Ontology highlight
ABSTRACT:
SUBMITTER: Moonens K
PROVIDER: S-EPMC4793151 | biostudies-literature | 2016 Jan
REPOSITORIES: biostudies-literature
Moonens Kristof K Gideonsson Pär P Subedi Suresh S Bugaytsova Jeanna J Romaõ Ema E Mendez Melissa M Nordén Jenny J Fallah Mahsa M Rakhimova Lena L Shevtsova Anna A Lahmann Martina M Castaldo Gaetano G Brännström Kristoffer K Coppens Fanny F Lo Alvin W AW Ny Tor T Solnick Jay V JV Vandenbussche Guy G Oscarson Stefan S Hammarström Lennart L Arnqvist Anna A Berg Douglas E DE Muyldermans Serge S Borén Thomas T Remaut Han H
Cell host & microbe 20160101 1
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 ...[more]