
Principle Investigator:
Prof. Dr. Bernd Meyer, Institute of Organic Chemistry, University of Hamburg
Background:
Fucosylated oligosaccharides play a major role in physiological and pathophysiological processes. Examples of this include the mimicry of bacteria by carbohydrate structures like LeX on the surface of Heliobacter pylori that uses the oligosaccharides to shield itself from attack by the human immune system. Rizobia utilize the fucosylation of Nod factors to yield an efficient nodulation of the roots of plants. Schistosoma mansonii utilizes the core fucosylation to shield itself from recognition by the human immune system.
The biosynthesis all fucosylated oligosaccharides is controlled by a group of enzymes, the fucosyltransferases. It is important to understand in detail the molecular mechanisms of the action of these enzymes and to have selective inhibitors for control of the action of the enzymes in order to selectively control the fucosylation. This knowledge is the basis for new therapeutic interferences. However, in general glycosyltransferases are a group of enzymes for which relatively little experimental data is available. Especially structural information on this class of proteins is scarce.
Homepage of the Meyer Group:
1.03.2012, 17 pm
by Prof. Dr. Gregers Anderson, Aarhus University, Denmark