Manganese superoxide dismutase as a target of autoantibodies in acute Epstein-Barr virus infection

Antibodies directed against the autoantigen p26 were detected in sera from 32 patients with acute Epstein-Barr virus (EBV) infection and clinical symptoms of infectious mononucleosis. P26 has now been identified as the enzyme manganese superoxide dismutase (MnSOD) by comparison of the NH2-terminal a...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1994
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Articles
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2191756/
https://www.ncbi.nlm.nih.gov/pubmed/7964476
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description Antibodies directed against the autoantigen p26 were detected in sera from 32 patients with acute Epstein-Barr virus (EBV) infection and clinical symptoms of infectious mononucleosis. P26 has now been identified as the enzyme manganese superoxide dismutase (MnSOD) by comparison of the NH2-terminal amino acid sequence. Antibodies against MnSOD belong to the immunoglobulin class M. They are not detectable in sera of patients with other herpesvirus infections. In the 32 patients investigated, the rise and fall of the autoantibodies coincides with the clinical symptoms. In vitro, the autoantibodies were shown to inhibit the dismutation of superoxide radicals by blocking MnSOD. As presented in the discussion this effect may contribute to the pathogenesis of acute EBV infection.
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spelling pubmed-21917562008-04-16 Manganese superoxide dismutase as a target of autoantibodies in acute Epstein-Barr virus infection J Exp Med Articles Antibodies directed against the autoantigen p26 were detected in sera from 32 patients with acute Epstein-Barr virus (EBV) infection and clinical symptoms of infectious mononucleosis. P26 has now been identified as the enzyme manganese superoxide dismutase (MnSOD) by comparison of the NH2-terminal amino acid sequence. Antibodies against MnSOD belong to the immunoglobulin class M. They are not detectable in sera of patients with other herpesvirus infections. In the 32 patients investigated, the rise and fall of the autoantibodies coincides with the clinical symptoms. In vitro, the autoantibodies were shown to inhibit the dismutation of superoxide radicals by blocking MnSOD. As presented in the discussion this effect may contribute to the pathogenesis of acute EBV infection. The Rockefeller University Press 1994-11-01 /pmc/articles/PMC2191756/ /pubmed/7964476 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
Manganese superoxide dismutase as a target of autoantibodies in acute Epstein-Barr virus infection
title Manganese superoxide dismutase as a target of autoantibodies in acute Epstein-Barr virus infection
title_full Manganese superoxide dismutase as a target of autoantibodies in acute Epstein-Barr virus infection
title_fullStr Manganese superoxide dismutase as a target of autoantibodies in acute Epstein-Barr virus infection
title_full_unstemmed Manganese superoxide dismutase as a target of autoantibodies in acute Epstein-Barr virus infection
title_short Manganese superoxide dismutase as a target of autoantibodies in acute Epstein-Barr virus infection
title_sort manganese superoxide dismutase as a target of autoantibodies in acute epstein-barr virus infection
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2191756/
https://www.ncbi.nlm.nih.gov/pubmed/7964476

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