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Influence of glycosylation on IL-12 family cytokine biogenesis and function

Sina Bohnacker1, Karen Hildenbrand2, Isabel Aschenbrenner2

  • 1Department of Chemistry and Institute for Advanced Study, Technical University of Munich, 85748, Garching, Germany; Center of Allergy & Environment (ZAUM), Technical University of Munich and Helmholtz Zentrum München, 80802, Munich, Germany.

Molecular Immunology
|August 22, 2020
PubMed

The interleukin 12 (IL-12) family of cytokines regulates T cell functions and is key for the orchestration of immune responses. Each heterodimeric IL-12 family member is a glycoprotein. However, the impact of glycosylation on biogenesis and function of the different family members has remained incompletely defined. Here, we identify glycosylation sites within human IL-12 family subunits that become modified upon secretion. Building on these insights, we show that glycosylation is dispensable for secretion of human IL-12 family cytokines except for IL-35. Furthermore, our data show that glycosylation differentially influences IL-12 family cytokine functionality, with IL-27 being most strongly affected. Taken together, our study provides a comprehensive analysis of how glycosylation affects biogenesis and function of a key human cytokine family and provides the basis for selectively modulating their secretion via targeting glycosylation.

Keywords:
immune signalinginterleukinsprotein assemblyprotein glycosylationprotein secretion

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