Résumé:
Lectins are ubiquitous, polyvalent and non immune origin which bind specifically and reversibly to carbohydrates. They are often multivalent and have the well-known ability to agglutinate erythrocytes.
Fungi, including microscopic fungi and yeasts, have been the subject of considerable interest in recent years because of their potential biomedical and biotechnological applications. The information on fungal lectins, especially the structural point of view, are minimal compared to those of their plant and animal counterparts. It is in this context that lies our purpose was realized by the biochemical and structural characterization of fungal lectin Terfezia boudieri ( Algerian Sahara Truffle) on which we previously had no such data.
Two lectins: TrFBL1 and TrFBL2 were extracted, purified, characterized and sequened. The structures of 3D TrFBL1 native protein and its complex with a ligand, fucoside sélénométhyl were obtained and are being refined .The structures of TrFBL2 complexes with N-acetylglucosamine and two other glycans were obtained at high resolution.
The Genome of Terfezia boudieri was obtained and is available from the month of December 2013 and will become part of the database collected Lectin 3D (http://lectin3d.cermav.cnrs.fr).
