Changes of serum IgG glycosylation patterns in rheumatoid arthritis

Abstract

Abstract Objective RA is a prevalent systemic autoimmune disease, whose diagnosis is based significantly on autoantibody detection. This study aims to investigate the glycosylation profile of serum IgG in RA patients using high-throughput lectin microarray technology. Method Lectin microarray containing 56 lectins was applied to detect and analyze the expression profile of serum IgG glycosylation in 214 RA patients, 150 disease controls (DC), and 100 healthy controls (HC). Significant differential glycan profiles between the groups of RA and DC/HC as well as RA subgroups were explored and verified by lectin blot technique. The predicted models were created to evaluate the feasibility of those candidate biomarkers. Results As a comprehensive analysis of lectin microarray and lectin blotting, results showed that compare to HC and DC groups, serum IgG from RA patients had a higher affinity to the SBA lectin (recognizing glycan GalNAc). For RA subgroups, RA-seropositive group had higher affinities to the lectins of MNA-M (recognizing glycan mannose) and AAL (recognizing glycan fucose), and RA-ILD group had higher affinities to the lections of ConA (recognizing glycan mannose) and MNA-M while a lower affinity to the PHA-E (recognizing glycan Galβ4GlcNAc) lectin. The predicted models indicated corresponding feasibility of those biomarkers. Conclusion Lectin microarray is an effective and reliable technique for analyzing glycan structure. RA, RA-seropositive, and RA-ILD patients exhibit distinct glycan profiles, respectively. Altered levels of glycosylation may be related to the pathogenesis of the disease, which could provide a direction for new biomarkers identification.