Helicobacter pylori Adhesin Binding Fucosylated Histo-Blood Group Antigens Revealed by Retagging

Author:

Ilver Dag12345,Arnqvist Anna12345,Ögren Johan12345,Frick Inga-Maria12345,Kersulyte Dangeruta12345,Incecik Engin T.12345,Berg Douglas E.12345,Covacci Antonello12345,Engstrand Lars12345,Borén Thomas12345

Affiliation:

1. D. Ilver, Department of Microbiology, Umeå University, SE-901 87 Umeå, Sweden.

2. A. Arnqvist, Department of Microbiology and Department of Oral Biology, Umeå University, SE-901 87 Umeå, Sweden.

3. J. Ögren and T. Borén, Department of Oral Biology, Umeå University, SE-901 87 Umeå, Sweden.

4. I.-M. Frick, Department of Cell and Molecular Biology, Lund University, SE-221 00 Lund, Sweden.

5. D. Kersulyte, E. T. Incecik, D. E. Berg, Department of Molecular Microbiology, Washington University Medical School, St. Louis, MO 63110, USA.

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 (Le b ) histo-blood group antigen. The Le b -binding adhesin, BabA, was purified by receptor activity–directed affinity tagging. The bacterial Le b -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.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference49 articles.

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