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Type 1 and type 2 human PrP^Sc have different aggregation sizes in methionine homozygotes with sporadic, iatrogenic and variant Creutzfeldt–Jakob disease

¹ Division of CJD Science and Technology, Department of Prion Research, Center for Translational and Advanced Animal Research on Human Diseases, Tohoku University Graduate School of Medicine, 2-1 Seiryo-machi, Aoba-ku, Sendai 980-8575, Japan
² Planova Division, Asahi Kasei Pharma Corporation, Tokyo, Japan
³ National Creutzfeldt–Jakob Disease Surveillance Unit, Division of Pathology, University of Edinburgh, Western General Hospital, Edinburgh, UK
⁴ Laboratory of Biomedicine, Center of Biomedical Research, Graduate School of Medical Sciences, Kyusyu University, Fukuoka, Japan

Correspondence
Tetsuyuki Kitamoto
kitamoto{at}mail.tains.tohoku.ac.jp

In Creutzfeldt–Jakob disease (CJD), the type (type 1 or 2) of abnormal isoform of the prion protein (PrP^Sc) in the brain and the genotype at codon 129 of the PrP gene are major determinants of clinicopathological phenotype. Little is known about the difference in biochemical properties between the two types of PrP^Sc, except for the different proteinase K cleavage sites. To investigate the size of aggregates formed by PrP^Sc types 1 and 2, brain homogenates from various cases of CJD with the same genotype (homozygous for methionine at codon 129) were passed through filters with a mean pore size of 72±4 nm. Type 2 PrP^Sc was efficiently removed from the filtrates by the filters, in contrast to type 1. Even type 2 PrP^Sc from a patient without amyloid plaques was removed more efficiently than type 1 from patients with amyloid plaques. These results indicate that type 2 PrP^Sc has a larger aggregation size than type 1, irrespective of the existence of amyloid plaques.