Lectin-binding Capacity of Glycoconjugates in Escherichia coli 09:K103:NM, 987P+ST+-Infected Porcine Lower Small Intestines (original) (raw)
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Phenotypic Characterization of E. coli Isolated from Farm Animals with Diarrhea: Use of Lectin as a Non-Specific Immunostimulant, 2012
Serogroups O26, O55:K59, O86, O91, O111, O118 and O145 of E. coli were prevalent among the diarrheic calves' and lambs' newborns which are of zoonotic impact posing a serious public health risk to humans. No single virulence factor was identified to be common to all isolates; nevertheless their virulence may be allied many and varied combinations of identified biological properties which work in concert with one another to produce a desired effect on the host cell. Lectin could overcome medication interference dilemma, since it improves host immunity which is the best way to overcome the worldwide threat of E. coli diarrhea in newborns as it significantly enhanced the phagocytic activity, phagocytic index and humeral immune response resulting in reduction of the death rate and the intense of infection evidenced by histopathological examination.
Journal of Veterinary Medical Science, 2003
Composition of glycoconjugates was examined in small intestines naturally infected with Isospora suis in preweaned pigs by use of 21 biotinylated-labeled lectins with avidin-biotin-peroxidase complex method. As compared with control pig, staining of 18 lectins altered in jejunal villus brush border and goblet cells of pigs naturally infected with I. suis. These results indicate that I. suis infection alters carbohydrate residues on the jejunal intestines.
Acta Histochemica, 1993
Seven recently isolated lectins were tested for their ability to bind to tissue sections of rat gut. Binding sites for N-Acetylgalactosamine specific lectins were found in mucins, in the brush border membrane and in goblet cells. Non-reducing terminal mannose residues were absent from cell surface membranes but were detected in the supranuclear region of goblet cells and enterocytes. The results of lectin binding obtained in this study were generally similar to lectin-gut interactions observed in vivo.
Food Chemistry, 2013
Enterotoxigenic (ETEC) Escherichia coli (E. coli) causes traveller's diarrhoea and high mortality among baby animals. ETEC adhesion is mediated by lectins (adhesins) that bind to glycoconjugates on the surface of host cells. Glycans that compete for adhesion could be used for disease prevention. Neoglycans of porcine albumin (PSA) that were conjugated with prebiotic galactooligosaccharides (GOS) were synthesised using the Maillard reaction. PSA glycation was confirmed by a reduction in the number of available free amino groups, decreased tryptophan intrinsic fluorescence, increased molecular mass and Ricinus communis lectin recognition. The adhesion of four ETEC strains (E. coli H10407, CFA + , K99 and K88) to PSA-GOS was examined by an enzyme-linked lectin assay. E. coli K88 bound to PSA-GOS with greater affinity (P < 0.05) than did E. coli H10407, CFA + and K99. In addition, PSA-GOS partially inhibited the adherence of the K88 strain to intestinal mucins. Pig ETEC strain was unable to ferment galactooligosaccharide-neoglycans. These results suggest that neoglycans obtained by the Maillard reaction may serve in the prophylaxis of ETEC K88 diarrhoea.
Characterization of glycoprotein glycan receptors forEscherichia coli F17 fimbrial lectin
Microbial Pathogenesis, 1995
The specificity of N-acetylglucosamine-binding F17 fimbrial lectin of coil (also called FY or Att25) for the oligosacharide structures was investigated by mannose-resistant hemagglutination inhibition tests and direct binding assays. The linkage position of N-acetylglucosamine influenced its affinity in the preferential order of/~1-3 >/~1-6 >/~1-4/~ >/Yl-2. Minimal GIcNAc/~l-3Gal/~l-sequence strongly bound to F17 lectin, whether located in terminal nonreducing position or internally in carbohydrate moieties. F17 lectin specifically interacted with this unit in O-glycosidically linked oligosaccharides of the bovine glycophorins and intestinal mucins. On the contrary, GIcNAc/~I-NAsn, GIcNAc/~l-6Man~-and GIcNAcpl-4GIcNAc-of N-glycosylated proteins failed to bind to the lectin. Our findings emphasized the presence of multiple F17 mucosal receptor complex in the newborn calf intestines. Furthermore, the density of receptors for F17 fimbrial lectin seemed to depend on the age of the calf and the intestinal segment.
Histochemistry, 1987
The labelling pattern of eight lectins was studied in jejunal samples from ten normal subjects, in order to define the normal distribution of structural and secretory glycoconjugates in the small bowel. The following lectins were studied by means of a peroxidase technique on formalin-fixed samples: Arachis hypogaea, Ricinus communis, Canavalia ensif ormis, Lens culinaris, Phaseolus vulgaris, Triticum vulgaris, Ulex europaeus, Dolichos biflorus. Phaseolus vulgaris reacted with goblet cell mucus throughout the villus-crypt axis. Conversely Ulex europaeus, Dolichos biJlorus and Triticum vulgaris lectin labelling of globet cells appeared to be confined to the upper part of the villi. This finding suggests that during cell migration from crypt to villus tip, the continuing maturation of goblet cells is associated with the differentiation of secretory carbohydrates, which probably parallels the cell maturation cycle. Lectin histochemistry appears to be a reliable tool for the study of structural and secretory glycoconjugates in the jejunal mucosa, and might be of value in the study of diseases in which the cell-maturation cycle in the small bowel is altered.
Molecular and cellular biochemistry, 1999
The capacity of cholera toxin (CT) and type I heat-labile enterotoxin produced by Escherichia coli isolated from human intestine (LTh) to interact with glycoconjugates bearing ABH blood group determinants from rabbit intestinal brush border membranes (BBM) was studied. On the basis of the type of intestinal compounds related to the human ABH blood group antigens, rabbits were classified as AB or H. Toxin binding to the intestinal glycolipids and glycoproteins depends on the blood group determinant borne by the glycoconjugate and on the analyzed toxin. LTh was capable of interacting preferentially with several blood group A- and B-active BBM glycolipids compared to those isolated from animals lacking these antigens (H rabbits). Also, LTh preferably bound to several BBM glycoproteins from AB rabbit intestines compared to those from H ones. One of these glycoproteins, the sucrase-isomaltase complex (EC 3.2.1.48-10) isolated from AB and H rabbits showed the same differential LTh binding...
Lectins and also bacteria modify the glycosylation of gut surface receptors in the rat
Glycoconjugate J. 12, 22-35, 1995
Oral exposure to lectins or the presence or absence of bacteria in the rat small intestine were shown by histological methods using anti-lectin antibodies or digoxigenin-labelled lectins to have major effects on the state of glycosylation of lumenal membranes and cytoplasmic glycoconjugates of epithelial cells. Taken together with the dramatic effects of exposure to lectins on gut function, metabolism and bacterial ecology, this can be used as a basis for new perspectives of biomedical manipulations to improve health.
FEBS Letters, 1990
Glycolipids from mucosa scrapings of small intestine of neonatal and adult pigs were tested by the thin‐layer chromatogram overlay assay for the binding of Escherichia coli K99. There was practically no binding to acid or non‐acid glycolipids of adult pig, known to be resistant to infection with this bacterium. However, piglets, which are susceptible to infection, showed a clear binding to a doublet band in the acid glycolipid fraction. The receptor‐active glycolipid was isolated and shown by mass spectrometry, NMR spectroscopy and degradation methods to be NeuGcα‐3Galß4GlcßCer (NeuGc‐GM3), the two bands being due to heterogeneity of the ceramide. When tested against various reference glycolipids, NeuAc‐GM3 was shown to be inactive. This ganglioside was dominating in adult pig. The apparent developmental disappearance of N‐glycolyl groups in glycolipids of intestinal mucosa may have a correspondence in protein‐linked sequences as well and thus explain the resistance of adult pigs to...
Acta Biochimica Polonica
Adhesion of enterotoxigenic (ETEC) E. coli to host intestinal cells is mediated by lectin-like fimbriae that bind to specific glycan moieties on the surfaces of enterocytes. To prevent in vitro binding of E. coli F4 fimbriae (F4 ETEC +) to piglet enterocytes, neoglycans were synthesized by the Maillard reaction conjugating lactose (Lac), galacto-oligosaccharides (GOS) or chitin oligosaccharides (Ochit) to porcine serum albumin (PSA). Neoglycans were characterized by SDS-PAGE, intrinsic tryptophan fluorescence and recognition by plant lectins, as well as by F4 ETEC variants. Electrophoretic patterns suggested the binding to PSA of 63, 13 and 2 molecules of Lac, GOS and Ochit, respectively. All neoglycans displayed quenching of tryptophan fluorescence consistent with the degree of glycation estimated by SDS-PAGE. Plant lectins recognized the neoglycans according to their specificity, whereas antigenic variants of F4 ETEC (ab, ac and ad) recognized PSA-Ochit and PSA-Lac with higher affinity than that for GOS. Neoglycans partially hindered the in vitro binding of F4 + ETEC to piglet enterocytes in a dose-dependent manner. The most effective blocking was observed with PSA-Lac that partially inhibited the adhesion of bacteria to enterocytes in a dose dependent manner, as quantified by flow cytometry. Increased production of the cytokines IL-6 and TNF-α was observed in response to F4 + ETEC infection of enterocytes and production was reduced in the presence of PSA-Ochit and PSA-GOS. These results suggest that neoglycans synthesized by the Maillard reaction could be useful in the prophylaxis of diarrhea in piglets.