The binding of lupus-derived autoantibodies to the C-terminal peptide (83-119) of the major SmD1 autoantigen can be mediated by double-stranded DNA and nucleosomes.
until further notice
SourceAnnals of the Rheumatic Diseases, 65, 11, (2006), pp. 1525-8
Article / Letter to editor
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Annals of the Rheumatic Diseases
SubjectIGMD 9: Renal disorder; N4i 4: Auto-immunity, transplantation and immunotherapy; NCMLS 1: Infection and autoimmunity; NCMLS 3: Tissue engineering and pathology; UMCN 5.4: Renal disorders
OBJECTIVES: To evaluate the binding of lupus-derived autoantibodies, double-stranded DNA and nucleosomes to the positively charged C-terminal SmD1(residues 83-119) peptide and the full-length SmD protein. METHODS: The binding of lupus-derived monoclonal antibodies, sera from patients with systemic lupus erythematosus, rheumatoid arthritis and systemic sclerosis, dsDNA and nucleosomes to the SmD1(83-119) peptide or the full-length SmD protein was determined using different ELISA methods. RESULTS: Monoclonal anti-dsDNA antibodies and the serum of patients with systemic lupus erythematosus that are positive for anti-dsDNA antibodies react with the SmD1(83-119) peptide in ELISA. However, DNaseI treatment of the blocking reagents leads to a decreased reactivity. Purified dsDNA and nucleosomes bind to the SmD1 peptide but not to the full-length SmD protein. CONCLUSIONS: The SmD1(83-119) peptide is able to bind dsDNA and nucleosomes, and dsDNA or nucleosomes in applied reagents lead to an apparent reactivity of anti-dsDNA, anti-histone or nucleosome-specific antibodies with the SmD1(83-119) peptide in ELISA.
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