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Updated: Apr 26, 2026
Author Spotlight: Dendritic Cells Maturation Using Sialidases-Based Enzymatic Treatment of the Cell Surface
Published on: October 20, 2023
Diversity in structure and functions of antibody sialylation in the Fc
T Shantha Raju1, Steven E Lang1
1Biologics Research, Biotechnology Center of Excellence, Janssen Research & Development, L.L.C., 1400 Welsh Road, Spring House, PA 19477, USA.
Abstract:
Terminal sialic acid residues of glycoconjugates exhibit remarkable functional and structural diversity. They affect biological activity, serum half-life and structural stability of glycoproteins. Alternatively, they act as mediators for pathogens to invade host systems. These surface exposed N-glycans are easily accessible for interactions with receptors, enzymes, etc. In contrast, Fc N-glycans of IgGs are sequestered within the two CH2 domains and exhibit high degree of heterogeneity. They are required for antibody effector functions including binding to C1q protein. Biological significance of Fc glycans has been extensively studied and importance of terminal galactose, bisecting GlcNAc and core fucose has been realized. This review focuses on the recent advances in structure and functions of terminal sialic acid residues of Fc glycans.
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