Journal
NATURE MEDICINE
Volume 13, Issue 2, Pages 211-217Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nm1488
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Funding
- NIAID NIH HHS [P01 AI045757, P01 AI039671, P01AI39671] Funding Source: Medline
- NIDDK NIH HHS [U01DK6192601] Funding Source: Medline
- NINDS NIH HHS [R01 NS024247, R01NS2424710, P01 NS038037, P01NS38037] Funding Source: Medline
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The role of autoantibodies in the pathogenesis of multiple sclerosis (MS) and other demyelinating diseases is controversial, in part because widely used western blotting and ELISA methods either do not permit the detection of conformation-sensitive antibodies or do not distinguish them from conformation-independent antibodies. We developed a sensitive assay based on self-assembling radiolabeled tetramers that allows discrimination of antibodies against folded or denatured myelin oligodendrocyte glycoprotein (MOG) by selective unfolding of the antigen domain. The tetramer radioimmunoassay (RIA) was more sensitive for MOG autoantibody detection than other methodologies, including monomer-based RIA, ELISA or fluorescent-activated cell sorting (FACS). Autoantibodies from individuals with acute disseminated encephalomyelitis (ADEM) selectively bound the folded MOG tetramer, whereas sera from mice with experimental autoimmune encephalomyelitis induced with MOG peptide immunoprecipitated only the unfolded tetramer. MOG-specific autoantibodies were identified in a subset of ADEM but only rarely in adult-onset MS cases, indicating that MOG is a more prominent target antigen in ADEM than MS.
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