Autoimmunity and Chronic Inflammation

Autoimmunity and Chronic Inflammation

CD BioGlyco has many state-of-the-art technology platforms including Glyco™ Synthesis Platform, Glycoproteomics Platform, Glycobiology Microarray Platform, Glycoengineering Platform, and Glycosylation Site-specific Antibody-Drug Conjugate (ADC) Development Platform. These platforms are conducive to studying autoimmunity and chronic inflammation to help our clients' projects.

Overview of Autoimmunity and Chronic Inflammation

The immune system normally recognizes and responds to foreign carbohydrate epitopes, such as lipopolysaccharides. However, loss of tolerance and autoimmunity may also occur, for example, if the glycosylation patterns of the host and pathogen overlap, possibly due to abnormal enzymatic activity. Changes in protein glycosylation patterns can also lead to the immunodetection of these neo-glycan epitopes and result in autoimmunity. In addition, the IgG effector function is controlled by N-glycosylation. Altered sialylation, galactosylation, and/or fucosylation, as well as changes in glycan composition, can lead to immune dysregulation and a range of autoimmune and chronic inflammatory diseases.

Immunoregulation pathways of antibody glycosylation in autoimmune diseases.Fig.1 Immunoregulation pathways of antibody glycosylation in autoimmune diseases. (Zhou, et al, 2021)

Antibody Glycosylation and Inflammation in Autoimmune Diseases

Antibodies play a key role in the humoral adaptive immune response by binding to specific antigens and linking them to the innate immune system. The ability of antibodies to harness this immunity is attributed to their unique structure and has been successfully applied in the treatment of many disease types, including autoimmune and inflammatory diseases

In recent years, the glycosylation level of IgG or other antibodies in human serum has become more and more clear by various means. In normal human serum, although IgG is regularly classified into different subgroups, the glycosylation of total IgG is usually quite constant. In addition, compared with healthy controls, different glycosylation patterns of total IgG were also observed in patients with various autoimmune diseases, including rheumatoid arthritis, systemic lupus erythematosus, inflammatory bowel disease, primary Sjogren's syndrome, ankylosing spondylitis, psoriatic arthritis, and multiple sclerosis. In patients with all these diseases, compared with healthy controls, the N- glycan of serum IgG lacks terminal galactose.

CD BioGlyco is willing to be the partner of customers in glycoscience. We provide comprehensive services including but not limited to Custom Glycosylation of Antibodies, Custom Glycosylation of Proteins, and Characterization of Glycosylation in Antibody Drugs. For further details, please don't hesitate to contact us.


  1. Zhou, X.; et al. Antibody glycosylation in autoimmune diseases. Autoimmunity Reviews. 2021, 20(5): 102804.
This service is for Research Use Only, not intended for any clinical use.

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