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Neutron crystallography reveals mechanisms used by Pseudomonas aeruginosa for host-cell binding

Author

Listed:
  • Lukas Gajdos

    (Institut Laue-Langevin
    Partnership for Structural Biology (PSB)
    Université Grenoble Alpes, CNRS, CERMAV)

  • Matthew P. Blakeley

    (Institut Laue-Langevin)

  • Michael Haertlein

    (Institut Laue-Langevin
    Partnership for Structural Biology (PSB))

  • V. Trevor Forsyth

    (Institut Laue-Langevin
    Partnership for Structural Biology (PSB)
    Keele University
    Lund University)

  • Juliette M. Devos

    (Institut Laue-Langevin
    Partnership for Structural Biology (PSB))

  • Anne Imberty

    (Université Grenoble Alpes, CNRS, CERMAV)

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.

Suggested Citation

  • Lukas Gajdos & Matthew P. Blakeley & Michael Haertlein & V. Trevor Forsyth & Juliette M. Devos & Anne Imberty, 2022. "Neutron crystallography reveals mechanisms used by Pseudomonas aeruginosa for host-cell binding," Nature Communications, Nature, vol. 13(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-021-27871-8
    DOI: 10.1038/s41467-021-27871-8
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    References listed on IDEAS

    as
    1. Daniel Passos da Silva & Michael L. Matwichuk & Delaney O. Townsend & Courtney Reichhardt & Doriano Lamba & Daniel J. Wozniak & Matthew R. Parsek, 2019. "The Pseudomonas aeruginosa lectin LecB binds to the exopolysaccharide Psl and stabilizes the biofilm matrix," Nature Communications, Nature, vol. 10(1), pages 1-11, December.
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    Cited by:

    1. Jahaun Azadmanesh & Katelyn Slobodnik & Lucas R. Struble & William E. Lutz & Leighton Coates & Kevin L. Weiss & Dean A. A. Myles & Thomas Kroll & Gloria E. O. Borgstahl, 2024. "Revealing the atomic and electronic mechanism of human manganese superoxide dismutase product inhibition," Nature Communications, Nature, vol. 15(1), pages 1-18, December.
    2. Jody Pacalon & Guillaume Audic & Justine Magnat & Manon Philip & Jérôme Golebiowski & Christophe J. Moreau & Jérémie Topin, 2023. "Elucidation of the structural basis for ligand binding and translocation in conserved insect odorant receptor co-receptors," Nature Communications, Nature, vol. 14(1), pages 1-11, December.

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