Mm. Newkirk et J. Rauch, BINDING OF HUMAN MONOCLONAL IGG RHEUMATOID FACTORS TO FC IS INFLUENCED BY CARBOHYDRATE, Journal of rheumatology, 20(5), 1993, pp. 776-780
Objective. The precise nature of the epitope on the Fc portion of the
IgG molecule to which IgG rheumatoid factors (RF) bind has not been id
entified. As patients with rheumatoid arthritis (RA) have abnormal gly
cosylation of the Fc portion of IgG, we investigated the impact of the
sugar present in the Fc on the binding of IgG RF. Methods. Binding of
monoclonal IgG RF to Fc fragments with varying oligosaccharide chains
was detected using an immunoblot assay. Results. We demonstrated that
the binding of human hybridoma derived monoclonal IgG RF was strongly
influenced by the presence of carbohydrate and was maximal when the c
arbohydrate molecule was intact. The RF did not bind directly to the c
arbohydrate moiety itself. Conclusion. This suggests that conformation
al changes in the polypeptide chain induced by the carbohydrate are re
sponsible for the observed binding patterns.