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

Sabin C, Mitchell EP, Pokorná M, Gautier C, Utille JP, Wimmerová M, Imberty A

CERMAV-CNRS (affiliated with Université Joseph Fourier), 601 rue de la Chimie, Grenoble BP53, F-38041 Grenoble cedex 09, France.

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.

Published 31 January 2006 in FEBS Lett, 580(3): 982-7.
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