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Glycosylation in three mouse strains analysed by xCGE-LIF

Glycosylation is an important co- and posttranslational protein modification regarding protein function, stability, clearence and is essential for multicellular life. Knowledge about mouse IgG glycome is lagging behind human IgG glycome even though mouse is the most widely used animal model for in vivo experiments. There is even less information about differences in glycosylation between mouse strains. The aim of this study is to evaluate biological variation between commonly used mouse strains in terms of IgG N-glycome. IgG was isolated from serum of individual sex- and aged-matched mice of BALB/c, C57BL/6 and C3H strains kept in the same environment. Obtained IgG N-glycans from each mouse sample were analysed by xCGE-LIF. GlyXtool software with built-in N-glycan database was used for data analysis, allowing structural assigment for most glycan peaks. To address biological variation we calculated and compared seven different derived traits in each strain.

glycosylation ; immunoglobulin G ; mouse ; capillary gel electrophoresis

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