ArticleScience advances2015
Structural basis of Lewis(b) antigen binding by the Helicobacter pylori adhesin BabA.
Article in Science advances, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed.
- Molecular Characterization and Genetic Diversity ofDiagnostics (Basel, Switzerland) · 2026Article
- Rice bran protein peptide PVLWGVPKG alleviate gastric mucosal damage induced by Helicobacter pylori infection.NPJ science of food · 2026Article
- Host range and zoonotic potential linked to P-like fimbrial (PLF) adhesin specificity in avian pathogenic Escherichia coli.PLoS pathogens · 2026Article
- Predicting clinical outcomes in Helicobacter pylori-positive patients using supervised learning through the integration of demographic and genomic features.BMC gastroenterology · 2026Article
- Divergent Enzymatic Synthesis of a Comprehensive Type‑1 Glycan Determinant Library.ACS catalysis · 2025Article
- Synergistic potentiation of antibiotics by chamomile phytochemicals against multidrug-resistant Helicobacter pylori.Gut pathogens · 2025Article
- Article
- Fucosylation of glycoproteins and glycolipids: opposing roles in cholera intoxication.Nature chemical biology · 2025Article
- Glycan-mediated adhesion mechanisms in antibiotic-resistant bacteria.BBA advances · 2025Article
- Architectural dissection of adhesive bacterial cell surface appendages from a "molecular machines" viewpoint.Journal of bacteriology · 2024Review
- Marine-Derived Fucose-Containing Carbohydrates: Review of Sources, Structure, and Beneficial Effects on Gastrointestinal Health.Foods (Basel, Switzerland) · 2024Review
- Targeted nanotherapeutics for the treatment of Helicobacter pylori infection.Journal of biomedical science · 2024Review
- Synthesis, DFT, andHeliyon · 2024Article
- Probing the expression and adhesion of glycans involved in Helicobacter pylori infection.Scientific reports · 2024Article
- High-Salt Diet ExacerbatesJournal of personalized medicine · 2023Review
- ABO, Lewis blood group systems and secretory status with H.pylori infection in yemeni dyspeptic patients: a cross- sectional study.BMC infectious diseases · 2023Article
- Fucosylated glycoproteins and fucosylated glycolipids play opposing roles in cholera intoxication.bioRxiv : the preprint server for biology · 2023Article
- The Role of Adhesion in Helicobacter pylori Persistent Colonization.Current microbiology · 2023Review
- Review
- Host Cell Antimicrobial Responses againstInternational journal of molecular sciences · 2022Review
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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 present the crystal structure of the extracellular domain of BabA, from H. pylori strain J99, in the absence and presence of Le(b) at 2.0- and 2.1-Å resolutions, respectively. BabA is a predominantly α-helical molecule with a markedly kinked tertiary structure containing a single, shallow Le(b) binding site at its tip within a β-strand motif. No conformational change occurs in BabA upon binding of Le(b), which is characterized by low affinity under acidic [K D (dissociation constant) of ~227 μM] and neutral (K D of ~252 μM) conditions. Binding is mediated by a network of hydrogen bonds between Le(b) Fuc1, GlcNAc3, Fuc4, and Gal5 residues and a total of eight BabA amino acids (C189, G191, N194, N206, D233, S234, S244, and T246) through both carbonyl backbone and side-chain interactions. The structural model was validated through the generation of two BabA variants containing N206A and combined D233A/S244A substitutions, which result in a reduction and complete loss of binding affinity to Le(b), respectively. Knowledge of the molecular basis of Le(b) recognition by BabA provides a platform for the development of therapeutics targeted at inhibiting H. pylori adherence to the gastric mucosa.
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