Wu Changde, Pang Wanyong, Zhao Deming
National Animal Transmissible Spongiform Encephalopathy Laboratory, College of Veterinary Medicine, China Agricultural University, Beijing 100094, China.
Virus Res. 2006 Oct;121(1):93-6. doi: 10.1016/j.virusres.2006.05.001. Epub 2006 Jun 15.
Prion diseases are fatal neurodegenerative disorders in human and animal associated with conformational conversion of a cellular prion protein (PrP(C)) into the pathologic isoform (PrP(Sc)). 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 ) and sheep, but differs significantly from other two cat Prnp sequences that were previously deposited in GenBank.
朊病毒疾病是人和动物中致命的神经退行性疾病，与细胞朊蛋白（PrP(C)）构象转变为病理性异构体（PrP(Sc)）有关。各种数据表明，PrP开放阅读框（ORF）内的多态性与朊病毒疾病的易感性相关，并控制物种屏障。在本研究中，克隆了25只东北虎的部分Prnp（tPrnp）并筛选多态性。发现了四个单核苷酸多态性（T423C、A501G、C511A、A610G）；C511A和A610G核苷酸替换分别导致氨基酸变化赖氨酸171谷氨酰胺和丙氨酸204苏氨酸。tPrnp氨基酸序列与家猫（Felis catus）和绵羊相似，但与先前存入GenBank的其他两个猫Prnp序列有显著差异。
