Chemical precision tools for N-linked glycans of viruses, microalgae and archea

Protein N-glycosylation, or the attachment of oligo- and polysaccharides at specific asparagine residues, is conserved throughout life, and is now observed even in the viral world.

In contrast to eukaryotes, whose well-studied N-glycosylation machineries are relatively simple, archaea, microalgae and bacteria utilize a wide variety of monosaccharides to create a wealth of structurally diverse N-glycans, and the same holds true for some recently discovered viruses.

Because protein glycosylation occurs far downstream of protein synthesis the complexity and diversity in N-glycan structures are poorly understood in detail. This holds true not only for animal cells, but also for N-glycosylation events in other organisms such as viruses.

In this project, we will employ tools and methodologies to unravel the effect of viral glycosylation machineries to the host cell.