Structural basis of high-affinity glycan recognition by bacterial and fungal lectins.
The structural diversity of bacterial and fungal lectins has been highlighted during the past few years. Some of the new structures reproduce folds previously observed in plants or mammals, but many constitute new folds that have never been observed before, either at all or not with a lectin function, testifying to the increasing diversity. The novelty of the new structures is greater at the level of the sugar-binding sites, with some bacterial lectins displaying unusually high affinity for oligosaccharides and even monosaccharides. Analysis of the thermodynamic contributions to the energy of binding gives clues to the strategies used by bacteria to recognise and attach to their host.
Imberty
Anne
A
CERMAV-CNRS (affiliated with Université Joseph Fourier), Grenoble BP53, F-38041 Grenoble cedex 09, France. anne.imberty@cermav.cnrs.fr
Mitchell
Edward P
EP
Wimmerová
Michaela
M
D000595:Amino Acid Sequence; D001419:Bacteria / Q000737:chemistry*; D001665:Binding Sites; D005658:Fungi / Q000737:chemistry*; D037102:Lectins / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009005:Monosaccharides / Q000737:chemistry; D011134:Polysaccharides / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D013816:Thermodynamics
D037102:Lectins; D009005:Monosaccharides; D011134:Polysaccharides