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Theme 2 colloquium by dr. Marthe Walvoort (RUG): 'Studying the mechanism of bacterial protein glycosyltransferases' (Lecture)

Tuesday 11 February 2020Add to my calendar
from 16:00
dr. Marthe Walvoort (RUG)

Marthe WalvoortProtein glycosylation is an abundant post-translational modification. While it has long been assumed to be specific to eukaryotes, it is now well established that also bacteria produce glycoproteins. Interestingly, in bacterial glycoproteins, there is a lot more structural variation of both the glycan and the linkage to the protein. The glycans of bacterial glycoproteins have been associated with virulence [1], and therefore may present a novel target for antibiotic strategies.

Recently, we linked the extracellular adhesin glycoproteins from Haemophilus influenzae to the etiology of multiple sclerosis [2]. The adhesins display a large number of glucose residues b-linked to asparagine (N-Glc), which is an unusual protein modification restricted to certain bacteria. Sera from MS patients contained significantly higher levels of antibodies against adhesin epitopes that displayed multiple N-Glc residues, compared to normal blood donors.

Multiply glycosylated proteins are rare, with the best-known example being the eukaryotic O-GlcNAc modification, which is dynamic and has been compared to phosphorylation. Recent studies suggest that the O-GlcNAc transferase operates through a distributive mechanism [3][4]. In this lecture, I will outline the variety of experiments from our lab that suggests that bacterial N-Glc transferase (NGT) harbors processive characteristics.

[1]          Kelly, J. et al. Journal of Bacteriology 2006, 188, 2427.
[2]          Walvoort, M.T.C. et al. Scientific Reports 2016, 6, 39430.
[3]          Lu, L. et al. Biochemistry 2016, 55, 1149.
[4]          Yakovlieva, L.; Walvoort, M.T.C. ACS Chemical Biology 2020, 15, 3.

dr. Evan Spruijt/ dr. Peter Korevaar