Molecular model of prion transmission to humans.
To assess interspecies barriers to transmission of transmissible spongiform encephalopathies, we investigated the ability of disease-associated prion proteins (PrPd) to initiate conversion of the human normal cellular form of prion protein of the 3 major PRNP polymorphic variants in vitro. Protein misfolding cyclic amplification showed that conformation of PrPd partly determines host susceptibility.
Jones
Michael
M
National CJD Surveillance Unit, School of Molecular and Clinical Medicine, University of Edinburgh, Western General Hospital, Edinburgh, Scotland EH4 2XU, UK. mjones1@staffmail.ed.ac.uk
Wight
Darren
D
Barron
Rona
R
Jeffrey
Martin
M
Manson
Jean
J
Prowse
Christopher
C
Ironside
James W
JW
Head
Mark W
MW
D000595:Amino Acid Sequence; D000818:Animals; D015153:Blotting, Western; D004198:Disease Susceptibility; D006801:Humans; D051379:Mice; D017096:Prion Diseases / Q000635:transmission*; D011328:Prions / Q000737:chemistry*; D017510:Protein Folding; D020033:Protein Isoforms
D011328:Prions; D020033:Protein Isoforms