Fig. 4: WIgGWAM identifies both symmetric and asymmetric IgG1 glycoforms from pooled human plasma and serum derived from human IgG1 knock-in mice.
From: Asymmetrically glycosylated IgG1 antibodies are universal and drive human disease
a, b Deconvoluted intact LC/MS spectrum of a pooled human plasma sample after WIgGWAM (a) treated with EndoS2. The peaks corresponding to the bifucosylated masses of the G1m1 and nG1m1 Fc alleles are labeled (b) with no enzymes added. The dotted lines annotate Fc-linked glycoforms whose peak heights were at least greater than 20% of the maximum peak height for the nG1m1 Fc allele (left) and the G1m1 Fc allele (right). For all intact LC/MS deconvoluted spectra, the highest peak was normalized to 100. c Bar graph showing the relative percentages of symmetric (purple), asymmetric (blue), and ambiguous (orange) glycoforms in pooled human plasma Fcs after WIgGWAM for three technical triplicates. Data are presented as mean values +/- SD. d, e Deconvoluted intact LC/MS spectrum of a serum sample from human IgG1 knock-in mice after WIgGWAM (d) treated with EndoS2. e with no enzymes added. The dotted lines annotate Fc-linked glycoforms whose peak heights were at least greater than 20% of the maximum peak height. f Bar graph showing the relative percentages of symmetric (purple), asymmetric (blue), and ambiguous (orange) glycoforms in hIgG1-KI mouse serum Fcs after WIgGWAM for three technical triplicates. Data are presented as mean values +/− SD. Source data are provided as a Source Data file.
