许晓东等 《Nature Communications》 2019

作者: 来源: 发布日期:2019-03-05 浏览次数:

  论文题目:A viral expression factor behaves as a prion

  论文作者: Hao Nan, Hongying Chen, Mick F. Tuite & Xiaodong Xu

  论文摘要:Prions are proteins that can fold into multiple conformations some of which are self-propagating. Such prion-forming proteins have been found in animal, plant, fungal and bacterial species, but have not yet been identified in viruses. Here we report that LEF-10, a baculovirus-encoded protein, behaves as a prion. Full-length LEF-10 or its candidate prion-forming domain (cPrD) can functionally replace the PrD of Sup35, a widely studied prion-forming protein from yeast, displaying a [PSI+]-like phenotype. Furthermore, we observe that high multiplicity of infection can induce the conversion of LEF-10 into an aggregated state in virus-infected cells, resulting in the inhibition of viral late gene expression. Our findings extend the knowledge of current prion proteins from cellular organisms to non-cellular life forms and provide evidence to support the hypothesis that prion-forming proteins are a widespread phenomenon in nature.

  论文链接:https://www.nature.com/articles/s41467-018-08180-z

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