Glycosylation is a non-template driven enzymatic process in which all the complex glycan structures found in and on a cell is produced. More than 200 glycosyltransferase enzymes are found in man and these orchestrate the synthesis of enormous diversity in glycan structures on proteins and lipids. We explore the function of these glycosyltransferases and their glycan products by precise gene editing strategies where we knockout individual transferases in cells and use the resulting isogenic cell models to explore and dissect the biology.

We have developed the SimpleCell strategy in which glycosylation is genetically simplified in cells to enable efficient enrichment of defined glycoproteins and characterization of glycoproteomes by nLC-MS/MS mass spectrometry.

Additionally, we apply glycoengineering to host cells which are used for production of recombinant glycoprotein therapeutics. This way, we are able to custom design glycosylation of glycoprotein drugs, such as antibodies, coagulation factors and enzymes for replacement therapy, in order to improve efficacy and develop new designer drugs.


  • To discover new O-glycoproteomes and expand the knowledge about O-glycoproteins and specific glycosites
  • To identify and dissect roles of glycogenes in common conditions and diseases implicated by GWAS signals
  • To test druggability of glycosyltransferases and improve glycoprotein drugs