Bartz Jason C
Department of Medical Microbiology and Immunology, School of Medicine, Creighton University, Omaha, Nebraska 68178.
Cold Spring Harb Perspect Med. 2016 Dec 1;6(12):a024349. doi: 10.1101/cshperspect.a024349.
Prion diseases affect a wide range of mammal species and are caused by a misfolded self-propagating isoform (PrP) of the normal prion protein (PrP). Distinct strains of prions exist and are operationally defined by differences in a heritable phenotype under controlled experimental transmission conditions. Prion strains can differ in incubation period, clinical signs of disease, tissue tropism, and host range. The mechanism by which a protein-only pathogen can encode strain diversity is only beginning to be understood. The prevailing hypothesis is that prion strain diversity is encoded by strain-specific conformations of PrP; however, strain-specific cellular cofactors have been identified in vitro that may also contribute to prion strain diversity. Although much progress has been made on understanding the etiological agent of prion disease, the relationship between the strain-specific properties of PrP and the resulting phenotype of disease in animals is poorly understood.
朊病毒疾病影响多种哺乳动物物种，由正常朊病毒蛋白（PrP）的错误折叠、自我传播异构体（PrP）引起。存在不同的朊病毒毒株，在受控的实验性传播条件下，根据可遗传表型的差异对其进行操作性定义。朊病毒毒株在潜伏期、疾病临床症状、组织嗜性和宿主范围方面可能有所不同。仅由蛋白质构成的病原体编码毒株多样性的机制才刚刚开始被理解。普遍的假说是，朊病毒毒株多样性由PrP的毒株特异性构象编码；然而，已在体外鉴定出可能也有助于朊病毒毒株多样性的毒株特异性细胞辅助因子。尽管在理解朊病毒疾病的病原体方面已取得很大进展，但PrP的毒株特异性特性与动物疾病最终表型之间的关系仍知之甚少。
