ArticleNature communications2022
Neutron crystallography reveals mechanisms used by Pseudomonas aeruginosa for host-cell binding.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 29 citations in OpenAlex.
- Fucose-tobramycin sponge-like microparticles to treat pulmonary Pseudomonas aeruginosa infections in a lectin-competitive approach.Journal of advanced research · 2026Article
- Environmental Contributions to Proton Sharing in Protein Low-Barrier Hydrogen Bonds.Biochemistry · 2026Article
- Environmental Contributions to Proton Sharing in Protein Low-Barrier Hydrogen Bonds.bioRxiv : the preprint server for biology · 2025Article
- Current and future perspectives for structural biology at the Grenoble EPN campus: a comprehensive overview.Journal of synchrotron radiation · 2025Review
- Counter-diffusion studies of human transthyretin: the growth of high-quality crystals for X-ray and neutron crystallography.Journal of applied crystallography · 2025Article
- Tools for structural lectinomics: From structures to lectomes.BBA advances · 2025Article
- Restoring protein glycosylation with GlycoShape.Nature methods · 2024Article
- Universality of critical active site glutamate as an acid-base catalyst in serine hydroxymethyltransferase function.Chemical science · 2024Article
- Revealing the atomic and electronic mechanism of human manganese superoxide dismutase product inhibition.Nature communications · 2024Article
- Neutron diffraction from a microgravity-grown crystal reveals the active site hydrogens of the internal aldimine form of tryptophan synthase.Cell reports. Physical science · 2024Article
- Photoswitchable glycoligands targetingBeilstein journal of organic chemistry · 2024Article
- Exploring the World of Membrane Proteins: Techniques and Methods for Understanding Structure, Function, and Dynamics.Molecules (Basel, Switzerland) · 2023Review
- Glycomimetics for the inhibition and modulation of lectins.Chemical Society reviews · 2023Review
- Anti-Bacterial Adhesion on Abiotic and Biotic Surfaces of the Exopolysaccharide from the Marine Bacillus licheniformis B3-15.Marine drugs · 2023Article
- Recent advances in therapeutic targets identification and development of treatment strategies towards Pseudomonas aeruginosa infections.BMC microbiology · 2023Review
- Relating protein crystal structure to ligand-binding thermodynamics.Acta crystallographica. Section F, Structural biology communications · 2022Article
- Discovery ofJournal of medicinal chemistry · 2022Article
- Multivalent glycocyclopeptides: conjugation methods and biological applications.Chemical Society reviews · 2022Review
- An N⋯H⋯N low-barrier hydrogen bond preorganizes the catalytic site of aspartate aminotransferase to facilitate the second half-reaction.Chemical science · 2022Article
- Structural Considerations for Building Synthetic Glycoconjugates as Inhibitors for Pseudomonas aeruginosa Lectins.ChemMedChem · 2022Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The opportunistic pathogen Pseudomonas aeruginosa, a major cause of nosocomial infections, uses carbohydrate-binding proteins (lectins) as part of its binding to host cells. The fucose-binding lectin, LecB, displays a unique carbohydrate-binding site that incorporates two closely located calcium ions bridging between the ligand and protein, providing specificity and unusually high affinity. Here, we investigate the mechanisms involved in binding based on neutron crystallography studies of a fully deuterated LecB/fucose/calcium complex. The neutron structure, which includes the positions of all the hydrogen atoms, reveals that the high affinity of binding may be related to the occurrence of a low-barrier hydrogen bond induced by the proximity of the two calcium ions, the presence of coordination rings between the sugar, calcium and LecB, and the dynamic behaviour of bridging water molecules at room temperature. These key structural details may assist in the design of anti-adhesive compounds to combat multi-resistance bacterial infections.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.