestinal mucins

Shear‐enhanced binding of intestinal colonization factor antigen I of enterotoxigenic Escherichia coli

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