Effect of enzymatic deimination on the conformation of recombinant prion protein

Duncan S. Young, Filip Meersman, David Oxley, Judith Webster, Andy Gill, Igor Bronstein, Denise V. Dear

Research output: Contribution to journalArticlepeer-review


Deimination is the post-translational conversion of arginine residues to citrulline. It has been implicated as a causative factor in autoimmune diseases such as multiple sclerosis and rheumatoid arthritis and more recently, as a marker of neurodegeneration. We have investigated the effect of the post-translational modification of arginine residues on the structure of recombinant ovine prion protein. Deiminated prion protein exhibited biophysical properties characteristic of the scrapie-associated conformer of prion protein viz. an increased β-sheet secondary structure, congophilic structures indicative of amyloid and proteinase K resistance which could be templated onto normal unmodified prion protein. In the light of these findings, a potential role of post-translational modifications to prion protein in disease initiation or propagation is discussed.
Original languageEnglish
Pages (from-to)1123-1133
JournalBBA - Proteins and Proteomics
Publication statusPublished - 2009


  • Prion protein
  • Post-translational modification
  • conformational change
  • Deimination
  • Citrulline
  • Arginine modificaiton
  • Amyloid


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