Antibody glycosylation in autoimmune diseases

Xing Zhou, Francesca Motta, Carlo F Selmi, William M. Ridgway, M. Eric Gershwin, Weici Zhang

Research output: Contribution to journalReview articlepeer-review

Abstract

The glycosylation of the fragment crystallizable (Fc) region of immunoglobulins (Ig) is critical for the modulation of antibody effects on inflammation. Moreover, antibody glycosylation may induce pathologic modifications and ultimately contribute to the development of autoimmune diseases. Thanks to progress in the analysis of glycosylation, more data are available on IgG and its subclass structures in the context of autoimmune diseases. In this review, we focused on the impact of Ig glycosylation in autoimmunity, describing how it modulates the immune response and how glycome profiles can be used as biomarkers of disease activity. The analysis of antibody glycosylation demonstrated specific features in human autoimmune and chronic inflammatory conditions, including rheumatoid arthritis, systemic lupus erythematosus, inflammatory bowel disease and autoimmune liver diseases, among others. Within the same disease, different patterns are associated with disease severity and treatment options. Future research may increase the information available on the distinct glycome profiles and expand their potential role as biomarkers and as targets for treatment, ultimately favoring an individualized approach.

Original languageEnglish (US)
Article number102804
JournalAutoimmunity Reviews
Volume20
Issue number5
DOIs
StatePublished - May 2021

Keywords

  • Antibody
  • Autoimmune Diseases
  • Fc fragment
  • Glycosylation
  • Inflammation

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

Fingerprint

Dive into the research topics of 'Antibody glycosylation in autoimmune diseases'. Together they form a unique fingerprint.

Cite this