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Influence of glycosylation on IL-12 family cytokine biogenesis and function.
Mol. Immunol. 126, 120-128 (2020)
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.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Interleukins ; Protein Glycosylation ; Protein Assembly ; Protein Secretion ; Immune Signaling; Cell Stimulatory Factor; Heterodimeric Cytokine; P40 Subunit; P35 Subunit; T-cells; Protein; Il-23; Receptor; Distinct; Form
ISSN (print) / ISBN
0161-5890
e-ISSN
1872-9142
Journal
Molecular Immunology
Quellenangaben
Volume: 126,
Pages: 120-128
Publisher
Elsevier
Publishing Place
The Boulevard, Langford Lane, Kidlington, Oxford Ox5 1gb, England
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute for Allergy Research (IAF)