NR AJWU
AU Raymond,G.J.; Bossers,A.; Raymond,L.D.; O'Rourke,K.I.; McHolland,L.E.; Bryant,P.K.3rd; Miller,M.W.; Williams,E.S.; Smits,M.; Caughey,B.W.
TI Evidence of a molecular barrier limiting susceptibility of humans, cattle and sheep to chronic wasting disease
QU EMBO Journal 2000 Sep 1; 19(17): 4425-30
IA http://www.cwd.cc/Evidence%20of%20a%20molecular%20barrier%20limiting.pdf
PT journal article
AB Chronic wasting disease (CWD) is a transmissible spongiform encephalopathy (TSE) of deer and elk, and little is known about its transmissibility to other species. An important factor controlling interspecies TSE susceptibility is prion protein (PrP) homology between the source and recipient species/genotypes. Furthermore, the efficiency with which the protease-resistant PrP (PrPres) of one species induces the in vitro conversion of the normal PrP (PrP-sen) of another species to the protease-resistant state correlates with the cross-species transmissibility of TSE agents. Here we show that the CWD-associated PrPres (PrP(CWD)) of cervids readily induces the conversion of recombinant cervid PrP-sen molecules to the protease-resistant state in accordance with the known transmissibility of CWD between cervids. In contrast, PrP(CWD)-induced conversions of human and bovine PrP-sen were much less efficient, and conversion of ovine PrP-sen was intermediate. These results demonstrate a barrier at the molecular level that should limit the susceptibility of these non-cervid species to CWD.
MH Amino Acid Sequence; Animal; Base Sequence; Cattle; Cloning, Molecular; DNA Primers; *Genetic Predisposition to Disease; Human; Molecular Sequence Data; Prion Diseases/*genetics; Prions/chemistry/genetics; Sequence Homology, Amino Acid; Sheep; Species Specificity
AD NIAID/NIH Rocky Mountain Laboratories, Hamilton, MT 59840,USA.
SP englisch
PO England
EA pdf-Datei und HTML-Version