1.58 rheumatoid factor binding is influenced by the N-Glycans of their IGG targets

摘要: Background and Objectives In autoimmune conditions, like rheumatoid arthritis (RA), the own immune system attacks body causes inflammation. One of consequences inflammation during diseases is a changed glycosylation profile IgG antibodies. RA not only characterised by an altered N-glycan structure bound to Fc portion molecules but also circulating factors (RF) that recognizes as antigen. The aim our work was investigate complexes in blood patients with seropositive seronegative RA. Material Methods Sera from 70 (RF positive n = 43 RF negative 27) 8 healthy donors (control) have been used analysis. (I) Random serum IgG-complexes were captured F(ab’) 2 fragments anti-human-IgG analysed ELISA for their interaction anti-human-IgG, anti-human-IgM, AAL lectin (fucose-specific) LCA (manose-specific). (II) eluted ELISA-plates Western Blots presence IgG, IgM well binding. (III) affinity purified AAL-, SNA- jacalin-agarose columns tested target factor. Results accessibility fucose residues much higher when compared donors. This reactivity independent IgM-RF. mannose be observed Blot confirmed increased fucosylation did differ between all groups. No difference detected IgM-RF towards fractions AAL- SNA-reactive IgG. However, displayed reduced binding minor fraction isolated jacalin-affinity chromatography. Conclusion not-denatured glycan shows lower fucose-specific lectin, contrast, due complexed discriminate reactive SNA lectin. – Aleuria aurantia (α-1,6 core fucose) Lens culimaris agglutinin (α-mannose) - Sambucus nigra (α-2,6-sialic acid)