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The gastric pathogen Helicobacter pylori is highly adapted to survival in the human stomach and responsible for the majority of peptic ulcer and gastric cancer cases worldwide. An important survival strategy for the bacterium involves the tight binding to the stomach mucosa, out of reach of the noxious gastric juices. To do so, H. pylori adheres to blood group sugars found on gastric mucus and underlying cells. Scientists at the labs of Han Remaut at VIB and Vrije Universiteit Brussel, and Thomas Borén at Umeå University in Sweden, provide detailed structural and functional insights into the protein responsible for this interaction. Part of this structural information was obtained on PROXIMA1 et PROXIMA2 beamlines.
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Figure: Superimposition of 3 structures of BabA (ribbons representation) from 3 H.pylori strains, bound to an blood group antigen hexasaccharide (molecule A to F). Two loops, DL1 and DL2 (« DL » = « diversification loop »), provide adaptive control to the bacterium binding affinity, notably ABO versus O blood group preference. CL2, « Cys-clasped loop », forms the basis for the rational design of novel anti-adhesive drugs that would reduce bacterial attachment, stomach inflammation and hence lower the risk for overt disease development.
Figure: Superimposition of 3 structures of BabA (ribbons representation) from 3 H.pylori strains, bound to an blood group antigen hexasaccharide (molecule A to F). Two loops, DL1 and DL2 (« DL » = « diversification loop »), provide adaptive control to the bacterium binding affinity, notably ABO versus O blood group preference. CL2, « Cys-clasped loop », forms the basis for the rational design of novel anti-adhesive drugs that would reduce bacterial attachment, stomach inflammation and hence lower the risk for overt disease development.