Tetter, S, Terasaka, N, Steinauer, A et al. (10 more authors) (2021) Evolution of a virus-like architecture and packaging mechanism in a repurposed bacterial protein. Science, 372 (6547). pp. 1220-1224. ISSN 0036-8075
Abstract
Viruses are ubiquitous pathogens of global impact. Prompted by the hypothesis that their earliest progenitors recruited host proteins for virion formation, we have used stringent laboratory evolution to convert a bacterial enzyme that lacks affinity for nucleic acids into an artificial nucleocapsid that efficiently packages and protects multiple copies of its own encoding messenger RNA. Revealing remarkable convergence on the molecular hallmarks of natural viruses, the accompanying changes reorganized the protein building blocks into an interlaced 240-subunit icosahedral capsid that is impermeable to nucleases, and emergence of a robust RNA stem-loop packaging cassette ensured high encapsidation yields and specificity. In addition to evincing a plausible evolutionary pathway for primordial viruses, these findings highlight practical strategies for developing nonviral carriers for diverse vaccine and delivery applications.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2021 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. This is the author’s version of the work. It is posted here by permission of the AAAS for personal use, not for redistribution. The definitive version was published in Science on 11th June 2021, Vol. 372, DOI: 10.1126/science.abg2822 |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) > Biological Chemistry (Leeds) The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) > Molecular Virology (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 25 Jun 2021 11:34 |
Last Modified: | 25 Jun 2021 11:34 |
Status: | Published |
Publisher: | American Association for the Advancement of Science (AAAS) |
Identification Number: | 10.1126/science.abg2822 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:175595 |