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

Autor: Corinne Houles, Anne Imberty, Edward P. Mitchell, Serge Pérez, Michaela Wimmerová, Catherine Gautier, Dvora Sudakevitz, Albert M. Wu, Nechama Gilboa-Garber
Přispěvatelé: Centre de Recherches sur les Macromolécules Végétales (CERMAV), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Joseph Fourier - Grenoble 1 (UJF)
Rok vydání: 2002
Předmět:
Zdroj: Nat. Struct. Biol.
Nat. Struct. Biol., 2002, pp.918-921
ISSN: 1072-8368
DOI: 10.1038/nsb865
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 (Le(a)) 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.
Databáze: OpenAIRE