Binding of different monosaccharides by lectin PA-IIL from Pseudomonas aeruginosa: thermodynamics data correlated with X-ray structures

FEBS Lett. 2006 Feb 6;580(3):982-7. doi: 10.1016/j.febslet.2006.01.030. Epub 2006 Jan 19.


The lectin from Pseudomonas aeruginosa (PA-IIL) is involved in host recognition and biofilm formation. Lectin not only displays an unusually high affinity for fucose but also binds to L-fucose, L-galactose and D-arabinose that differ only by the group at position 5 of the sugar ring. Isothermal calorimetry experiments provided precise determination of affinity for the three methyl-glycosides and revealed a large enthalpy contribution. The crystal structures of the complexes of PA-IIL with L-galactose and Met-beta-D-arabinoside have been determined and compared with the PA-IIL/fucose complex described previously. A combination of the structures and thermodynamics provided clues for the role of the hydrophobic group in affinity.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adhesins, Bacterial / chemistry*
  • Adhesins, Bacterial / metabolism
  • Binding Sites / physiology
  • Biofilms / growth & development
  • Lectins / chemistry*
  • Lectins / metabolism
  • Monosaccharides / chemistry*
  • Monosaccharides / metabolism
  • Protein Binding / physiology
  • Protein Structure, Tertiary
  • Pseudomonas aeruginosa / chemistry*
  • Pseudomonas aeruginosa / physiology
  • Thermodynamics


  • Adhesins, Bacterial
  • Lectins
  • Monosaccharides
  • adhesin, Pseudomonas