The N-terminal cleavage site of PrPSc from BSE differs from that of PrPSc from scrapie

Hiroko K Hayashi; Takashi Yokoyama; Masuhiro Takata; Yoshifumi Iwamaru; Morikazu Imamura; Yuko K Ushiki; Morikazu Shinagawa

doi:10.1016/j.bbrc.2005.01.065

The N-terminal cleavage site of PrPSc from BSE differs from that of PrPSc from scrapie

Biochem Biophys Res Commun. 2005 Mar 25;328(4):1024-7. doi: 10.1016/j.bbrc.2005.01.065.

Authors

Hiroko K Hayashi¹, Takashi Yokoyama, Masuhiro Takata, Yoshifumi Iwamaru, Morikazu Imamura, Yuko K Ushiki, Morikazu Shinagawa

Affiliation

¹ Prion Disease Research Center, National Institute of Animal Health, 3-1-5 Kannondai, Tsukuba, Ibaraki 305-0856, Japan.

PMID: 15707980
DOI: 10.1016/j.bbrc.2005.01.065

Abstract

Heterogeneity in transmissible spongiform encephalopathy is thought to have derived from conformational variation in an abnormal isoform of the prion protein (PrPSc). To characterize PrPSc in bovine spongiform encephalopathy (BSE) and scrapie, we analyzed the newly generated N-terminus of PrPSc isoforms by digestion with proteinase K (PK). With a lower concentration of PK, the terminal amino acid of BSE PrPSc converged at N96. Under the same conditions, however, the terminal amino acid of scrapie PrPSc was G81 or G85. Furthermore, with an increase of PK concentration, the N-terminal amino acid was shifted and converged at G89. The results suggest that the PK cleavage site of BSE PrPSc is uniform and is different from the cleavage site of scrapie PrPSc.

Publication types

Comparative Study
Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Animals
Binding Sites
Cattle
Encephalopathy, Bovine Spongiform / metabolism*
Molecular Sequence Data
PrPSc Proteins / analysis
PrPSc Proteins / chemistry*
PrPSc Proteins / classification*
Protein Binding
Protein Conformation
Scrapie / metabolism*
Sequence Analysis, Protein / methods*
Sequence Homology, Amino Acid

Substances

PrPSc Proteins