The role of glucose metabolism and O-GlcNAc glycosylation in the regulation of immunity

Lead Researcher Email Number Webpage
Dr Nishma Gupta | Professor Jose Villadangos +61 3 903 57684 (JV) View page

Project Details

localisation of o-GlcNAC proteins in dendritic cells

Localisation of O-GlcNAC proteins in Dendritic cells: CD8+ splenic DCs were stained for O-GlcNAc proteins (green), the nucleus (blue) and other cellular compartments (red).

OGlcNAc glycosylation involves addition of a single sugar, β-N-acetylglucosamine, to serine or threonine residues of proteins. It is a unique type of glycosylation found on nuclear and cytoplasmic proteins. The addition and removal of OGlcNAc is catalysed by OGlcNAc transferase (OGT) and OGlcNAse (OGA) respectively. It is a rapidly reversibly modification akin to phosphorylation. Indeed, OGlcNAc glycosylation occurs in dynamic interplay with phosphorylation, either on the same or adjacent residues. The cross-talk between these two modifications in turn regulates various cellular processes. We are characterising the function of OGlcNAc glycosylation in immune cells by identifying changes in patterns of glycosylation in different metabolic states and upon encounter of pathogens. The function of glycosylated proteins will be further studied to understand the relevance of their OGlcNAc status in various immune cell activities.


Dr Nishma Gupta

Professor Jose Villadangos


Professor Malcolm McConville (University of Melbourne)

Dr Justine Mintern (University of Melbourne)