PMID: 8947598Nov 1, 1996Paper

Binding specificities of a polyreactive and a monoreactive human monoclonal IgG rheumatoid factor: role of oligosaccharides

Scandinavian Journal of Immunology
S al-BalaghiE Möller

Abstract

The immunological specificites of two human rheumatoid factor-reactive IgG monoclonal antibodies derived from unstimulated rheumatoid synovial lymphocytes have been analysed. A malaria antigen-reactive IgG monoclonal antibody from an immune donor served as a control. Purified IgG monoclonal antibody from one IgG-RF hybridoma (L1), but not from the other IgG-RF hybridoma (D1) or the anti-malaria monoclonal antibody, exhibited dose-dependent binding to multiple self and non-self antigens such as ds-DNA, cytochrome-c, bovine thyroglobulin, transferrin, cellulose and lipopolysaccharide and therefore was considered polyreactive. The immunological specificity was confirmed by inhibition experiments using the same soluble antigens as inhibitors. The polyreactivity of the IgG-RF MoAb was markedly inhibited by absorption with glycoproteins such as thyroglobulin, a commonly used target for xenoreactive natural antibodies, and cytochrome-c, indicating that the monoclonal antibody is reactive with epitopes expressed on these ligands. Since some naturally occurring antibodies are carbohydrate specific, the authors tested the IgG-RF MoAb for possible carbohydrate specificity. Absorption with certain polysaccharides containing only one or two...Continue Reading

Citations

Jul 1, 1997·Human Immunology·T C RodmanR Winston
Nov 18, 2003·Xenotransplantation·William Parker
Jul 8, 2000·Free Radical Research·L ValgimigliL Bolondi
Sep 28, 2018·Frontiers in Immunology·Elena PipiFrancesca Barone

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