Abstract
In autoimmune disorders such as rheumatoid arthritis and systemic lupus erythematosus (SLE), autoantibodies are generated against a variety of macromolecules. Myositis is a human autoimmune disease characterized by weakness and wasting of muscle1. In American studies2,3, antibodies directed against soluble cellular constituents were detected by immunodiffusion in about 60% of cases; the commonest of these, found in 25% of patients, was antibody to the Jo-1 antigen. An antibody system referred to as PL-1 was recognized at a similar frequency in a series of patients studied at Hammersmith Hospital, London4. We show here that this system is identical with the Jo-1 system and demonstrate that the antigen is a polypeptide of molecular weight (Mr) 50,000. The protein is immunoprecipitated with tRNAHis and appears to be histidyl-tRNA synthetase. The identity of the Jo-1 antigen, the first of the RNA-associated antigens familiar in autoimmune disease5,6 to be characterized as a specific enzyme, suggests a model for virus involvement in autoantibody generation.
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Mathews, M., Bernstein, R. Myositis autoantibody inhibits histidyl-tRNA synthetase: a model for autoimmunity. Nature 304, 177–179 (1983). https://doi.org/10.1038/304177a0
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DOI: https://doi.org/10.1038/304177a0
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