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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Baculoviridae / genetics*
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Baculoviridae / metabolism
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Gene Expression
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Genes, Reporter
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Genetic Complementation Test
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Green Fluorescent Proteins / genetics
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Green Fluorescent Proteins / metabolism
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Luminescent Proteins / genetics
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Luminescent Proteins / metabolism
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Peptide Termination Factors / genetics*
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Peptide Termination Factors / metabolism
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Phenotype
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Prion Proteins / genetics*
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Prion Proteins / metabolism
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Promoter Regions, Genetic
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Protein Aggregates
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Protein Folding
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Red Fluorescent Protein
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Saccharomyces cerevisiae / genetics*
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Saccharomyces cerevisiae / metabolism
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Saccharomyces cerevisiae Proteins / genetics*
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Saccharomyces cerevisiae Proteins / metabolism
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Sf9 Cells
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Spodoptera
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Viral Proteins / genetics*
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Viral Proteins / metabolism
Substances
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Luminescent Proteins
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Peptide Termination Factors
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Prion Proteins
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Protein Aggregates
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SUP35 protein, S cerevisiae
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Saccharomyces cerevisiae Proteins
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Viral Proteins
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enhanced green fluorescent protein
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Green Fluorescent Proteins