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A viral expression factor behaves as a prion

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  • Hao Nan

    (Northwest A&F University)

  • Hongying Chen

    (Northwest A&F University)

  • Mick F. Tuite

    (University of Kent)

  • Xiaodong Xu

    (Northwest A&F University)

Abstract

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.

Suggested Citation

  • Hao Nan & Hongying Chen & Mick F. Tuite & Xiaodong Xu, 2019. "A viral expression factor behaves as a prion," Nature Communications, Nature, vol. 10(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-018-08180-z
    DOI: 10.1038/s41467-018-08180-z
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