Structural basis for oligosaccharide-mediated adhesion of Pseudomonas aeruginosa in the lungs of cystic fibrosis patients

Varování

Publikace nespadá pod Ekonomicko-správní fakultu, ale pod Přírodovědeckou fakultu. Oficiální stránka publikace je na webu muni.cz.

Autoři	MITCHELL Edward HOULES Corinne SUDAKEVITZ Dvora WIMMEROVÁ Michaela GAUTIER Catherine PÉREZ Serge WU Albert M. GILBOA-GARBER Nechama IMBERTY Anne
Rok publikování	2002
Druh	Článek v odborném periodiku
Časopis / Zdroj	Nature Structural Biology
Fakulta / Pracoviště MU	Přírodovědecká fakulta
Citace
Obor	Biochemie
Klíčová slova	lectin; Pseudomonas aeruginosa; cystic fibrosis; crystal structure
Popis	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.
Související projekty:	Biomolekulární centrum