A viral expression factor behaves as a prion

Hao Nan, Hongying Chen, Mick F. Tuite and Xiaodong Xu ()
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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

Nature Communications, 2019, vol. 10, issue 1, 1-11

Abstract: 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.

Date: 2019
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DOI: 10.1038/s41467-018-08180-z

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