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

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

Salmonella typhimurium 798 is known to persistently colonize swine. A key step required to initiate colonization of intestines is adhesion of the organism to the intestinal epithelium. However, S. typhimurium 798 initially failed to attach to porcine enterocytes in vitro. An enrichment procedure was used to select adhesive S. typhimurium, and when cells of one colony type were grown in tryptone phosphate broth they were adhesive. Cells from a colony with a different morphology were not adhesive. Adhesion was time dependent, with maximal adhesion occurring at 1 h. As determined by electron microscopy, cells of the adhesive phenotype had pili while none of the cells with the nonadhesive phenotype produced pili. The pili on the adhesive cells were morphologically similar to type 1 pili. Mannose (0.5%) did not affect adhesion, suggesting that the adhesin on strain 798 did not recognize mannose as a receptor. An analysis of envelope proteins from cells of both phenotypes showed that the adhesive-phenotype cells expressed at least 10 unique proteins ranging in size from 20 to 60 kDa. Absorbed antiserum against cells of the adhesive phenotype agglutinated adhesive cells and was used to detect unique surface antigens on the cells of the adhesive phenotype by Western blots (immunoblots). These antigens were in the range of 30 kDa in size. An envelope extract competitively inhibited the binding of S. typhimurium to enterocytes, as did Fab fragments prepared from the absorbed serum. Cells of both phenotypes contained two plasmids, and each had identical restriction digestion patterns. Cells of the adhesive phenotype consistently were found to be more readily phagocytosed by pig leukocytes, and once in the phagocytes they survived better than cells of the nonadhesive phenotype.
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PMID:Adhesion of Salmonella typhimurium to porcine intestinal epithelial surfaces: identification and characterization of two phenotypes. 163 89

The occurrence and significance of bacterial carbohydrate recognition proteins (bacterial lectins) and endogenous carbohydrate binding proteins (endogenous lectins) of human urothelium as well as kidney tubulus epithelium was analyzed with respect to the adhesion of urotoxogenic Escherichia coli bacteria. Using biotinylated neoglycoproteins, we demonstrated a wide spectrum of endogenous lectins with Galactose-, Mannose-, Fucose-, N-Acetylgalactosamine-, and N-Acetylglucosamine binding activities in the urothelium. In the kidney the distal nephron and especially the medullar collecting ducts exhibited a similar spectrum of endogenous carbohydrate binding activities as detected for the urothelium. Adhesion- as well as inhibition-experiments with selective blocking of either bacterial lectins or endogenous lectins of the target cells by different carbohydrates both reduced the bacterial adhesion. However, maximal inhibition of bacterial adhesion was achieved by simultanous blocking of microbial and target cell lectins with mannose or mannan. From these results it is reasonable to conclude that specific adhesion which may result in an organotropism (urotropism) of E. coli infection is due to a dual recognition mechanism which is accomplished by the combined interaction of the bachterial and host cell lectins with the corresponding carbohydrates of E. coli and that of the target cells respectively. Further studies showed that normal human serum possesses natural antiadhesins which are represented by the glycan parts of the serum-glycoproteins.
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PMID:[Topography and mechanisms of adhesion of uropathogenic Escherichia coli bacteria in the human kidney and renal pelvis]. 248 13

Adhesion of P. aeruginosa to normal and injured rat tracheas was examined. Rat tracheas were injured by exposure to 0.1N HCl for 10 min, and incubated with P. aeruginosa. Adhesion was quantitated by direct count of the number of bacteria attached to a fixed surface area as viewed by scanning electron microscopy. P. aeruginosa adhered to injured tracheas much more than to normal tracheas. The adhesion of P. aeruginosa, preincubated with mucin and sugars, to acid injured trachea was examined. Mucin, N-acetylneuraminic acid and N-acetyl-D-galactosamine inhibited the adhesion of P. aeruginosa to injured tracheas, but not N-acetylglucosamine, L-fucose, D-mannose and D-galactose. Periodate oxidation and neuraminidase treatment of acid injured tracheas reduced the adhesion of P. aeruginosa. These data suggest that N-acetylneuraminic acid (sialic acid) is the receptor for P. aeruginosa or a part of the receptor in acid injured rat trachea and in tracheobronchial mucin.
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PMID:[Study of the receptor for P. aeruginosa on tracheal cells and in tracheobronchial mucin]. 250 16

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

Adhesions of 211 strains of uropathogenic Escherichia coli and 19 strains of normal fecal E. coli were characterized by patterns of agglutination with human erythrocytes, Saccharomyces cerevisiae, and horse erythrocytes coated with the P blood-group receptor (P). Mannose-resistant (MR) hemagglutination was significantly associated with P agglutination (P less than .001). E. coli expressing MR and/or P (MR/P) agglutinins concurrently with mannose-sensitive (MS) agglutinins predominated in all clinical categories. The highest percentage of E. coli demonstrating MR/P agglutinins, in the absence of MS agglutinins, was recovered from patients with acute pyelonephritis (35%) compared with percentages of patients with chronic pyelonephritis (13%), asymptomatic bacteriuria (16%), cystitis (11%), and normal fecal control E. coli (11%). Sixty-nine percent of E. coli isolates causing acute pyelonephritis agglutinated P-coated horse erythrocytes compared with only 11% of the fecal isolates. Strains expressing MR/P agglutinins (in the absence of MS agglutinins) isolated from patients with acute pyelonephritis, chronic pyelonephritis, and asymptomatic bacteriuria were significantly associated with the presence of antibody-coated bacteria in patients' urine sediments (P less than .010), an observation indicative of an immune response associated with bacterial invasion of host tissues.
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PMID:Mannose-resistant hemagglutination and P receptor recognition of uropathogenic Escherichia coli isolated from adult patients. 285 51

The effect of various lectins and sugars on adhesion of five strains of Candida albicans to buccal and vaginal epithelial cells in vitro was investigated. Adhesion of C. albicans GDH 2346 was inhibited primarily by L-fucose and winged-pea lectin, whereas adhesion of strain GDH 2023 was inhibited by N-acetyl-D-glucosamine, or D-glucosamine, and wheat-germ agglutinin. Three other strains of C. albicans (MRL 3153, GRI 681 and GRI 682) gave results similar to those obtained with strain GDH 2346. Extracellular polymeric material (EP) isolated from strain GDH 2346 inhibited adhesion of strains MRL 3153, GRI 681 and GRI 682 by more than 50%, but that of strain GDH 2023 by only 30%. EP from strain GDH 2023 had little or no effect on the adhesion of any other yeast strain. Lectin-like proteins with affinities for L-fucose, N-acetyl-D-glucosamine and D-mannose were detected in EP from all five strains in different amounts. These results indicate that there are at least two types of adhesion mechanism and that glycosides containing L-fucose or N-acetyl-D-glucosamine can function as epithelial cell receptors for C. albicans.
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PMID:Role of glycosides as epithelial cell receptors for Candida albicans. 330 64

Several properties of the adhesins of eight isolates of Moraxella bovis recovered from cattle suffering from infectious keratoconjunctivitis, were studied. Adhesions were detected through autoagglutination in saline and hemagglutination. Autoagglutinating strains agglutinated red blood cells of the chicken, rabbit, sheep and swine, but not those of the guinea pig. The adhesins were not inhibited by D-mannose or D-galactose and resisted heating at 100 degrees C for 15 minutes. Magnesium chloride at a final concentration of 10% inhibited autoagglutination and hemagglutination. The value of the hemagglutination test for monitoring synthesis of fimbriae by M. bovis, is discussed.
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PMID:Moraxella bovis hemagglutinins: effect of carbohydrates, heating and erythrocytes. 398 74

Cell-cell aggregation and cell-substratum adherence, two functional manifestations of granulocytes of potential clinical relevance, are widely considered to result from identical cell membrane alterations. Our study casts doubt on this assumption and defines the complement-derived adhesion-inducing (pectic)/enzyme releasing activity as an entity that is clearly separable from the chemotactic/aggregating activity (C5adesArg). Using selective activators of the alternative and the classical pathway of the complement system, unexpected dissimilarities were observed. Adhesion inducing potency that went in parallel with secondary granule content liberation, and respiratory burst activation (hexose monophosphate shunt activation), was confined to alternate pathway activators, was heat-labile (50 degrees) and could be inhibited by the protease inhibitor di-isopropylfluorophosphate. In contrast, plasma activated with aggregated gamma-globulin or cobra venom factor had no pectic/burst activating capacity but was equally potent in inducing heat- and DFP-resistant chemotactic-aggregating activity. It was further shown that, even in the presence of cytochalasin B, C5adesArg (evoked in whole plasma) does not liberate secondary granule constituents. These findings were corroborated by using highly purified C5adesArg. Our data suggest that the complement system plays a dual role in PMN accumulation at the inflammatory focus: whereas C5adesArg orientates cellular movement toward the site of bacterial invasion, the complement-dependent pexin(s) is mainly involved in confining infections localized by the adhesion-induced trapping of highly reactive cells.
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PMID:Complement-induced granulocyte adhesion and aggregation are mediated by different factors: evidence for non-equivalence of the two cell functions. 649 97

The ability of rabbit alveolar macrophages to specifically recognize and adhere to surfaces derivatized with carbohydrates was examined. Otherwise inert polyacrylamide gels were derivatized with aminohexylglycosides as previously described (Guarnaccia, S. P., and Schnaar, R. L. (1982) J. Biol. Chem. 257, 14288-14292). Intact viable rabbit alveolar macrophages, isolated by lung lavage, were placed in contact with surfaces derivatized with different glycosides. Only those surfaces derivatized with alpha-D-mannose residues were capable of supporting rabbit alveolar macrophage adhesion. Adhesion was rapid, obtaining maximal levels within 10 min, and occurred readily at either 0 or 37 degrees C. The carbohydrate specificity of the cell adhesion was investigated by the use of soluble carbohydrate inhibitors. The potency of various saccharides to block the adhesion correlated with that demonstrated for blocking the uptake or binding of radiolabeled soluble glycoproteins (Shepherd, V. L., Lee, Y. C., Schlesinger, P. H., and Stahl, P. D. (1981) Proc. Natl. Acad. Sci. U.S.A. 78, 1019-1022). Thus, the order of potency observed was: D-Man congruent to L-Fuc greater than D-GlcNAc congruent to D-Glc much greater than D-Gal congruent to D-GalNAc congruent to L-rhamnose. While soluble monosaccharides were capable of blocking adhesion when added in millimolar concentrations, polymannosylated neoglycoproteins were able to block adhesion in the nanomolar concentration range. Adhesion to the mannose-derivatized surfaces was a dynamic event even at 0 degrees C, since adhesion was less susceptible to monosaccharide inhibition at later incubation times. Surfaces derivatized with aminohexyl S-mannoside ligands were more effective in supporting adhesion than those derivatized with the corresponding O-mannosides. Soluble inhibitor studies suggest that this was due to a more favorable conformation of the S-glycoside for binding to the cell surface receptor. The results reported here demonstrate that the previously reported alveolar macrophage mannose/fucose receptor can mediate carbohydrate-specific cell adhesion.
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PMID:Carbohydrate-specific adhesion of alveolar macrophages to mannose-derivatized surfaces. 669 35


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