INVITRO EXPRESSION IN EUKARYOTIC CELLS OF A PRION PROTEIN GENE CLONED FROM SCRAPIE-INFECTED MOUSE-BRAIN
INVITRO EXPRESSION IN EUKARYOTIC CELLS OF A PRION PROTEIN GENE CLONED FROM SCRAPIE-INFECTED MOUSE-BRAIN
复制标题
DOI：
10.1073/pnas.85.13.4657
复制
发表时间：
1988-07-01
影响因子：
11.1
通讯作者：
CHESEBRO, B
中科院分区：
文献类型：
--
作者：
CAUGHEY, B;RACE, RE;CHESEBRO, B
有人提出，瘙痒病的病原体是一类缺乏核酸的感染性颗粒，内源性朊病毒蛋白（PrP）的一种改变是病原体。然而，很难排除从痒病组织中纯化的PrP可能被更传统的病毒剂污染的可能性。为了获得未被瘙痒病感染组织污染的PrP，我们在小鼠C127细胞中体外表达了从瘙痒病感染小鼠脑中克隆的PrP cDNA。鉴定了克隆的PrP基因所编码的mRNA和蛋白。表达的PrP多肽似乎被糖基化并从细胞表面释放到培养基中。将表达克隆PrP基因的细胞匀浆接种于易感小鼠，但未引起瘙痒的临床症状。因此，要么PrP不是瘙痒病的传播因子，要么表达的PrP需要额外的修饰才能具有传染性。
It has been proposed that the causative agent of scrapie represents a class of infectious particle that is devoid of nucleic acid and that an altered from of the endogenous prion protein (PrP) is the agent. However, it has been difficult to exclude the possibility that PrP purified from scrapie tissues might be contaminated with a more conventional viral agent. To obtain PrP uncontaminated by scrapie-infected tissues, PrP cDNA cloned from a scrapie-infected mouse brain was expressed in mouse C127 cells in vitro. mRNA and protein encoded by the cloned PrP gene were identified. The expressed PrP polypeptides appeared to be glycosylated and were released from the cell surface into the medium. Homogenates of the cells expressing the cloned PrP gene were inoculated into susceptible mice but failed to induce clinical signs of scrapie. Thus, either PrP is not the transmissible agent of scrapie or the expressed PrP requires additional modification to be infectious.