Christian Büll
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E-mail: christian.bull[at]ru.nl Phone: +31(0)24 3615063 HG room: 03.026 |
Genetic and chemical engineering of sialoglycoproteins in human cells
Glycosylation is the most diverse post-translational modification of proteins and largely contributes to the staggering diversity of proteoforms found in cells, tissues, and organisms. Human cells assemble chemically diverse sugar molecules into glycans; short, long, linear, and branched chain-like structures. Glycans are attached to the majority of membrane and secreted proteins. They regulate protein folding, and functions and mediate many biological interactions with the immune system and microbiome. Altered protein glycosylation is found in every major disease and contributes to pathological processes in cancer and inflammation. The glycome is assembled by >200 glycosyltransferase enzymes in the ER/Golgi system. However, how these enzymes work together to produce specific glycan structures and how they are regulated is largely unknown. The aim of this project is to use genetic engineering and chemically-modified sugar building blocks to dissect the biosynthetic network of glycosyltransferases. This will enable identification of the binding specificities of glycan-binding proteins in the immune system and microbiome and the production of therapeutic glycoproteins with distinct glycan structures.