Versatile Biosensor Deciphering Glycoenzymatic Activities

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Programme Social programme Plenary speakers Keynote speakers 1st EuroCarb Young Researcher (ECYR) Workshop CarboMet Workshop Mini symposium: Glycobiology at the LUMC and beyond Favourites/Agenda

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1st EuroCarb Young Researcher (ECYR) Workshop

CarboMet Workshop

Mini symposium: Glycobiology at the LUMC and beyond

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Versatile Biosensor Deciphering Glycoenzymatic Activities

Daniel Marquez-Martin 1 , Christine Saint-Pierre 2 , Aurelie Bouchet-Spinelli 4 , Olivier Lerouxel 3 , Didier Gasparutto 2

1 Grenoble Alpes University-Glyco@Alps, Grenoble, France, 2 Atomic Energy and Alternative Energies Commission (CEA), Grenoble, France, 3 Vegetal Macromolecules Research Centre (CERMAV), SAINT MARTIN D´HERES, France, 4 Molecular SYstems and nanoMaterials for Energy and Health (SYMMES), Grenoble, France

To date, glycosyltransferases (GTs) are an essential family of enzymes poorly characterize both structurally and mechanistically which is being a major bottleneck in Glycoscience. They play a crucial role in living organisms catalysing the stereo- and regiospecific transfer of an activate donor sugar to an acceptor moiety to build up complex oligosaccharides onto the cell surface [1]. It requires the development of new methodologies able to elucidate and characterize the interactions between the glycosyl moiety and the enzyme. Surface plasmon resonance imaging (SPRi) has spread as a powerful analytical tool for deciphering many biomolecular processes exploring the kinetics and monitoring multiple interactions of biological and chemical substrates at real time and without any labels [2]. We aim at the development of a biosensor enable to rationalize the characterization of glycosyltransferases activities involved in the plant cell wall biosynthesis. To this aim, a fucosyltransferase from the plant Arabidosis thaliana (AtFUT1) (CAZY family GT37), was selected as model glycosyltransferase. This enzyme participates in the last step in the biosynthesis of xyloglucan (XG) transferring L-Fucose molecule from GDP-Fucose (donor) to a galactose sugar (acceptor) [3]. To that end, multiple chemical strategies to functionalize large moieties of xyloglucan to graft it on the gold surface have been developed [4] [5]. Depicting and monitoring the interactions between the AtFUT1 and the xyloglucan in terms of both specificity and activity represent a strong challenge. Complementary techniques such as isothermal titration calorimetry (iTC) may guide to streamline the comprehension and support the rationalization of the glycosylation process [6].

Albesa-Jové, D; Guerin, M. Current Opinion in Structural Biology. 2016, 40, 23-32.

Bosch, M; Sánchez, A.J; Rojas, F; Ojeda, C. Sensors. 2007, 7, 797-859.

Cicéron, F; Rocha, J; Kousar, S; Hansen, S; Chazalet, V; Gillon, E; Breton, C; Lerouxel, O. Biochimie. 2016, 128-129, 183-192.

Mallevre, F; Roget, A; Minon, T; Kervella, Y; Ropartz, D; Ralet, M.C; Canut, H; Livache, T. Bioconjugate Chem. 2013, 24, 1264-1269.

Thakar, D; Migliorini, E; Coche-Guerente, L; Sadir, R; Lortat-Jacob, H; Boturyn, D; Renaudet, O; Labbe, P and Richter, R. Chem Commun. 2014, 50, 15148.

Mazzei, L; Ciurli, S; Zambelli, B. Journal of Visualized Experiments. 2014, 86, 1-8.

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