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Research Article Free access | 10.1172/JCI117781
Department of Medicine, University of California, San Diego, La Jolla 92093-0663.
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Department of Medicine, University of California, San Diego, La Jolla 92093-0663.
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Department of Medicine, University of California, San Diego, La Jolla 92093-0663.
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Department of Medicine, University of California, San Diego, La Jolla 92093-0663.
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Department of Medicine, University of California, San Diego, La Jolla 92093-0663.
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Department of Medicine, University of California, San Diego, La Jolla 92093-0663.
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Department of Medicine, University of California, San Diego, La Jolla 92093-0663.
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Published March 1, 1995 - More info
In previous studies of infectious mononucleosis, we found IgM autoantibodies which react with hematopoietic cell antigens. Many of these were inhibited by synthetic glycine/alanine peptides representing the glycine/alanine repeat of Epstein-Barr virus nuclear antigen-1. We have cloned and expressed fragments of genes encoding two of these autoantigens. One gene (p542) encodes a protein containing a glycine-rich 28-mer, which is its chief autoantigenic epitope and which represents a newly identified class of evolutionarily conserved autoepitopes. The other gene (p554) encodes a protein that is not demonstrably cross-reactive with Epstein-Barr virus nuclear antigen-1 or with any other EBV protein, but forms complexes with other proteins. Immunoaffinity-purified anti-p542 and anti-p554 have relatively high binding affinities, as evidenced by inhibition at 10(6)-10(8) M-1, and neither autoantibody showed polyreactivity with other common antigens. The data thus suggest that neither autoantibody is simply an expression of polyclonal B cell activation. We conclude that the two autoantigens stimulate autoantibody synthesis by different mechanisms. One autoantigen shares homology to a viral protein which generates cross-reacting antibodies to the autoantigenic epitope. The other has no recognizable cross-reaction with the infecting pathogen and may become immunogenic through complexing with other proteins.
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