Abstract
Abstract The family of IgG Abs is a crucial component of adaptive immunity. Glycosylation of IgG maintains its structural integrity and modulates its effector functions. In this review, we discuss IgG glycosylation covering cell biological as well as therapeutic and disease-related aspects, focusing on the glycan structures in distinct IgG regions (Fab versus Fc). We also cover the impact of IgG glycosylation on disease modulation and therapeutic outcomes, alongside the potential for development of vaccines designed to induce Ag-specific IgG with glycoforms for optimal immune responses. Overall, we emphasize the significance of studying glycosylation to enhance our understanding of the dynamics and functional impacts of IgG glycosylation. These insights could be beneficial for advancing future research and clinical applications.
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