Faculty of Biotechnology and Drug Development, University of Rijeka, Rijeka, Croatia.
Division of Genetics, Department of Biology, Friedrich Alexander University Erlangen-Nuremberg, Erlangen, Germany.
J Immunol. 2024 Dec 1;213(11):1573-1584. doi: 10.4049/jimmunol.2400447.
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.
IgG 抗体家族是适应性免疫的重要组成部分。IgG 的糖基化维持其结构完整性并调节其效应功能。在这篇综述中，我们讨论了 IgG 糖基化，涵盖了细胞生物学以及治疗和疾病相关方面，重点介绍了不同 IgG 区域（Fab 与 Fc）中的聚糖结构。我们还讨论了 IgG 糖基化对疾病调节和治疗结果的影响，以及开发旨在诱导具有最佳免疫反应的糖型的抗原特异性 IgG 的疫苗的潜力。总的来说，我们强调了研究糖基化的重要性，以增强我们对 IgG 糖基化动力学和功能影响的理解。这些见解可能有助于推进未来的研究和临床应用。
