Key result
A defined SmD-like epitope consisting of Gly-Arg repeats is recognized by 35% of sera from patients with SLE and other autoimmune diseases, and cross-reacts with EBNA1 protein.
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Two mouse cDNA clones were isolated by immunoscreening with an SLE serum. These clones encode an epitope which consists of a di-peptide repeat (Gly-Arg)n (n = 9 and 19 in isolated clones). These sequences, when expressed as fusion proteins, inhibit the binding of antibodies from one patient's serum to the SmD autoantigen. This cross-reactivity is based on the sequence identity with the carboxyterminal end of the human SmD [(Gly-Arg)g]. An Exonuclease III deletion analysis demonstrates that the minimal number of Gly-Arg repeats necessary for immune recognition on the Western blot is patient-specific, and varies from nine to three. The defined epitope is recognized by 35% of sera from patients with SLE as well as with other autoimmune diseases (rheumatoid arthritis, scleroderma, Sjogren's syndrome), in contrast to SLE-specificity of anti-Sm antibodies. Affinity-purified antibodies of the identified epitope cross-react with EBNA1 protein in EBV-infected B-cell lines.
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Rivkin et al. (1994) studied Systemic Lupus Erythematosus (SLE) and other autoimmune diseases. SmD-like epitope (Gly-Arg repeats) was evaluated on Immune recognition and cross-reactivity. A defined SmD-like epitope consisting of Gly-Arg repeats is recognized by 35% of sera from patients with SLE and other autoimmune diseases, and cross-reacts with EBNA1 protein.
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