Theranostics 2021; 11(11):5430-5446. doi:10.7150/thno.53961 This issue Cite
Review
1. Department of Dermatology, Union Hospital, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, China.
2. Hubei Engineering Research Center for Skin Repair and Theranostics, Wuhan, China.
3. Britton Chance Center for Biomedical Photonics at Wuhan National Laboratory for Optoelectronics-Hubei Bioinformatics & Molecular Imaging Key Laboratory, Systems Biology Theme, Department of Biomedical Engineering, College of Life Science and Technology, Huazhong University of Science and Technology, Wuhan, China.
4. Department of Dermatology, The Central Hospital of Wuhan, Tongji Medical College, Huazhong University of Science and Technology (HUST), Wuhan, China.
*These authors contributed equally to this work.
Human immunoglobulin G (IgG), especially autoantibodies, has major implications for the diagnosis and management of a wide range of autoimmune diseases. However, some healthy individuals also have autoantibodies, while a portion of patients with autoimmune diseases test negative for serologic autoantibodies. Recent advances in glycomics have shown that IgG Fc N-glycosylations are more reliable diagnostic and monitoring biomarkers than total IgG autoantibodies in a wide variety of autoimmune diseases. Furthermore, these N-glycosylations of IgG Fc, particularly sialylation, have been reported to exert significant anti-inflammatory effects by upregulating inhibitory FcγRIIb on effector macrophages and reducing the affinity of IgG for either complement protein or activating Fc gamma receptors. Therefore, sialylated IgG is a potential therapeutic strategy for attenuating pathogenic autoimmunity. IgG sialylation-based therapies for autoimmune diseases generated through genetic, metabolic or chemoenzymatic modifications have made some advances in both preclinical studies and clinical trials.
Keywords: sialylation, immunoglobulin G, glycosylation, autoimmune diseases, precision medicine