Fungwall Partner 5

The fungal cell wall as a target for antifungal therapies

Partner 5

Architecture et Fonction des Macromolécules Biologiques
Centre National de la Recherche Scientifique, Délégation Provence,
DR12, Marseille, France.

Principal scientist
Dr B. Henrissat

Other scientists
Prof. P.M. Coutinho - Dr E. Danchin

31, Rue Joseph Aiguier
13402 Marseille Cedex 20
+33-491164516 - fax +33-491164536

Experience of the participating organisation and scientists

Participating organisation

The work will be carried out in the Unit Architecture et Fonction des Macromolécules Biologiques of the CNRS. This partner routinely analyses and assigns to families all carbohydrate-active enzymes released daily by EMBL/GenBank, including from all the newly released genomes from bacterial, archaeal and eukaryotic origin. The data are assembled and made available in the Carbohydrate-Active enzyme database (http://afmb.cnrs-mrs.fr/CAZY/).
A number of automatic routines have already been implemented, allowing processing of ever-expanding data-bases. The Carbohydrate-Active enzyme database currently hosts over 18,000 curated and non-redundant sequences of glycosyltransferase-, glycosidase- and transglycosidase-related proteins. A total of 146 complete genomes have been already processed and analyzed as of Sept 2003. The Carbohydrate-Active enZYme database (that has been created and maintained since 1998) is the only resource dedicated to this category of enzymes available worldwide and has become the reference in the field. Because of its highly specialised nature and the integration of modular and structural data at all stages of the analysis, the Carbohydrate-Active enzyme database out-performs the general databases and general tools for the detection and functional prediction of carbohydrate-active enzymes in genomes. The laboratory has now engaged in the annotation of carbohydrate-active enzymes in several on-going genomes including that of the white-rot fungus Phanerochaete chrysosporium (collaboration with the Joint Genome Institute).

Participating scientists

Dr B. Henrissat is currently a CNRS Directeur de Recherches and heads the laboratory "Architecture et Fonction des Macromolécules Biologiques (AFMB)". Dr Henrissat has over 20 years experience in the field of glycoside hydrolases and glycosyltransferases and he has over 150 refereed publications in this field. Most notably, he proposed the classifications of glycoside hydrolases and glycosyltransferases based on amino acid sequence similarities. These classifications have become the reference of the field, because the families correlate not only with the structure but also with the molecular mechanism of carbohydrate-active enzymes. A large body of genome annotations are already made in reference to the families he has discovered. Together with Prof. P.M. Coutinho, also member of the AFMB laboratory, he maintains the "Carbohydrate-active enzyme" web server CAZy based on these classifications. With the help of a postdoctoral fellow to be recruited within this project, Dr Henrissat and Prof. Coutinho will undertake the bioinformatics part outlined in this proposal.

Relevant publications

Martinez, D., Larrondo, L.F., Putnam, N., Gelpke, M.D., Huang, K., Chapman, J., Helfenbein, K.G., Ramaiya, P., Detter, J.C., Larimer, F., Coutinho, P.M., Henrissat, B., Berka, R., Cullen, D., Rokhsar, D. (2004) Genome sequence of the lignocellulose degrading fungus Phanerochaete chrysosporium strain RP78. Nat Biotechnol. 22:695-700.

Coutinho, P.M., Stam, M., Blanc, E., Henrissat, B. (2003) Why are there so many carbohydrate-active enzyme-related genes in plants ? Trends Plant Sci. 8:563-565.

Coutinho, P.M., Deleury, E., Davies, G.J., Henrissat, B. (2003) An evolving hierarchical family classification for glycosyltransferases. J. Mol. Biol. 328:307-317.

Henrissat, B., Deleury, E., Coutinho, P.M. (2002) Glycogen metabolism loss: a common marker of parasitic behaviour in bacteria ? Trends Genet. 18:437-440.

Henrissat, B., Coutinho, P.M., Davies, G.J. (2001) A census of carbohydrate-active enzymes in the genome of Arabidopsis thaliana. Plant Mol. Biol. 47:55-72.

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