Inhibition of self-binding antibodies (autobodies) by a V H-derived peptide

Academic Article


  • The self-binding properties of a dominant idiotypic antibody (T15) and a minor idiotypic antibody (M603), both specific for phosphorylcholine, were examined as models of self-binding antibodies (autobodies). Observed differences in the self-binding affinity of T15 and M603 relate to variable sequence differences in their respective heavy and light chains. A molecular recognition theory based on the translation of coding and noncoding DNA strands was used to identify complementary amino acid sequences responsible for self-binding. The second hypervariable region of the heavy chain domain, extending into the third framework region, was predicted as the primary self-binding locus. Among peptides synthesized with different variable heavy and light chain regions, a 24-residue peptide spanning the second hypervariable and third framework regions of the heavy chain of T15 was nearly as effective as phosphorylcholine in inhibiting the self-binding complexes.
  • Authors

    Published In

  • Science  Journal
  • Digital Object Identifier (doi)

    Author List

  • Kang CY; Brunck TK; Kieber-Emmons T; Blalock JE; Kohler H
  • Start Page

  • 1034
  • End Page

  • 1036
  • Volume

  • 240
  • Issue

  • 4855