Fig. 6: Chemoenzymatic glycan remodeling of E. coli-derived hinge-Fc proteins. | Nature Communications

Fig. 6: Chemoenzymatic glycan remodeling of E. coli-derived hinge-Fc proteins.

From: Discovery of a single-subunit oligosaccharyltransferase that enables glycosylation of full-length IgG antibodies in bacteria

Fig. 6

a Schematic representation of the chemoenzymatic reaction for trimming and remodeling hinge-Fc glycans. b Immunoblot analysis of the four E. coli-derived glycoforms (from left to right): aglycosylated hinge-Fc, glycosylated GalNAc5GlcNAc-hinge-Fc, GlcNAc-hinge-Fc, and G2-hinge-Fc. Blot was probed with anti-human IgG (anti-IgG) to detect human Fc. Molecular weight (MW) markers are indicated on the left. The g0, g1, and g2 arrows indicate un-, mono-, and diglycosylated Fc proteins, respectively. Blot is representative of biological replicates (n = 3). c ELISA analysis of same constructs in (b) with FcγRIIIA-V158 as immobilized antigen. Data are average of biological replicates (n = 3) ± SD. Schematics created with BioRender. DeLisa, M. (2025) https://BioRender.com/wesqljn.

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