RESUMO
Prion diseases are a group of human and animal neurodegenerative conditions, which are caused by the deposition of an abnormal isoform prion protein (PrPSc) encoded by a single copy prion protein gene (Prnp). In sheep, genetic variations of Prnp were found to be associated with the incubation period, susceptibility, and species barrier to the scrapie disease. We investigated the sequence and polymorphisms of the prion protein gene of Mongolian gazelles (gPrnp). gPrnp gene sequence analysis of blood samples from 26 Mongolian gazelles showed high identity within species. The gPrnp gene was closely related to the Prnp genes of Thomson's gazelle, blackbuck, and cattle with 100, 100, and 98.5% identity, respectively, whereas the gPrnp gene with a deletion was closely related to the Prnp genes of wildebeest, Western roe deer, and sheep with 99.3, 99.3, and 98.9% identity, respectively. Polymorphisms of the open reading frame of Prnp as amino acid substitutions were detected at codons 119(N --> S), 143(S --> G) or 160(Y --> H), 172(V --> A), 182(N --> S) and 221(V --> A). There was also deletion of one octapeptide repeat at the N-terminal octapeptide repeat region. The polymorphisms of gPrnp will assist the study of prion disease pathogenesis, resistance, and cross species transmission.
