engleski

IgG N-glycosylation in three mouse strains analyzed with nanoUPLC-ESI-MS and CGE-LIF

N-glycosylation of immunoglobulin G (IgG) is important for its biological functions. Biantennary N-glycans attached to the heavy chains of the fragment crystallizable (Fc) moiety of the IgG molecule influence its stability and effector functions. Additionally, around 15-20% of IgG molecules carry biantennary N-glycans in the antigen-binding (Fab) fragment, potentially affecting its interaction with the antigen. Changes in the IgG N-glycosylation profile are observed in many autoimmune diseases. Mouse models are often used to study the role of IgG N-glycosylation in immunology. However, detailed studies of the mouse IgG N-glycome lag behind those of the human glycome. The aim of this study is to evaluate the biological variation of IgG N-glycans between three commonly used mouse strains. IgG was isolated from the serum of individual sex- and aged-matched mice of BALB/c, C57BL/6 and C3H strains kept in the same environment. The obtained IgG N-glycans were analysed by the capillary gel electrophoresis with laser-induced fluorescence (CGE-LIF) method, which characterizes both Fc and Fab N-glycans, and by the nano ultra-performance liquid chromatography coupled with mass spectrometer (nanoUPLC-ESI-MS) method, which provides information on subclass- specific N-glycosylation of the Fc region. We compared several derived N-glycan traits, describing the relative abundance of N-glycan structural features. We observed differences in the IgG N-glycome of the 3 strains with both methods. The profiles of the Fc-linked and the total IgG N- glycomes are different even within one strain and so are the subclass-specific profiles. These results suggest that there is a strong genetic component defining IgG N-glycosylation and that it might work in a subclass-specific manner.

IgG glycosylation ; mouse ; nanoUPLC-ESI-MS ; CGE-LIF

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