Haemagglutination patterns of the different variants of Escherichia coli K88 antigen with porcine, bovine, guinea pig, chicken, ovine and equine erythrocytes

Bijlsma, I. G. W.; Frik, J. F.

doi:10.1016/s0034-5288(18)30755-0

Cited by 14 publications

(10 citation statements)

References 11 publications

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“…Within the lactosyl group, all three K88 variants bound to Lc 3 , K88ac bound to Lc 4 , and K88ad bound to Lc 2 . Within the neolactosyl group, all three K88 variants bound to nLc 4 and nLc 6 . Within the globosyl family, all three variants bound to Gb 3 .…”

Section: Resultsmentioning

confidence: 99%

“…Each K88 variant has a different, but related, carbohydrate-binding specificity. The differences in carbohydrate specificity among the three K88 adhesin variants are reflected in the different hemagglutination patterns of the K88 variants, determined by using erythrocytes from various species (6), and in the presence of multiple phenotypes of pigs whose intestinal epithelial cells contain receptors that bind different combinations of K88 adhesin variants (3,5,44).…”

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confidence: 99%

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Evaluation of Receptor Binding Specificity ofEscherichia coliK88 (F4) Fimbrial Adhesin Variants Using Porcine Serum Transferrin and Glycosphingolipids as Model Receptors

Grange

Mouricout²,

Levery

et al. 2002

Infect Immun

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Diarrheal disease caused by enterotoxigenic Escherichia coli expressing the K88 (F4) fimbrial adhesin (K88 ETEC) is a significant source of mortality and morbidity among newborn and weaned piglets. K88 fimbrial adhesins are filamentous surface appendages whose lectin (carbohydrate-binding) activity allows K88 ETEC to attach to specific glycoconjugates (receptors) on porcine intestinal epithelial cells. There are three variants of K88 adhesin (K88ab, K88ac, and K88ad), which possess different, yet related, carbohydrate-binding specificities. We used porcine serum transferrin (pSTf) and purified glycosphingolipids (GSL) to begin to define the minimal recognition sequence for K88 adhesin variants. We found that K88ab adhesin binds with high affinity to pSTf (dissociation constant, 75 M), while neither K88ac nor K88ad adhesin recognizes pSTf. Degradation of the N-glycan on pSTf by extensive metaperiodate treatment abolished its interaction with the K88ab adhesin, indicating that the K88ab adhesin binds to the single N-glycan found on pSTf. Using exoglycosidase digestion of the pSTf glycan, we demonstrated that K88ab adhesin recognizes N-acetylglucosamine (GlcNAc) residues in the core of the N-glycan on pSTf. All three K88 variants were found to bind preferentially to GSL containing a ␤-linked N-acetylhexosamine (HexNAc), either GlcNAc or N-acetylgalactosamine, in the terminal position or, alternatively, in the penultimate position with galactose in the terminal position. Considering the results from pSTf and GSL binding studies together, we propose that the minimal recognition sequence for the K88 adhesin variants contains a ␤-linked HexNAc. In addition, the presence of a terminal galactose ␤-linked to this HexNAc residue enhances K88 adhesin binding.Diarrheal disease caused by enterotoxigenic Escherichia coli expressing the K88 (F4) fimbrial adhesin (K88 ETEC) is a significant source of mortality and morbidity among newborn and weaned piglets (9,25,38,41,59). K88 fimbrial adhesins are filamentous surface appendages whose lectin (carbohydratebinding) activity allows K88 ETEC to attach to specific glycoconjugates (receptors) on porcine intestinal epithelial cells (28). Attachment of bacteria to their receptors on intestinal epithelial cells is an essential step in the colonization of the small intestine by ETEC.Three serologically distinguishable variants of K88 adhesin (K88ab, K88ac, and K88ad) have been identified (21, 40). Each variant consists of a conserved antigenic region shared by all three variants, designated a, and variant-specific antigenic regions, designated b, c, and d for K88ab, K88ac, and K88ad, respectively (13, 29). The antigenic differences among the three K88 variants can be ascribed exclusively to a small number of nucleotide changes in the major fimbrial subunit gene, resulting in the amino acid substitutions that distinguish the three K88 variants. Several researchers have investigated the molecular interaction of K88 fimbrial adhesin variants with erythrocytes, intestinal mucus, and intestina...

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Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

Evaluation of Receptor Binding Specificity ofEscherichia coliK88 (F4) Fimbrial Adhesin Variants Using Porcine Serum Transferrin and Glycosphingolipids as Model Receptors

Grange

Mouricout²,

Levery

et al. 2002

Infect Immun

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“…K88 fimbriae are composed of a single adhesin major protein subunit and minor subunits that are suspected to regulate fimbrial expression (1,31). K88 fimbriae bind to cell surface receptors that contain carbohydrate structures, with ␤-D-galactose being an essential component (2,6,23). Galactose-containing glycoprotein in pig gastric mucin, glucosamine, and chondrosine inhibited hemagglutination in ETEC K88 strains (17,20).…”

mentioning

confidence: 99%

Exopolysaccharide Synthesized by Lactobacillus reuteri Decreases the Ability of Enterotoxigenic Escherichia coli To Bind to Porcine Erythrocytes

Wang

Gänzle

Schwab

2010

Appl Environ Microbiol

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This study investigated the therapeutic potential of bacterial polysaccharides by employing a model system based on enteroxigenic Escherichia coli (ETEC)-induced hemagglutination of erythrocytes. Exopolysaccharides produced by strains of Lactobacillus reuteri inhibited ETEC-induced hemagglutination of porcine erythrocytes. No effect was observed for dextran produced from Weissella cibaria and commercially available oligo-and polysaccharides.Lactic acid bacteria (LAB) are important in food production due to their positive contribution to flavor and preservation of the final product. Some of these food-grade microorganisms are also valuable for their ability to synthesize exopolysaccharides (EPSs). EPSs are high-molecular-weight sugar polymers, which remain attached to the microorganism as capsular EPS or become excreted into the environment in the form of slime or ropy EPS (26,30). LAB utilize two distinct biosynthetic pathways to produce EPSs. Heteropolysaccharides (HePSs) comprised of two to eight repeating units of monosaccharides are assembled by cell wall-bound glycosyltransferases in low quantities from intracellular sugar nucleotide precursors (4). Extracellular glycansucrases (glucan-or fructansucrases) synthesize homopolysaccharides (HoPSs) consisting of either glucose or fructose from sucrose, and their yield can be as high as 40 g liter Ϫ1 (13, 19). EPS formation by glycansucrases has been reported for lactobacilli of the species Lactobacillus reuteri, L. pontis, L. panis, L. acidophilus, and L. frumenti (28, 29). HoPS synthesis and the corresponding genes have been especially well characterized in L. reuteri (27). All EPSs used in this study were HoPSs formed in the presence of sucrose. In addition to HoPS synthesis, glycansucrases are capable of producing oligosaccharides (OSs). Several OSs are found to have prebiotic properties as they can benefit host health by acting as nondigestible food ingredients and by enhancing the growth of desired microbial members of the gastrointestinal microbiota (7). Emerging research efforts have investigated potential applications of OSs as antiadhesive agents in preventing pathogen colonization. Shoaf et al. (24) suggested that commercial oligoand polysaccharides reduce the adherence of enteropathogenic Escherichia coli (EPEC) to cell lines. reported antiadhesive properties of human milk oligosaccharides against human strains of enterotoxigenic Escherichia coli (ETEC) and uropathogenic E. coli. Similarly, Martín et al. (15) confirmed the binding of milk oligosaccharides to ETEC isolated from calves. In contrast, adhesion studies with EPS are limited.The inhibition of ETEC is of special interest to the swine industry because ETEC is the primary cause for diarrhea in neo-and postnatal piglets and results in substantial economic losses. We therefore aimed to test for antiadhesive properties of EPSs synthesized by LAB and commercially available prebiotics against porcine ETEC strains. Hemagglutination assays were used; these assays are generally accepted as an effe...

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“…However, K88ac is by far the most common variant associated with diarrheal disease in pigs (18,39). Each antigenic variant of K88 exhibits uniqueness in its hemagglutinating properties with respect to erythrocytes from various species (2,4). In addition, each variant exhibits uniqueness in the specificity of its binding to porcine enterocytes (1,3,4,36).…”

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confidence: 99%

“…Each antigenic variant of K88 exhibits uniqueness in its hemagglutinating properties with respect to erythrocytes from various species (2,4). In addition, each variant exhibits uniqueness in the specificity of its binding to porcine enterocytes (1,3,4,36). Bijlsma et al (3) identified five phenotypes of pigs with regard to the adhesion of K88 ϩ E. coli to enterocyte brush borders.…”

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confidence: 99%

Inhibition of Adhesion ofEscherichia coliK88ac Fimbria to Its Receptor, Intestinal Mucin-Type Glycoproteins, by a Monoclonal Antibody Directed against a Variable Domain of the Fimbria

et al. 2000

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Strains of enterotoxigenic Escherichia coli that express K88 fimbriae are among the most common causes of diarrhea in young pigs. Adhesion of bacteria to receptors on intestinal epithelial cells, mediated by K88 fimbriae, is the initial step in the establishment of infection. Three antigenic variants of K88 fimbriae exist in nature: K88ab, K88ac, and K88ad. K88ac is the most prevalent and may be the only variant of significance in swine disease. Each K88 fimbrial variant is composed of multiple antigenic determinants. Some of these determinants are shared among the three variants and may be referred to as conserved epitopes, whereas others are unique to a specific variant and may be referred to as variable epitopes. In this study, monoclonal antibodies (MAbs) specific to either variable or conserved epitopes of K88ac fimbriae were produced. The specificity of each MAb was tested by enzyme-linked immunosorbent and immunoblot assays. Fab fragments were prepared from these MAbs and were tested for their ability to block the binding of K88-positive bacteria and purified fimbriae to porcine enterocyte brush border vesicles and purified K88 receptors, respectively. The purified receptors were intestinal mucin-type sialoglycoproteins (

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Haemagglutination patterns of the different variants of Escherichia coli K88 antigen with porcine, bovine, guinea pig, chicken, ovine and equine erythrocytes

Cited by 14 publications

References 11 publications

Evaluation of Receptor Binding Specificity ofEscherichia coliK88 (F4) Fimbrial Adhesin Variants Using Porcine Serum Transferrin and Glycosphingolipids as Model Receptors

Evaluation of Receptor Binding Specificity ofEscherichia coliK88 (F4) Fimbrial Adhesin Variants Using Porcine Serum Transferrin and Glycosphingolipids as Model Receptors

Exopolysaccharide Synthesized by Lactobacillus reuteri Decreases the Ability of Enterotoxigenic Escherichia coli To Bind to Porcine Erythrocytes

Inhibition of Adhesion ofEscherichia coliK88ac Fimbria to Its Receptor, Intestinal Mucin-Type Glycoproteins, by a Monoclonal Antibody Directed against a Variable Domain of the Fimbria

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