A viral expression factor behaves as a prion

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

rticle | Open | Published: 21 January 2019 A viral expression factor behaves as a prion

• Hao Nan ORCID: orcid.org/0000-0002-4028-5974¹,
• Hongying Chen¹,
• Mick F. Tuite² &
• Xiaodong Xu ORCID: orcid.org/0000-0001-6452-8419¹

Nature Communicationsvolume 10, Article number: 359 (2019) | Download Citation

Subjects

• Prions
• Protein aggregation
• Virology

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.