ArticleThe Journal of biological chemistry2014
The three-dimensional structure of the extracellular adhesion domain of the sialic acid-binding adhesin SabA from Helicobacter pylori.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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33 citing papers in PubMed, 70 citations in OpenAlex.
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- Synergic Effects of Curcumin, Licorice, and Endoscopic Photodynamic Therapy Against Helicobacter Pylori by Modulating the NF-Κb Signaling Pathway.Iranian journal of biotechnology · 2025Article
- Architectural dissection of adhesive bacterial cell surface appendages from a "molecular machines" viewpoint.Journal of bacteriology · 2024Review
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- The Role of Adhesion in Helicobacter pylori Persistent Colonization.Current microbiology · 2023Review
- Exploring the inhibitory potential ofFrontiers in molecular biosciences · 2023Article
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- Antimicrobial resistance patterns and genetic elements associated with the antibiotic resistance of Helicobacter pylori strains from Shanghai.Gut pathogens · 2022Article
- Comparative Structural Dynamics of Isoforms ofFrontiers in molecular biosciences · 2022Article
- Review
- Structural and binding characterization of the LacdiNAc-specific adhesin (LabA; HopD) exodomain fromCurrent research in structural biology · 2021Article
- Helicobacter pylori treatment in the post-antibiotics era-searching for new drug targets.Applied microbiology and biotechnology · 2020Review
- Virulence of Helicobacter pylori outer membrane proteins: an updated review.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2020Review
- Sugar Codes Conjugated Alginate: An Innovative Platform to Make a Strategic Breakthrough in Simultaneous Prophylaxis of GERD andDrug design, development and therapy · 2020Article
- Type V Secretion in Gram-Negative Bacteria.EcoSal Plus · 2019Article
- Helicobacter pylori SabA binding gangliosides of human stomach.Virulence · 2018Article
- TheThe EMBO journal · 2018Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The gastric pathogen Helicobacter pylori is a major cause of acute chronic gastritis and the development of stomach and duodenal ulcers. Chronic infection furthermore predisposes to the development of gastric cancer. Crucial to H. pylori survival within the hostile environment of the digestive system are the adhesins SabA and BabA; these molecules belong to the same protein family and permit the bacteria to bind tightly to sugar moieties Lewis(B) and sialyl-Lewis(X), respectively, on the surface of epithelial cells lining the stomach and duodenum. To date, no representative SabA/BabA structure has been determined, hampering the development of strategies to eliminate persistent H. pylori infections that fail to respond to conventional therapy. Here, using x-ray crystallography, we show that the soluble extracellular adhesin domain of SabA shares distant similarity to the tetratricopeptide repeat fold family. The molecule broadly resembles a golf putter in shape, with the head region featuring a large cavity surrounded by loops that vary in sequence between different H. pylori strains. The N-terminal and C-terminal helices protrude at right angles from the head domain and together form a shaft that connects to a predicted outer membrane protein-like β-barrel trans-membrane domain. Using surface plasmon resonance, we were able to detect binding of the SabA adhesin domain to sialyl-Lewis(X) and Lewis(X) but not to Lewis(A), Lewis(B), or Lewis(Y). Substitution of the highly conserved glutamine residue 159 in the predicted ligand-binding pocket abrogates the binding of the SabA adhesin domain to sialyl-Lewis(X) and Lewis(X). Taken together, these data suggest that the adhesin domain of SabA is sufficient in isolation for specific ligand binding.
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