Brainwide silencing of prion protein by AAV-mediated delivery of an engineered compact epigenetic editor

Science. 2024 Jun 28;384(6703):ado7082. doi: 10.1126/science.ado7082. Epub 2024 Jun 28.

Abstract

Prion disease is caused by misfolding of the prion protein (PrP) into pathogenic self-propagating conformations, leading to rapid-onset dementia and death. However, elimination of endogenous PrP halts prion disease progression. In this study, we describe Coupled Histone tail for Autoinhibition Release of Methyltransferase (CHARM), a compact, enzyme-free epigenetic editor capable of silencing transcription through programmable DNA methylation. Using a histone H3 tail-Dnmt3l fusion, CHARM recruits and activates endogenous DNA methyltransferases, thereby reducing transgene size and cytotoxicity. When delivered to the mouse brain by systemic injection of adeno-associated virus (AAV), Prnp-targeted CHARM ablates PrP expression across the brain. Furthermore, we have temporally limited editor expression by implementing a kinetically tuned self-silencing approach. CHARM potentially represents a broadly applicable strategy to suppress pathogenic proteins, including those implicated in other neurodegenerative diseases.

MeSH terms

  • Animals
  • Brain* / metabolism
  • DNA (Cytosine-5-)-Methyltransferases / genetics
  • DNA (Cytosine-5-)-Methyltransferases / metabolism
  • DNA Methylation*
  • Dependovirus* / genetics
  • Gene Silencing*
  • Histones* / metabolism
  • Humans
  • Mice
  • Prion Diseases / genetics
  • Prion Diseases / metabolism
  • Prion Proteins* / genetics
  • Prion Proteins* / metabolism
  • Transgenes

Substances

  • DNA (Cytosine-5-)-Methyltransferases
  • Histones
  • Prion Proteins