Selected Publication


Network inference from glycoproteomics data reveals new reactions in the IgG glycosylation pathway

Literature-based Immunoglobulin G glycan synthesis pathway

Glycosylation is a post-translational modification that covalently binds chains of monosaccharides, called glycans, to proteins and lipids. The structure of the bound sugar molecule can have a huge impact on the tridimensional structure of the protein, and highly affect its functionality. One example of this effect is Immunoglobulin G, the most abundant antibody and glycoprotein in human blood: while some glycans enhance the pro-inflammatory function of the protein, others promote immuno-suppression. Given the impact of glycans on protein activity, it is important to understand how these molecules are synthesized and regulated at a molecular level. In collaboration with several experimental groups across the world (Croatia, USA, Finland, Russia), scientists at the Institute of Computational Biology developed a data-driven network-based inference approach to predict previously unknown glycosylation reactions from large scale IgG glycomics mass spectrometry measurements. The statistically determined hypotheses were subsequently validated with targeted experiments. The results of the study have now been published in Nature Communications.

For more information, see the  press release by the Helmholtz Zentrum  München and the original publication: Benedetti, E. et al. (2017). Network inference from glycoproteomics data reveals new reactions in the IgG glycosylation pathway. Nature Communications, 8. doi:10.1038/s41467-017-01525-0

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