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

Varování

Publikace nespadá pod Pedagogickou 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