Pseudomonas aeruginosa galactose- and fucose-binding lectins (PA-IL and PA-IIL) contribute to the virulence of this pathogenic bacterium, which is a major cause of morbidity and mortality in cystic fibrosis patients. The crystal structure of PA-IIL in complex with fucose reveals a tetrameric structure. Each monomer displays a nine-stranded, antiparallel β-sandwich arrangement and contains two close calcium cations that mediate the binding of fucose in a recognition mode unique among carbohydrate-protein interactions. Experimental binding studies, together with theoretical docking of fucose-containing oligosaccharides, are consistent with the assumption that antigens of the Lewis a (Lea) series may be the preferred ligands of this lectin. Precise knowledge of the lectin-binding site should allow a better design of new antibacterial-adhesion prophylactics.
|Number of pages||4|
|Journal||Nature Structural Biology|
|State||Published - 1 Dec 2002|
Bibliographical noteFunding Information:
We thank J. Lescar for his help in data collection and ESRF for provision of synchrotron facilities. C.H. is supported by a grant from the French association ANRS, M.W. is supported by the French minister program for invited scientists and partial financial support is acknowledged from the Ministry of Education of the Czech Republic.