Structural basis of Lewis antigen binding by the Helicobacter pylori adhesin BabA
نویسندگان
چکیده
School of Pharmacy, University of Nottingham, University Park, Nottingham NG7 2RD, UK. Discovery Sciences, Innovative Medicines and Early Development, AstraZeneca R&D, Alderley Park, Cheshire SK10 4TG, UK. Discovery Sciences, Innovative Medicines and Early Development, AstraZeneca R&D, Darwin Building, 310 Cambridge Science Park, Milton Road, Cambridge CB4 0WG, UK. Pharmaceutical Development, AstraZeneca R&D, Charter Way, Macclesfield, Cheshire SK10 2NA, UK. *These authors contributed equally to this work. †Corresponding author. E-mail: [email protected] (T.H.); franco.falcone@ nottingham.ac.uk (F.H.F.)
منابع مشابه
Structural basis of Lewisb antigen binding by the Helicobacter pylori adhesin BabA
Helicobacter pylori is a leading cause of peptic ulceration and gastric cancer worldwide. To achieve colonization of the stomach, this Gram-negative bacterium adheres to Lewis(b) (Le(b)) antigens in the gastric mucosa using its outer membrane protein BabA. Structural information for BabA has been elusive, and thus, its molecular mechanism for recognizing Le(b) antigens remains unknown. We prese...
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The strength of binding between the Helicobacter pylori blood group antigen-binding adhesin (BabA) and its cognate glycan receptor, the Lewis b blood group antigen (Le(b)), was measured by means of atomic force microscopy. High-resolution measurements of rupture forces between single receptor-ligand pairs were performed between the purified BabA and immobilized Le(b) structures on self-assemble...
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UNLABELLED Helicobacter pylori undergoes rapid microevolution during chronic infection, but very little is known about how this affects host interaction factors. The best-studied adhesin of H. pylori is BabA, which mediates binding to the blood group antigen Lewis b [Le(b)]. To study the dynamics of Le(b) adherence during human infection, we analyzed paired H. pylori isolates obtained sequentia...
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تاریخ انتشار 2015