Mechanisms of action of therapeutic amyloidogenic hexapeptides in amelioration of inflammatory brain disease

J Exp Med. 2014 Aug 25;211(9):1847-56. doi: 10.1084/jem.20140107. Epub 2014 Jul 29.

Abstract

Amyloid fibrils composed of peptides as short as six amino acids are effective therapeutics for experimental autoimmune encephalomyelitis (EAE). Immunosuppression arises from at least two pathways: (1) expression of type 1 IFN by pDCs, which were induced by neutrophil extracellular traps arising from the endocytosis of the fibrils; and (2) the reduced expression of IFN-γ, TNF, and IL-6. The two independent pathways stimulated by the fibrils can act in concert to be immunosuppressive in Th1 indications, or in opposition, resulting in inflammation when Th17 T lymphocytes are predominant. The generation of type 1 IFN can be minimized by using polar, nonionizable, amyloidogenic peptides, which are effective in both Th1 and Th17 polarized EAE.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adoptive Transfer
  • Adult
  • Amyloid / immunology*
  • Amyloid / therapeutic use*
  • Animals
  • Encephalomyelitis, Autoimmune, Experimental / genetics
  • Encephalomyelitis, Autoimmune, Experimental / immunology*
  • Encephalomyelitis, Autoimmune, Experimental / therapy*
  • Female
  • Gene Expression
  • Humans
  • Immunosuppressive Agents / therapeutic use
  • Interferon Type I / metabolism
  • Interferon-gamma / metabolism
  • Interleukin-6 / metabolism
  • Mice
  • Mice, Inbred C57BL
  • Mice, Knockout
  • Peptide Fragments / immunology*
  • Peptide Fragments / therapeutic use*
  • Th1 Cells / immunology
  • Th17 Cells / immunology
  • Tumor Necrosis Factor-alpha / metabolism
  • tau Proteins / immunology
  • tau Proteins / therapeutic use

Substances

  • Amyloid
  • Immunosuppressive Agents
  • Interferon Type I
  • Interleukin-6
  • Peptide Fragments
  • Tumor Necrosis Factor-alpha
  • tau Proteins
  • Interferon-gamma