Altered glycan accessibility on native immunoglobulin G complexes in early rheumatoid arthritis and its changes during therapy

Journal article


Publication Details

Author(s): Stuemer J, Biermann M, Knopf J, Magorivska I, Kastbom A, Svaerd A, Janko C, Bilyy R, Schett G, Sjoewall C, Herrmann M, Munoz LE, Munoz Becerra LE
Journal: Clinical and Experimental Immunology
Publication year: 2017
Volume: 189
Journal issue: 3
Pages range: 372-382
ISSN: 0009-9104


Abstract


The goal of this study was to investigate the glycosylation profile of native immunoglobulin (Ig)G present in serum immune complexes in patients with rheumatoid arthritis (RA). To accomplish this, lectin binding assays, detecting the accessibility of glycans present on IgG-containing immune complexes by biotinylated lectins, were employed. Lectins capturing fucosyl residues (AAL), fucosylated tri-mannose N-glycan core sites (LCA), terminal sialic acid residues (SNA) and O-glycosidically linked galactose/N-acetylgalactosamine (GalNac-L) were used. Patients with recent-onset RA at baseline and after 3-year follow-up were investigated. We found that native IgG was complexed significantly more often with IgM, C1q, C3c and C-reactive protein (CRP) in RA patients, suggesting alterations of the native structure of IgG. The total accessibility of fucose residues on captured immune complexes to the respective lectin was significantly higher in patients with RA. Moreover, fucose accessibility on IgG-containing immune complexes correlated positively with the levels of antibodies to cyclic citrullinated peptides (anti-CCP). We also observed a significantly higher accessibility to sialic acid residues and galactose/GalNAc glyco-epitopes in native complexed IgG of patients with RA at baseline. While sialic acid accessibility increased during treatment, the accessibility of galactose/GalNAc decreased. Hence, successful treatment of RA was associated with an increase in the SNA/GalNAc-L ratio. Interestingly, the SNA/GalNAc-L ratio in particular rises after glucocorticoid treatment. In summary, this study shows the exposure of glycans in native complexed IgG of patients with early RA, revealing particular glycosylation patterns and its changes following pharmaceutical treatment.



FAU Authors / FAU Editors

Biermann, Mona
Lehrstuhl für Biochemie und Molekulare Medizin
Herrmann, Martin Prof. Dr.
Medizinische Klinik 3 - Rheumatologie und Immunologie
Janko, Christina Dr. rer. nat.
Einrichtungen, die zum Universitätsklinikum Erlangen gehören
Knopf, Jasmin
Medizinische Klinik 3 - Rheumatologie und Immunologie
Munoz Becerra, Luis Enrique Dr.
Medizinische Klinik 3 - Rheumatologie und Immunologie
Schett, Georg Prof. Dr. med.
Lehrstuhl für Innere Medizin III


External institutions with authors

Falu Hospital / Falu lasarett
Linköping University


How to cite

APA:
Stuemer, J., Biermann, M., Knopf, J., Magorivska, I., Kastbom, A., Svaerd, A.,... Munoz Becerra, L.E. (2017). Altered glycan accessibility on native immunoglobulin G complexes in early rheumatoid arthritis and its changes during therapy. Clinical and Experimental Immunology, 189(3), 372-382. https://dx.doi.org/10.1111/cei.12987

MLA:
Stuemer, J., et al. "Altered glycan accessibility on native immunoglobulin G complexes in early rheumatoid arthritis and its changes during therapy." Clinical and Experimental Immunology 189.3 (2017): 372-382.

BibTeX: 

Last updated on 2018-08-10 at 03:13