Fig. 8: Monofucosylated IgG binds to FcγRIIIA in a high-affinity orientation.
From: Asymmetrically glycosylated IgG1 antibodies are universal and drive human disease
a Crystal structure of bifucosylated Fc with FcγRIIIA (PDB: 5XJE)57. The N-glycans are depicted as spheres with the Fc N297 core fucoses colored in red. Distances between E269 of chain A of the Fc and K131 of FcγRIIIA and E269 of chain B of the Fc and K114 of the receptor are highlighted. b Diagram depicting the potential binding orientations of bifucosylated, afucosylated, and monofucosylated IgGs to FcγRIIIA, shown as a gray oval. Surface plasmon resonance (SPR) sensograms of c bifucosylated A330W E269I KiH Rituximab IgG1, d afucosylated A330W E269I KiH Rituximab IgG1, e monofucosylated A330W E269I KiH Rituximab IgG1, f bifucosylated A330W E269M KiH Rituximab IgG1, g afucosylated A330W E269M KiH Rituximab IgG1, and h monofucosylated A330W E269M KiH Rituximab IgG1 binding to FcγRIIIA-F158. Created in BioRender. D, J. (2025) https://BioRender.com/2vqcv7e Source data are provided as a Source Data file.
