Characteristics of binding of Escherichia coli serotype O157:H7 strain CL-49 to purified intestinal mucin

Sajjan, S. Umadevi; Forstner, Janet F.

doi:10.1128/iai.58.4.860-867.1990

Cited by 54 publications

(25 citation statements)

References 55 publications

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“…A large variety of bacteria have been reported to interact with mucin carbohydrate, including Streptococcus sanguis and Streptococcus mutans (2, 7), P. aeruginosa (33,35) and P. cepacia (36), species of Staphylococcus (39), strains of E. coli (3,37,48), and Helicobacter pylori (47). We therefore examined whether sugars could interfere with the binding of virulent Y enterocolitica to rabbit intestinal mucin in hapten inhibition studies (Table 2).…”

Section: Resultsmentioning

confidence: 99%

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Adhesion of Yersinia enterocolitica to purified rabbit and human intestinal mucin

Mantle

Husar

1993

Infect Immun

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Interactions between Yersinia enterocolitica and purified intestinal mucins from rabbit and humans were investigated. Plasmid-bearing virulent organisms (but not plasmid-free nonvirulent bacteria) bound well to both mucins, suggesting that adherence was controlled by the virulence plasmid. Examination of binding to 14 different preparations of purified human intestinal mucin (8 preparations obtained from normal subjects and 6 samples from patients with cystic fibrosis) revealed no differences between normal and cystic fibrotic mucins in ability to serve as a binding substrate for virulent Y. enterocolitica. Analyses of binding curves suggested the presence of a single type of noninteracting receptor for Y. enterocolitica in both rabbit and human mucins with similar (but not necessarily identical) structures. Virulent bacteria bound to polystyrene through hydrophobic interactions that could be disrupted by treating the organisms with tetramethyl urea. In contrast, binding of plasmid-bearing Y. enterocolitica to intestinal mucin was not susceptible to tetramethyl urea and therefore does not appear to involve hydrophobic interactions. Prior incubation of organisms with mucin significantly inhibited binding to polystyrene, suggesting that mucin can mask hydrophobic adhesins on the bacterial surface. Hapten inhibition studies revealed that the monosaccharides galactose and N-acetylgalactosamine and the disaccharide lactose could markedly reduce (but not abolish) bacterial adherence to mucin but other monosaccharides and the RGD peptide had no effect on mucin binding. We conclude that virulent Y. enterocolitica is capable of interacting with the carbohydrate moiety of intestinal mucin. These interactions appear to be plasmid mediated and not hydrophobic.Yersinia enterocolitica is an enteroinvasive bacterium that causes gastroenteritis (4, 40). The mechanisms enabling the organism to colonize the gut and produce disease have not yet been clearly defined, but all pathogenic strains (in contrast to nonpathogenic environmental isolates) contain a 42to 50-MDa plasmid (6, 31), indicating that the plasmid is essential for virulence. A variety of proteins (16 to 20) are encoded by the plasmid, and their expression is regulated by both temperature and the availability of calcium (6,31,32,43). Some of these proteins are secreted, and a number then associate with the outer membrane of the organism and are referred to as Yops (for yersinia outer membrane proteins) (22,24,25,31,32). In addition, the plasmid encodes for YadA, a fibrillar adhesin that is a true outer membrane protein (12). When expressed, these plasmid-encoded proteins change the surface charge and hydrophobicity of the bacterium, promote autoagglutination and mannose-resistant hemagglutination, enhance adherence to cell lines, collagen, and fibronectin, and confer on the organism the ability to resist phagocytosis by polymorphonuclear leukocytes and the bacteriocidal effects of serum (1, 9, 12-15, 22, 23, 29, 41, 46). Thus, plasmid proteins may participate in attac...

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Section: Resultsmentioning

confidence: 99%

“…Hydrophobic interactions have been shown to play a role in the binding of several bacteria to mucin (5,37,38).…”

Section: Discussionmentioning

confidence: 99%

Adhesion of Yersinia enterocolitica to purified rabbit and human intestinal mucin

Mantle

Husar

1993

Infect Immun

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“…Although the mechanisms of adhesion of various pathogenic bacteria by fimbriae (pilus) or flagella have been extensively investigated (Girardeau et al . 1988;Lindahl & Carlstedt 1990;Sajjan & Forstner 1990;Simpson et al . 1992;Purushothaman et al .…”

Section: Introductionmentioning

confidence: 99%

Selection of useful probiotic lactic acid bacteria from the Lactobacillus acidophilus group and their applications to functional foods

Saito

2004

Animal Science Journal

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In the present review, a new mass screening system for selecting probiotic strains from Lactobacillus ( L) acidophilus group lactic acid bacteria (LAB) with strong adhesion to the human intestinal tract is described. Characteristics of antimicrobial peptides (bacteriocin), lactose-hydrolyzing enzymes and immunostimulative oligo DNA motifs in L. gasseri strains are also described. Finally, the use of L. acidophilus LAB, selected by our screening method, that have strong adhesion to the human colonic mucosa in functional yogurt products is described. Adhesiveness to the human intestine is one of the most important characteristics of probiotic LAB. A new screening system that involves a combination of three methods is proposed: rat colonic mucin (RCM)-micro plate assay, Carnoy's histochemical staining method and carbohydrate probe binding assay. By using an RCM-coated poly-vinylidene-diflouride membrane that mimics the human colonic mucous layer, a new lectin was isolated and its structure was clarified by gene cloning. Furthermore, the structures and functions of a new cyclic bacteriocin (gassericin A), new lactose-hydrolyzing enzymes, and new immunostimulating oligo DNA motifs from Lactobacillus gasseri (B 1 subgroup) were clarified. A new functional yogurt 'Fit down' is proposed, that is fermented by an adhesive strain of L. acidophilus LA67 selected by our screening and contains antihypertensive peptides derived from whey proteins by protease digestion. In the future, superior functional foods containing more effective probiotic LAB are expected to be developed by the use of the proposed mass screening system.

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“…On the other hand, bacteria (including E. coli ) were reported to attach to the mucin layer through fimbrial [type 1 pili (fimbriae)] and afimbrial (multivalent adhesion molecule) adhesins as well as induce mucin hypersecretion in the rabbits' ileal loop and cultured human mucin‐secreting intestinal HT29‐MTX cells . E. coli was also reported to attach to the intestinal mucus via its flagellum .…”

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confidence: 99%

Mucin adsorbed by E. coli can affect neutrophil activation in vitro

et al. 2019

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Bacteria colonizing human intestine adhere to the gut mucosa and avoid the innate immune system. We previously demonstrated that Escherichia coli isolates can adsorb mucin from a diluted solution in vitro. Here, we evaluated the effect of mucin adsorption by E. coli cells on neutrophil activation in vitro. Activation was evaluated based on the detection of reactive oxygen species production by a chemiluminescent reaction (ChL), observation of morphological alterations in neutrophils and detection of exocytosis of myeloperoxidase and lactoferrin. We report that mucin adsorbed by cells of SharL1 isolate from Crohn's disease patient's inflamed ileum suppressed the potential for the activation of neutrophils in whole blood. Also, the binding of plasma complement proteins and immunoglobulins to the bacteria was reduced. Desialylated mucin, despite having the same adsorption efficiency to bacteria, had no effect on the blood ChL response. The effect of mucin suggests that it shields epitopes that interact with neutrophils and plasma proteins on the bacterial outer membrane. Potential candidates for these epitopes were identified among the proteins within the bacterial outer membrane fraction by 2D‐PAGE, fluorescent mucin binding on a blot and HPLC‐MS/MS. In vitro, the following proteins demonstrated mucin adsorption: outer membrane porins (OmpA, OmpC, OmpD and OmpF), adhesin OmpX, the membrane assembly factor OmpW, cobalamine transporter, ferrum uptake protein and the elongation factor Ef Tu‐1. In addition to their other functions, these proteins are known to be bacterial surface antigens. Therefore, the shielding of epitopes by mucin may affect the dynamics and intensity of an immune response.

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Characteristics of binding of Escherichia coli serotype O157:H7 strain CL-49 to purified intestinal mucin

Cited by 54 publications

References 55 publications

Adhesion of Yersinia enterocolitica to purified rabbit and human intestinal mucin

Adhesion of Yersinia enterocolitica to purified rabbit and human intestinal mucin

Selection of useful probiotic lactic acid bacteria from the Lactobacillus acidophilus group and their applications to functional foods

Mucin adsorbed by E. coli can affect neutrophil activation in vitro

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