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Three-dimensional conformation of the epitopes of human superoxide dismutase-2 recognized by antibody against HIV-1p17.

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We have previously reported that antibodies against HIV-1p17 protein cross-react with human superoxide dismutase-2 (SOD-2). To identify and characterize the epitopes of human SOD-2 recognized by anti-HIV-1p17 antibody, we synthesized several peptide fragments of human SOD-2 and found that the antibody did not bind to the LQPALK hexapeptide which is contained in both HIV-1p17 and human SOD-2. Instead, this antibody bound to four peptides which contain amino acid sequences similar, but not identical, to the known epitopes of HIV-1p17. These peptides have two features in three-dimensional (3-D) conformation: two protruded carbohydrate side chains on the peptide chain or a concave structure in the molecule. It is suggested that the antibody does not strictly recognize the amino acid sequence itself, but may recognize these 3-D conformations.
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Document Type: Research Article

Affiliations: Third Department of Internal Medicine, Yamagata University School of Medicine, Yamagata 990-23, Japan.

Publication date: January 1, 1998

More about this publication?
  • The International Journal of Molecular Medicine is a monthly, peer-reviewed journal devoted to the publication of high quality studies related to the molecular mechanisms of human disease. The journal welcomes research on all aspects of molecular and clinical research, ranging from biochemistry to immunology, pathology, genetics, human genomics, microbiology, molecular pathogenesis, molecular cardiology, molecular surgery and molecular psychology.

    The International Journal of Molecular Medicine aims to provide an insight for researchers within the community in regard to developing molecular tools and identifying molecular targets for the diagnosis and treatment of a diverse number of human diseases.
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