Emily
Editor, Senior Moderator
https://www.nature.com/articles/s41467-018-08180-z
rticle | Open | Published: 21 January 2019 [h=1]A viral expression factor behaves as a prion[/h]
[h=3]Subjects[/h]
[h=2]Abstract[/h] 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[SUP]+[/SUP]]-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.
rticle | Open | Published: 21 January 2019 [h=1]A viral expression factor behaves as a prion[/h]
- Hao Nan ORCID: orcid.org/0000-0002-4028-5974[SUP]1[/SUP],
- Hongying Chen[SUP]1[/SUP],
- Mick F. Tuite[SUP]2[/SUP] &
- Xiaodong Xu ORCID: orcid.org/0000-0001-6452-8419[SUP]1[/SUP]
[h=3]Subjects[/h]
[h=2]Abstract[/h] 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[SUP]+[/SUP]]-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.