Binding of human IgM from a rheumatoid factor to IgG of 12 animal species |
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| Authors: | Jiharu Hamako Yasuhiro Ozeki Taei Matsui Yoshinobu Yamamoto Takashi Inoue Jun Yukitake Koiti Titani |
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| Institution: | ∗Division of Biomedical Polymer Science, Institute for Comprehensive Medical Science, Fujita Health University, Toyoake, Japan;†Department of Clinical Immunology, Fujita Health University College, Toyoake, Japan;‡Department of Microbiology, School of Health Science, Fujita Health University, Toyoake, Japan;§Research Laboratory of Clinical Medicine, Fujita Health University Hospital, Toyoake, Japan |
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| Abstract: | The binding of IgM from a rheumatoid factor (RF-IgM) to IgG from 12 animal species was analyzed by an ELISA system. The RF-IgM bound various animal IgG with dissimilar affinities. The binding of RF-IgM to animal IgG was inhibited by addition of protein A, which binds some animal IgG by recognizing the junctional site on CH2-CH3 domains in the Fc region. As previously reported, no significant correlation was observed between the binding of RF-IgM to IgG and the content of galactose-free oligosaccharides, which is increased in IgG of rheumatoid arthritis patients or autoimmune mice. We suggest that the crucial epitope of IgG for RF-IgM binding is not the oligosaccharide structure generated specifically in IgG of autoimmune diseases but that RF-IgM may recognize a certain protein conformation of a region in IgG near the binding site of protein A. |
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| Keywords: | Rheumatoid factor IgM IgG Oligosaccharide Asn-linked sugar chain Protein A ELISA Rheumatoid arthritis |
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