| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 3431131 | Virus Research | 2006 | 4 Pages |
Prion diseases are fatal neurodegenerative disorders in human and animal associated with conformational conversion of a cellular prion protein (PrPC) into the pathologic isoform (PrPSc). Various data indicate that the polymorphisms within the open reading frame (ORF) of PrP are associated with the susceptibility and control the species barrier in prion diseases. In the present study, partial Prnp from 25 Amur tigers (tPrnp) were cloned and screened for polymorphisms. Four single nucleotide polymorphisms (T423C, A501G, C511A, A610G) were found; the C511A and A610G nucleotide substitutions resulted in the amino acid changes Lysine171Glutamine and Alanine204Threoine, respectively. The tPrnp amino acid sequence is similar to house cat (Felis catus AF003087) and sheep, but differs significantly from other two cat Prnp sequences that were previousely deposited in GenBank.
