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Structural Insights into Polymorphic ABO Glycan Binding by Helicobacter pylori
VIB, Struct Biol Res Ctr, Struct & Mol Microbiol, Pl Laan 2, B-1050 Brussels, Belgium.;Vrije Univ Brussel, Struct Biol Brussels, Pl Laan 2, B-1050 Brussels, Belgium..
Umeå Univ, Dept Med Biochem & Biophys, SE-90187 Umeå, Sweden..
VIB, Struct Biol Res Ctr, Struct & Mol Microbiol, Pl Laan 2, B-1050 Brussels, Belgium.;Vrije Univ Brussel, Struct Biol Brussels, Pl Laan 2, B-1050 Brussels, Belgium..
Umeå Univ, Dept Med Biochem & Biophys, SE-90187 Umeå, Sweden..
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2016 (English)In: Cell Host and Microbe, ISSN 1931-3128, E-ISSN 1934-6069, Vol. 19, no 1, p. 55-66Article in journal (Refereed) Published
Abstract [en]

The Helicobacter pylori adhesin BabA binds mucosal ABO/Le b blood group (bg) carbohydrates. BabA facilitates bacterial attachment to gastric surfaces, increasing strain virulence and forming a recognized risk factor for peptic ulcers and gastric cancer. High sequence variation causes BabA functional diversity, but the underlying structural-molecular determinants are unknown. We generated X-ray structures of representative BabA isoforms that reveal a polymorphic, three-pronged Le(b) binding site. Two diversity loops, DL1 and DL2, provide adaptive control to binding affinity, notably ABO versus O bg preference. H. pylori strains can switch bg preference with single DL1 amino acid substitutions, and can coexpress functionally divergent BabA isoforms. The anchor point for receptor binding is the embrace of an ABO fucose residue by a disulfide-clasped loop, which is inactivated by reduction. Treatment with the redox-active pharmaceutic N-acetylcysteine lowers gastric mucosal neutrophil infiltration in H. pylori-infected Le(b)-expressing mice, providing perspectives on possible H. pylori eradication therapies.

Place, publisher, year, edition, pages
Elsevier BV , 2016. Vol. 19, no 1, p. 55-66
National Category
Microbiology in the medical area
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URN: urn:nbn:se:kth:diva-305697DOI: 10.1016/j.chom.2015.12.004ISI: 000369839900010PubMedID: 26764597Scopus ID: 2-s2.0-84959550066OAI: oai:DiVA.org:kth-305697DiVA, id: diva2:1617250
Note

QC 20211206

Available from: 2021-12-06 Created: 2021-12-06 Last updated: 2022-06-25Bibliographically approved

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Lahmann, Martina

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Mendez, MelissaLahmann, MartinaCoppens, FannySolnick, Jay V.Vandenbussche, GuyOscarson, StefanMuyldermans, SergeRemaut, Han
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