Epitope mapping of human aromatic L-amino acid decarboxylase

Biochem Biophys Res Commun. 2007 Feb 16;353(3):692-8. doi: 10.1016/j.bbrc.2006.12.080. Epub 2006 Dec 22.

Abstract

Autoimmune polyendocrine syndrome type I (APS I) is a rare hereditary condition considered a model disease for organ specific autoimmunity. A wide range of autoantibodies targeting antigens present in the affected organs have been identified. Autoantibodies against aromatic L-amino acid decarboxylase (AADC) are present in about 50% of APS I patients. In order to increase our understanding of autoantibody specificity in APS I, the aim of the present study was to localize target regions on AADC recognized by sera from APS I patients. Using several complementing strategies, we have shown that autoantibodies against AADC mainly recognize conformational epitopes. The major antigenic determinants were detected N-terminally to amino acid residue 237. Replacement of amino acids 227-230 (ERDK) with alanine residues reduced the reactivity towards AADC by >80% in all patient sera tested, suggesting that amino acids 227-230 are an important part of an immunodominant epitope.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aromatic-L-Amino-Acid Decarboxylases / genetics
  • Aromatic-L-Amino-Acid Decarboxylases / immunology*
  • Autoantibodies
  • Carboxy-Lyases / genetics
  • Carboxy-Lyases / immunology
  • Epitope Mapping / methods*
  • Humans
  • Models, Molecular
  • Mutagenesis, Site-Directed
  • Polyendocrinopathies, Autoimmune / enzymology
  • Polyendocrinopathies, Autoimmune / immunology
  • Recombinant Fusion Proteins / immunology

Substances

  • Autoantibodies
  • Recombinant Fusion Proteins
  • Carboxy-Lyases
  • Aromatic-L-Amino-Acid Decarboxylases
  • sulfoalanine decarboxylase