Nature Structural Biology9, 918 - 921 (2002)
Published online: 4 November 2002; | doi:10.1038/nsb865
Structural basis for oligosaccharide-mediated adhesion of Pseudomonas aeruginosa in the lungs of cystic fibrosis patients
Edward Mitchell1, Corinne Houles2, Dvora Sudakevitz3, Michaela Wimmerova2, Catherine Gautier2, Serge Pérez2, Albert M. Wu4, Nechama Gilboa-Garber3
& Anne Imberty2
1
E.S.R.F. Experiments Division, BP 220, F-38043 Grenoble cedex, France.
2
CERMAV-CNRS (affiliated with Université Joseph Fourier), BP 53, F-38041 Grenoble cedex 09, France.
3
Bar-Ilan University, Faculty of Life Sciences, Ramat Gan 52900, Israel.
4
Institute of Molecular and Cellular Biology, College of Medicine, Chang-Gung University, Kwei-San, Tao-yuan, 333, Taiwan.
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 b-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.
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