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      Helicobacter pylori adhesin binding fucosylated histo-blood group antigens revealed by retagging.

      Science (New York, N.Y.)

      Virulence, Adhesins, Bacterial, chemistry, genetics, isolation & purification, metabolism, Amino Acid Sequence, Antigens, Bacterial, Bacterial Adhesion, Bacterial Proteins, physiology, Base Composition, Base Sequence, Biotinylation, Cell Membrane, Cloning, Molecular, Codon, Initiator, Fucose, Gastric Mucosa, microbiology, Genes, Bacterial, Glycoconjugates, Helicobacter pylori, pathogenicity, Humans, Lewis Blood-Group System, Ligands, Molecular Sequence Data

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          Abstract

          The bacterium Helicobacter pylori is the causative agent for peptic ulcer disease. Bacterial adherence to the human gastric epithelial lining is mediated by the fucosylated Lewis b (Leb) histo-blood group antigen. The Leb-binding adhesin, BabA, was purified by receptor activity-directed affinity tagging. The bacterial Leb-binding phenotype was associated with the presence of the cag pathogenicity island among clinical isolates of H. pylori. A vaccine strategy based on the BabA adhesin might serve as a means to target the virulent type I strains of H. pylori.

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          9430586

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