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

Abstract

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.

• Authors: Edward Mitchell, Corinne Houles, Dvora Sudakevitz, Michaela Wimmerova, Catherine Gautier, Serge Pérez, Albert M Wu, Nechama Gilboa-Garber, Anne Imberty
• Journal: Nature structural biology (Nat Struct Biol) Vol. 9 Issue 12 Pg. 918-21 (Dec 2002) ISSN: 1072-8368 [Print] United States
• PMID: 12415289 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Adhesins, Bacterial
• Lectins
• Macromolecular Substances
• Oligosaccharides
• adhesin, Pseudomonas
• Fucose
• Calcium

Topics

• Adhesins, Bacterial (chemistry, metabolism)
• Bacterial Adhesion
• Binding Sites
• Calcium (chemistry, metabolism)
• Crystallography, X-Ray
• Cystic Fibrosis (microbiology)
• Fucose (chemistry, metabolism)
• Humans
• Lectins (chemistry, metabolism)
• Lung (microbiology)
• Macromolecular Substances
• Models, Molecular
• Oligosaccharides (chemistry, metabolism)
• Protein Binding
• Pseudomonas aeruginosa (pathogenicity)