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

Nat Struct Biol. 2002 Dec;9(12):918-21. doi: 10.1038/nsb865.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

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


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

Associated data

  • PDB/1GZT