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

Lukas Gajdos, Matthew P. Blakeley, Michael Haertlein, V. Trevor Forsyth, Juliette M. Devos () and Anne Imberty ()
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Lukas Gajdos: Institut Laue-Langevin
Matthew P. Blakeley: Institut Laue-Langevin
Michael Haertlein: Institut Laue-Langevin
V. Trevor Forsyth: Institut Laue-Langevin
Juliette M. Devos: Institut Laue-Langevin
Anne Imberty: Université Grenoble Alpes, CNRS, CERMAV

Nature Communications, 2022, vol. 13, issue 1, 1-9

Abstract: 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.

Date: 2022
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DOI: 10.1038/s41467-021-27871-8

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