FLYGLYGAN
Systematic Isolation of Glycosyltransferases in Drosophila melanogaster Using The Toxicity of Fungal Lectins
| Coordinatore | EIDGENOESSISCHE TECHNISCHE HOCHSCHULE ZURICH
Organization address
address: Raemistrasse 101 contact info |
| Nazionalità Coordinatore | Switzerland [CH] |
| Totale costo | 256˙364 € |
| EC contributo | 256˙364 € |
| Programma | FP7-PEOPLE
Specific programme "People" implementing the Seventh Framework Programme of the European Community for research, technological development and demonstration activities (2007 to 2013) |
| Code Call | FP7-PEOPLE-2011-IIF |
| Funding Scheme | MC-IIF |
| Anno di inizio | 2012 |
| Periodo (anno-mese-giorno) | 2012-03-01 - 2014-02-28 |
Partecipanti
| # | ||||
|---|---|---|---|---|
| 1 |
EIDGENOESSISCHE TECHNISCHE HOCHSCHULE ZURICH
Organization address
address: Raemistrasse 101 contact info |
CH (ZUERICH) | coordinator | 256˙364.20 |
Mappa
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Obiettivo del progetto (Objective)
'Glycosyltransferases catalyze the transfer of a sugar from a glycosyl donor to an acceptor substrate and though this action are responsible for the synthesis of the vast array of glycan modifications found in nature. Identifying genes that encode proteins with glycosyltransferase activity and determining the glycan structures generated by a specific glycosyltransferase is challenging. This project exploits the toxicity associated with the glycan-binding function of fungal lectins to systematically isolate genes that encode glycosyltransferases and link enzymes with the glycan structures they generate. This study will be carried out using the genetic model insect Drosophila melanogaster where abundant genetic resources make the systematic screening of genes possible and existing knowledge of the glycome indicates the existence of uncharacterized, novel glycosyltransferases. The findings produced from this study will broaden our understanding of glycosyltransferases and glycan structures. This has applications for chemical and medical technologies based on bioactive glycans and glycoconjugant biosynthesis. It is also an essential step towards the delineation of glycan biosynthetic pathways in a whole animal system and will pave the way for further studies that link specific glycan structures to biological functions. The study also lays vital groundwork for the biotechnological application of lectins as effective insecticides.'
Introduzione (Teaser)
In nature, many biological molecules such as proteins and lipids become modified through the addition of a sugar (glycan) molecule. A European study investigated the association between the enzymes that catalyse this addition with the presence of carbohydrate-binding proteins known as lectins.