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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adhesins, Bacterial / chemistry
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Adhesins, Bacterial / genetics
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Adhesins, Bacterial / isolation & purification*
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Adhesins, Bacterial / metabolism
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Amino Acid Sequence
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Antigens, Bacterial*
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Bacterial Adhesion
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Bacterial Proteins / genetics
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Bacterial Proteins / physiology
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Base Composition
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Base Sequence
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Biotinylation
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Cell Membrane / chemistry
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Cloning, Molecular
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Codon, Initiator
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Fucose
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Gastric Mucosa / microbiology
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Genes, Bacterial
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Glycoconjugates / metabolism
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Helicobacter pylori / isolation & purification
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Helicobacter pylori / metabolism*
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Helicobacter pylori / pathogenicity
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Humans
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Lewis Blood Group Antigens / metabolism*
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Ligands
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Molecular Sequence Data
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Virulence
Substances
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Adhesins, Bacterial
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Antigens, Bacterial
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Bacterial Proteins
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Codon, Initiator
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Glycoconjugates
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Lewis Blood Group Antigens
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Ligands
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cagA protein, Helicobacter pylori
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Fucose
Associated data
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GENBANK/AF001388
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GENBANK/AF001389
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GENBANK/AF033654