Glycobiology Advance Access originally published online on February 16, 2005
Glycobiology 2005 15(7):700-708; doi:10.1093/glycob/cwi049
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Identification and characterization of binding properties of Helicobacter pylori by glycoconjugate arrays
2 Department of Operative Dentistry and Periodontology, Dental School, University of Regensburg, D-93053 Regensburg, Germany; 3 Max von Pettenkofer Institute, Ludwig-Maximilians University, D-80336 München, Germany; 4 School of Health Sciences, University College of Borås, SE-501 90 Borås, Sweden; and 5 Department of Medical Biochemistry and Biophysics, Umeå University, SE-90187 Umeå, Sweden
1 To whom correspondence should be addressed; e-mail: stefan.ruhl{at}klinik.uni-regensburg.de
Received on December 28, 2004; revised on February 11, 2005; accepted on February 14, 2005
The microaerophilic bacterium Helicobacter pylori is well established for its role in development of different gastric diseases. Bacterial adhesins and corresponding binding sites on the epithelial surface allow H. pylori to colonize the gastric tissue. In this investigation, the adhesion of H. pylori to dot blot arrays of natural glycoproteins and neoglycoproteins was studied. Adhesion was detected by overlay with fluorescence-labeled bacteria on immobilized (neo)glycoproteins. The results confirmed the interaction between the adhesin BabA and the H-1-, Lewis b-, and related fucose-containing antigens. In addition, H. pylori bound to terminal 
2-3-linked sialic acids as previously described. The use of a sabA mutant and sialidase treatment of glycoconjugate arrays showed that the adherence of H. pylori to laminin is mediated by the sialic acid-binding adhesin, SabA. The adhesion to salivary mucin MUC5B is mainly associated with the BabA adhesin and to a lesser extent with the SabA adhesin. This agrees with reports, that MUC5B carries both fucosylated blood group antigens and 2-3-linked sialic acids. The adhesion of H. pylori to fibronectin and lactoferrin persisted in the babA/sabA double mutant. Because binding to these molecules was abolished by denaturation rather than by deglycosylation, it was suggested to depend on the recognition of unknown receptor moieties by an additional unknown bacterial surface component. The results demonstrate that the bacterial overlay method on glycoconjugate arrays is a useful tool for exploration and the characterization of unknown adhesin specificities of H. pylori and other bacteria.
Key words: adhesins / glycoproteins / Helicobacter pylori / lectins / neoglycoproteins
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