NR AGVC
AU Kretzschmar,H.A.; Neumann,M.; Riethmüller,G.; Prusiner,S.B.
TI Molecular cloning of a mink prion protein gene
QU Journal of General Virology 1992 Oct; 73(10): 2757-61
IA http://vir.sgmjournals.org/cgi/reprint/73/10/2757
PT journal article
AB 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.
IN Von einer genomischen DNA-Sequenz wurde die 257 Aminosäuren lange Sequenz eine Nerzprionproteins abgeleitet. Die Homologie zu anderen Säugerprionproteinen soll zwischen 84 und 90% liegen.
MH Amino Acid Sequence; Animal; Base Sequence; Brain Chemistry; Cloning, Molecular; Mink/*microbiology; Molecular Sequence Data; PrPsc Proteins; Prions/*genetics; RNA/isolation & purification; Sequence Homology, Amino Acid; Species Specificity; Support, Non-U.S. Gov't
AD Institute of Neuropathology, University of Munich, Germany.
SP englisch
PO England
OR Prion-Krankheiten 5