Molecular cloning of a mink prion protein gene.
Transmissible mink encephalopathy (TME) is a rare disease which is presumably transmitted to ranch-raised mink from scrapie-infected sheep offal or bovine spongiform encephalopathy-infected cattle products. Although the infectious agent of TME has not been isolated, there is circumstantial evidence that TME is caused by prions. The experimental host range of TME includes sheep, cattle, monkeys and hamsters. However, TME has never been transmitted to mice. Since experiments in transgenic animals have shown that the prion protein (PrP) gene modulates the susceptibility, incubation time and neuropathology of prion-induced disease, we have started to analyse the mink PrP gene. PrP, as deduced from a genomic DNA sequence, consists of 257 amino acids and overall shows similarity of 84 to 90% with the sequences of the PrPs of other mammalian species. It remains to be determined whether these differences in the primary structure of PrP will explain the peculiar host range of TME.
Kretzschmar
H A
HA
Institute of Neuropathology, University of Munich, Germany.
Neumann
M
M
Riethmüller
G
G
Prusiner
S B
SB
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001923:Brain Chemistry; D003001:Cloning, Molecular; D008907:Mink / Q000382:microbiology*; D008969:Molecular Sequence Data; D018620:PrPSc Proteins; D011328:Prions / Q000235:genetics*; D012313:RNA / Q000302:isolation & purification; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity
D018620:PrPSc Proteins; D011328:Prions; D012313:RNA