Profiling and genetic control of the murine immunoglobulin G glycome
| Autor: | Marija Pezer, Quang Nguyen, Gordan Lauc, Kathleen Davern, Irena Trbojević-Akmačić, Mislav Novokmet, Olga O. Zaytseva, Ramesh Ram, Frano Vučković, Grant Morahan, Marija Vilaj, Jasminka Krištić |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Glycan Aging Glycosylation IgG glycosylation Quantitative Trait Loci Immunoglobulin G Acetylglucosamine 03 medical and health sciences chemistry.chemical_compound Mice 0302 clinical medicine Immune system Mice Inbred NOD Polysaccharides Genetic variation Animals Humans Molecular Biology Fucose Genetics biology Laboratory mouse Glycopeptides Genetic Variation Cell Biology Igg glycosylation Glycome carbohydrates (lipids) Mice Inbred C57BL 030104 developmental biology Phenotype chemistry Gene Expression Regulation 030220 oncology & carcinogenesis biology.protein Peptides |
| Zdroj: | NATURE CHEMICAL BIOLOGY Nature Chemical Biology |
| ISSN: | 1552-4450 |
| DOI: | 10.1038/s41589-018-0034-3 |
| Popis: | Immunoglobulin G (IgG) glycosylation is essential for function of the immune system, but the genetic and environmental factors that underlie its inter- individual variability are not well defined. The Collaborative Cross (CC) genetic resource harnesses over 90% of the common genetic variation of the mouse. By analyzing the IgG glycome composition of 95 CC strains, we made several important observations: (i) glycome variation between mouse strains was higher than between individual humans, despite all mice having the same environmental influences ; (ii) five genetic loci were found to be associated with murine IgG glycosylation ; (iii) variants outside traditional glycosylation site motifs affected glycome variation ; (iv) bisecting N- acetylglucosamine (GlcNAc) was produced by several strains although most previous studies have reported the absence of glycans containing the bisecting GlcNAc on murine IgGs ; and (v) common laboratory mouse strains are not optimal animal models for studying effects of glycosylation on IgG function. |
| Databáze: | OpenAIRE |
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