Work

IgG subclass and vaccination stimulus determine changes in antigen specific antibody glycosylation in mice

Year: 2017

Type: article

Abstract: Immunoglobulin G (IgG) glycosylation can modulate antibody effector functions. Depending on the precise composition of the sugar moiety attached to individual IgG glycovariants either pro- or anti-inflammatory effector pathways can be initiated via differential binding to type I or type II Fc-receptors. However, an in depth understanding of how individual IgG subclasses are glycosylated during the steady state and how their glycosylation pattern changes during vaccination is missing. To monitor IgG subclass glycosylation during the steady state and upon vaccination of mice with different T-cell dependent and independent antigens, tryptic digests of serum, and antigen-specific IgG preparations were analyzed by reversed phase-liquid chromatography-mass spectrometry. We show that there is a remarkable difference with respect to how individual IgG subclasses are glycosylated during the steady state. More importantly, upon T-cell dependent and independent vaccinations, individual antigen-specific IgG subclasses reacted differently with respect to changes in individual glycoforms, suggesting that the IgG subclass itself is a major determinant of restricting or allowing alterations in specific IgG glycovariants.

Source: European Journal of Immunology

DOI: 10.1002/eji.201747208

Authors: Daniela Kao, Anja Lux, Anja Schaffert, Roland Lang, Friedrich Altmann, Falk Nimmerjahn

Institutions: Friedrich-Alexander-Universität Erlangen-Nürnberg, Universitätsklinikum Erlangen, BOKU University

Language: English

Topic: Glycosylation and Glycoproteins Research

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: bronze

Funder: Deutsche Forschungsgemeinschaft