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A viral expression factor behaves as a prion

Nan, Hao, Chen, Hongying, Tuite, Mick F, Xu, Xiaodong (2019) A viral expression factor behaves as a prion. Nature Communications, 10 (1). p. 359. ISSN 2041-1723. (doi:10.1038/s41467-018-08180-z) (KAR id:71784)

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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.

Item Type: Article
DOI/Identification number: 10.1038/s41467-018-08180-z
Subjects: Q Science > QR Microbiology
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: Mick Tuite
Date Deposited: 23 Jan 2019 12:52 UTC
Last Modified: 30 May 2019 08:46 UTC
Resource URI: (The current URI for this page, for reference purposes)
Tuite, Mick F:
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