Lawrence Steinman

Publication Details

  • A POLYALANINE PEPTIDE WITH ONLY 5 NATIVE MYELIN BASIC-PROTEIN RESIDUES INDUCES AUTOIMMUNE ENCEPHALOMYELITIS JOURNAL OF EXPERIMENTAL MEDICINE Gautam, A. M., Pearson, C. I., Smilek, D. E., Steinman, L., McDevitt, H. O. 1992; 176 (2): 605-609

    Abstract:

    The minimum structural requirements for peptide interactions with major histocompatibility complex (MHC) class II molecules and with T cell receptors (TCRs) were examined. In this report we show that substituting alanines at all but five amino acids in the myelin basic protein (MBP) peptide Ac1-11 does not alter its ability to bind A alpha uA beta u (MHC class II molecules), to stimulate specific T cells and, surprisingly, to induce experimental autoimmune encephalomyelitis (EAE) in (PL/J x SJL/J)F1 mice. Most other amino acid side chains in the Ac1-11 peptide are essentially irrelevant for T cell stimulation and for disease induction. Further analysis revealed that binding to A alpha uA beta u occurred with a peptide that consists mainly of alanines and only three of the original residues of Ac1-11. Moreover, when used as a coimmunogen with MBP Ac1-11, this peptide inhibited EAE. The finding that a specific in vivo response can be generated by a peptide containing only five native residues provides evidence that disease-inducing TCRs recognize only a very short sequence of the MHC-bound peptide.

    View details for Web of Science ID A1992JF80300031

    View details for PubMedID 1380066

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