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. 2023 Oct 23;14:6693. doi: 10.1038/s41467-023-42572-0

Fig. 1. Glycosylation analysis of murine IgGs during subcutaneous GAS infection.

Fig. 1

Representative time-resolved elution profiles of murine tryptic IgG glycopeptides based on extracted ion chromatograms (XIC) of the N-acetylglucosamine (GlcNAc) oxonium ion m/z 204.09, generated upon glycopeptide fragmentation in (a), uninfected conditions, b 24 h post infection with a wildtype AP1 GAS strain, and (c), 24 h post infection with an isogenic EndoS mutant AP1 strain. Stars denote differential chromatographic peaks compared to uninfected controls. d MS1 precursor intensities of main truncated glycoforms derived from IgG3. e Assigned fragmentation pattern of the precursor m/z 732.83 (2 + ) corresponding to the murine IgG3 peptide backbone modified with one GlcNAc and one fucose (Fuc). f Expected IgG deglycosylation products produced by EndoS enzymatic activity. g Quantification of truncated glycopeptide products in wildtype vs mutant bacterial infections. Relative quantification of the changes in glycosylation patterns of (h) IgG1, (i) IgG2c, (j) IgG3, and (k) IgG2b across infected animals (n = 5–10 animals/ time point) over the time course of the infection. Truncated glycoforms are highlighted with stars. The glycan composition of the most abundant glycoforms are drawn. Source data are provided as a Source Data file.