5F97

Blood group antigen binding adhesin BabA of Helicobacter pylori strain A730 in complex with blood group A type 1 hexasaccharide

5F97 の概要

• エントリーDOI: 10.2210/pdb5f97/pdb
• 分子名称: Adhesin binding fucosylated histo-blood group antigen,Adhesin,Adhesin binding fucosylated histo-blood group antigen, Nanbody Nb-ER19, alpha-L-fucopyranose-(1-2)-[2-acetamido-2-deoxy-alpha-D-galactopyranose-(1-3)]beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-3)-beta-D-galactopyranose-(1-4)-beta-D-glucopyranose, ... (4 entities in total)
• 機能のキーワード: adhesin, lectin, nanobody, complex, cell adhesion
• 由来する生物種: Helicobacter pylori; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 257102.48

構造登録者

Moonens, K.,Gideonsson, P.,Subedi, S.,Romao, E.,Oscarson, S.,Muyldermans, S.,Boren, T.,Remaut, H. (登録日: 2015-12-09, 公開日: 2016-01-20, 最終更新日: 2024-10-09)

主引用文献

Moonens, K.,Gideonsson, P.,Subedi, S.,Bugaytsova, J.,Romao, E.,Mendez, M.,Norden, J.,Fallah, M.,Rakhimova, L.,Shevtsova, A.,Lahmann, M.,Castaldo, G.,Brannstrom, K.,Coppens, F.,Lo, A.W.,Ny, T.,Solnick, J.V.,Vandenbussche, G.,Oscarson, S.,Hammarstrom, L.,Arnqvist, A.,Berg, D.E.,Muyldermans, S.,Boren, T.,Remaut, H.
Structural Insights into Polymorphic ABO Glycan Binding by Helicobacter pylori.
Cell Host Microbe, 19:55-66, 2016

PubMed Abstract: 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.

PubMed: 26764597
DOI: 10.1016/j.chom.2015.12.004

実験手法

X-RAY DIFFRACTION (2.62 Å)