Fig. 6: The capacity of SARS-CoV-2 S-specific IgG1 to bind to Fcγ2B and Fcγ3B receptors is regulated by the Fc-fragment glycosylation pattern. | Nature Immunology

Fig. 6: The capacity of SARS-CoV-2 S-specific IgG1 to bind to Fcγ2B and Fcγ3B receptors is regulated by the Fc-fragment glycosylation pattern.

From: ChAdOx1 nCoV-19 (AZD1222) vaccine-induced Fc receptor binding tracks with differential susceptibility to COVID-19

Fig. 6

a,b, The overall representation (the percentage of total glycans) of major sugar classes, including galactose (agalactose: G0; single galactose: G1; digalactose: G2; fucose (F), sialic acid (S) and a bisecting GlcNAc (B)) across SARS-CoV-2 S-specific low and high FcγR2- and FcγR3B-binding IgG1 (FcγR2B+3B+, FcγR2B+3B, FcγR2B−3B) (a) and total antigen unspecific+, FcγR2B−3B− groups (b) measured by LC–MS. Each bar shows the average of two replicates for FcγR2B+3B+, FcγR2B+3B−, FcγR2B−3B+ and FcγR2B−3B samples (pool of n = 5 per sample). c, PCA applied to all samples and data to examine the impact of various glycoforms on FcγR2B and FcγR3B binding for IgG1.

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