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Query: UMLS:C0001511 (Adhesion)
 5,955 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Adhesion of vibrios to the small intestine may occur (i) by association of the bacteria with secreted mucus gel or (ii) by adherence of the bacteria to the surface of epithelial cells. In the present study, vibrios readily adhered to isolated brush border membranes obtained from rabbit intestinal epithelial cells. Adhesion was temperature dependent and required the presence of divalent cations such as calcium. The agglutination of human O erythrocytes by Vibrio cholerae was observed also, and the hemagglutination test appeared to detect the same mechanism that was involved in the adhesion of vibrios to brush borders. When the bacteria were grown in broth they were adhesive and hemagglutinating, but vibrios grown on agar plates or suspended in buffer for 15 min at 37 C lacked these abilities, even though they retained undiminished motility. These two model systems differed, however, in that strontium promoted only adhesion to brush borders. The significance of this difference remains to be determined. Vibrios were observed to penetrate intestinal mucus gel and occasionally to become entrapped in it. However, there was no evidence that vibrios attached to mucus gel.
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PMID:Adhesive properties of Vibrio cholerae: adhesion to isolated rabbit brush border membranes and hemagglutinating activity. 98 4

Nonmotile vibrio mutants lacked the ability to adhere to rabbit intestinal brush border membranes and to agglutinate human group O erythrocytes, but motile revertant vibrios isolated from such strains expressed adhesiveness equivalent to that of the original parent. Two possible explanations for the relation between vibrio motility and adhesion in these assays systems are (i) that the rate of adhesion depends on the rate of chance contact brought about by motility, and (ii) that the flagellum either acts as a carrier for the bacterial adhesin or may itself be the adhesin. The present study indicates, however, that the lack of adhesion by nonmotile vibrios did not depend on motility as such and did not involve greater rates of elution. Increasing the rate of contact between nonmotile vibrio mutants and brush border membranes by compaction did not restore the adhesive properties of the defective strains. Accordingly, we speculate that the flagellum may function in some indirect way that allows the expression of the adhesive properties, such as by acting as a carrier for a specific vibrio adhesin. Adhesion to brush borders and agglutination of human group O erythrocytes was specifically inhibited by L-fucose and various glycosides of L-fucose and to a lesser extent by D-mannose. Vibrios adhered specifically to agarose beads that carried covalently linked L-fucose on their surfaces. The results suggest that L-fucose-containing structures of eukaryotic cell surfaces may function as receptors for the vibrio adhesin and may therefore be an important determinant of host susceptibility.
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PMID:Adhesive properties of Vibrio cholerae: nature of the interaction with isolated rabbit brush border membranes and human erythrocytes. 98 5

Twenty-five strains of lactobacilli were tested for their ability to adhere to human enterocyte-like Caco-2 cells in culture. Seven Lactobacillus strains adhered well to the Caco-2 cells, of which three possessed calcium-independent adhesion properties. A high level of calcium-independent adhesion was observed with the human stool isolate Lactobacillus acidophilus strain LB. Scanning electron microscopy revealed that this strain adhered to the apical brush border of the cells. Adhesion increased in parallel with the morphological and functional differentiation of the Caco-2 cells. Two Lactobacillus components were involved in this adhesion. One was protease-resistant and bacterial-surface-associated; the other was heat-stable, extracellular and protease-sensitive.
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PMID:Adhesion of human Lactobacillus acidophilus strain LB to human enterocyte-like Caco-2 cells. 152 9

This thesis is based on 8 publications and a review of the literature. The aim was to summarize present knowledge on molecular components of Yersinia enterocolitica involved in (i) adhesion, with special reference to plasmid encoded factors and (ii) induction of antibodies in the host, and the quantitation of these two phenomena. Adhesion of Y. enterocolitica was quantitatively studied by methods that measured binding to cultured epithelial cells, mucosal constituents immobilized on polystyrene, intestinal tissue, and nonbiological solid surfaces. The chromosomal inv and ail gene products have been shown by others to be independently able to mediate adhesion to and invasion of cultured epithelial cells. However, the Yersinia virulence plasmid, pYV, also encodes for at least one product that may mediate adhesion. It was shown that pYV carrying Y. enterocolitica strains adhered more efficiently than their isogenic pYV cured derivatives to rabbit and human ileal intestinal tissue and to rabbit ileal brush border membrane vesicles (BBVs). Using Y. enterocolitica mutants that were defective for production of the pYV encoded outer membrane protein, YadA, and Escherichia coli strains carrying the cloned yadA gene it was verified that YadA was responsible for the pYV encoded adhesion. The YadA promoted adhesion was found likely to be non-specific and, at least in part, mediated by hydrophobic interaction. YadA, however, also mediated binding to one or more constituents present in intestinal mucus. Such binding led to decreased ability to penetrate a layer of mucus in vitro and subsequent decreased ability to adhere to BBVs. Based upon these results, it remains uncertain whether Y. enterocolitica is able to benefit from the YadA mediated adhesion in the intestinal millieu. In vivo results have suggested that expression of YadA confers on Y. enterocolitica an increased ability to colonize the intestine, but no definitive conclusions have been reached so far. A large number of antigens were identified in Y. enterocolitica by means of crossed immunoelectrophoresis (XIE). Quantitation of serological cross-reactions between chromosome-encoded Y. enterocolitica antigens and antigens from other bacterial species was performed by means of XIE and proved useful for taxonomic purposes. Using XIE it was shown that infection with Y. enterocolitica induced an antibody response against a wide range of antigens. Tube agglutination, enzyme linked immunosorbent assays (ELISAs) using purified lipopolysaccharide (LPS) or formalin-killed whole pYV carrying cells as antigens, and XIE were evaluated for their applicability to detect recent Y. enterocolitica O:3 infection.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Interactions between Yersinia enterocolitica and the host with special reference to virulence plasmid encoded adhesion and humoral immunity. 161 21

Evidence for the existence of two phenotypes of piglets born to experimental herds was obtained based on the susceptibility of intestinal brush borders to adhesion of K99-positive Escherichia coli. The enterocytes of the K99-receptive piglets displayed a characteristic sialoglycolipid pattern, with a higher content of the monosialoglycolipids II3NeuGc-LacCer (GM3Gc), IV3NeuGc-nLcOse4Cer (SPGGc) and IV3NeuAc-nLcOse4Cer (SPG) and the oligosialogangliosides IV3NeuAc,II3NeuAc-GgOse4Cer (GD1a), II3(NeuAc)2-GgOse3Cer (GD2), II3(NeuAc)2-GgOse4Cer (GD1b) and IV3NeuAc,II3(NeuAc)2-GgOse4Cer (GT1b) when compared to the gangliosides of non-receptive piglets. The gangliosides from enterocytes of the non-receptive piglets were mainly the monosialogangliosides II3NeuAc-GgOse3Cer (GM2) and II3NeuAc-LacCer (GM3), only traces of the other sialoglycolipids being detected. Adhesion of 14C-labelled K99-positive E. coli cells to the piglet small intestinal sialoglycolipids, as tested by the thin-layer chromatogram overlay assay, revealed that the receptive enterocyte membrane was richer in glycolipids containing K99 receptor structures than the non-receptive enterocyte. Adhesion of K99-positive E. coli correlated with the degree of sialylation of the brush border glycolipids.
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PMID:Adhesion of K99 fimbriated Escherichia coli to pig intestinal epithelium: correlation of adhesive and non-adhesive phenotypes with the sialoglycolipid content. 168 99

An enterotoxigenic Escherichia coli strain, E. coli 8786, of serotype O117:H4 produced only heat-stable enterotoxin and gave mannose-resistant hemagglutination with human and bovine erythrocytes. The strain adhered to the brush border of human enterocytes and to enterocytelike cell line Caco-2. Adhesion inhibition assays using Caco-2 cells with different adhesive factor extracts showed that the adhesive factor of E. coli 8786 is different from colonization factor antigen I (CFA/I). CFA/II, CFA/III of Darfeuille et al. (A. Darfeuille, B. Lafeuille, B. Joly, and R. Cluzel, Ann. Microbiol. Inst. Pasteur 134A:53-64, 1983), CS6, and antigen 2230. A bacterial surface protein, designated antigen 8786, with a molecular mass of 16,300 Da was responsible for the adhesion to intestinal cells. It was immunologically different from previously described adhesive factors as determined by immunoblotting. Antigen 8786 was detected on the bacterial cell surface and appeared to be nonfimbrial. NH2-terminal analysis of antigen 8786 showed no homology with the previously described adhesive factors. Nevertheless, antigen 8786 is closely related to the NH2-terminal sequence of Salmonella enteritidis fimbrin. A hybridization experiment using a synthetic oligonucleotide probe based on the NH2-terminal amino acid sequence of antigen 8786 revealed that the coding region was located on a 70-MDa plasmid.
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PMID:New adhesive factor (antigen 8786) on a human enterotoxigenic Escherichia coli O117:H4 strain isolated in Africa. 200 11

The inhibitory effect of human milk on plasmid-encoded adhesion of Yersinia enterocolitica to rabbit ileal brush border membrane vesicles immobilized on polystyrene was evaluated. Adhesion was reduced to about 50% after incubation of equal volumes of bacteria and undiluted human milk, but a significant reduction was also detectable after incubation with milk samples at a final 1:10 dilution. Removal of immunoglobulins from human milk by means of immunoadsorption did not change the inhibitory effect on adhesion. Both milk fat, proteins, and factors resistant to proteolytic and heat treatment contributed to the reduction in adhesion.
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PMID:Inhibition of plasmid-encoded adhesion of Yersinia enterocolitica by non-immunoglobulin fraction of human milk. 206 8

Enterotoxigenic Escherichia coli (ETEC) strains possessing colonization factor antigen I (CFA/I), CFA/II, CFA/III, and antigen 2230 were tested for their ability to adhere to the following cell lines: HeLa, HEp-2, HRT 18, Hutu 80, MDBK, MDCK, Vero, and Caco-2. ETEC strains adhered only to the Caco-2 cell line. Irrespective of the known adhesive factors, the ETEC strains that adhered to the brush border of human enterocytes also adhered to the Caco-2 cell line. The negative variants, which were cured of the plasmid encoding the adhesive factor, did not adhere. Adhesion of ETEC strains no longer occurred when the Caco-2 cells were pretreated with the homologous colonization factor antigen or when the bacterial cells were pretreated with homologous antibodies raised against the adhesive factors. This indicates that this adhesion is specific and that a different receptor exists for each type of adhesion factor. Electron micrographs of cross sections of the monolayer showed that the adhesion of ETEC strains to the brush border microvilli does not induce any lesion. Therefore, the Caco-2 cell line behaves in the same way as human enterocytes do.
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PMID:Adhesion of enterotoxigenic Escherichia coli to the human colon carcinoma cell line Caco-2 in culture. 218 Aug 23

Escherichia coli F-18, an excellent colonizer of the streptomycin-treated mouse large intestine, produces type 1 pili. E. coli F-18 FimA-, type 1 pilus negative, and E. coli F-18 FimH-, type 1 pilus positive but adhesin negative, were constructed by bacteriophage P1 transduction of defective fimA and fimH genes from the E. coli K-12 strains ORN151 and ORN133, respectively, into E. coli F-18. Adhesion of E. coli F-18 to an immobilized mannose-bovine serum albumin glycoconjugate was about sixfold greater than that of either E. coli F-18 FimA- or E. coli F-18 FimH-, and adhesion of E. coli F-18 to immobilized cecal epithelial cell brush border membranes was between two- and threefold greater than that of E. coli F-18 FimA- or E. coli F-18 FimH-. When either E. coli F-18 FimA- or E. coli FimH- was fed to streptomycin-treated mice together with E. coli F-18, the pilus-negative and adhesin-negative strains colonized as well as their type 1-piliated parent. Essentially the same result was observed when the type 1-piliated E. coli K-12 strain ORN152 was fed to streptomycin-treated mice together with a nearly isogenic K-12 FimA- strain, ORN151. Furthermore, when streptomycin-treated mice were fed E. coli F-18 FimA- or E. coli F-18 FimH- together with E. coli F-18 Col-, which also makes type 1 pili but is a poor colonizer relative to E. coli F-18 because it grows poorly in mucus in the presence of E. coli F-18, the F-18 FimA- and F-18 FimH- strains colonized well (10(6) to 10(7) CFU/g of feces), whereas the number of E. coli F-18 Col- in feces decreased rapidly to 10(2) CFU/g of feces. These data show that in streptomycin-treated mice, the inability to produce functional type 1 pili has no effect on the ability of E. coli F-18 and E. coli K-12 to colonize the large intestine.
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PMID:Type 1 pili are not necessary for colonization of the streptomycin-treated mouse large intestine by type 1-piliated Escherichia coli F-18 and E. coli K-12. 257 Jul 52

Escherichia coli F-18, a normal fecal isolate, was previously shown to be an excellent colonizer of the streptomycin-treated CD-1 mouse large intestine, whereas E. coli F-18col-, a derivative of E. coli F-18 that no longer makes the E. coli F-18 colicin, was shown to be a poor mouse colonizer. It was also shown that E. coli F-18 bound two to three times more soluble colonic mucus protein than did E. coli F-18col- and that a major receptor in CD-1 mouse colonic mucus was a 50.5-kilodalton glycoprotein. In the present investigation, an additional E. coli F-18 colonic mucus glycoprotein receptor (66 kilodaltons) and three cecal mucus glycoprotein receptors (94, 73, and 66 kilodaltons) were identified. Numerous colonic and cecal brush border protein receptors specific for E. coli F-18 were also identified. Furthermore, E. coli F-18col- was found to bind to the same mucus and brush border receptors as E. coli F-18, although to a far lesser extent. Adhesion of both E. coli F-18 and F-18col- was inhibited by D-mannose and alpha-methyl-D-mannoside, and both strains were shown to bind specifically to the mannose moiety of a mannose-bovine serum albumin glycoconjugate, although again E. coli F-18col- bound to a lesser extent. Finally, both E. coli F-18 and F-18col- were shown to be piliated. The possible role of pilus mediated adhesion in E. coli F-18 colonization of the streptomycin-treated mouse large intestine is discussed.
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PMID:Colonization of the streptomycin-treated mouse large intestine by a human fecal Escherichia coli strain: role of adhesion to mucosal receptors. 283 41


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