title: Effect of enzymatic deimination on the conformation of recombinant prion protein.
abstract: 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 beta-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.
authors.affiliation: Institute of Biotechnology, University of Cambridge, Tennis Court Road, Cambridge, UK.
authors.forename: Duncan S
authors.initials: DS
authors.lastname: Young
authors.forename: Filip
authors.initials: F
authors.lastname: Meersman
authors.forename: David
authors.initials: D
authors.lastname: Oxley
authors.forename: Judith
authors.initials: J
authors.lastname: Webster
authors.forename: Andrew C
authors.initials: AC
authors.lastname: Gill
authors.forename: Igor
authors.initials: I
authors.lastname: Bronstein
authors.forename: Christopher R
authors.initials: CR
authors.lastname: Lowe
authors.forename: Denise V
authors.initials: DV
authors.lastname: Dear