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-Structure paper
Title | Evolution of a virus-like architecture and packaging mechanism in a repurposed bacterial protein. |
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Journal, issue, pages | Science, Vol. 372, Issue 6547, Page 1220-1224, Year 2021 |
Publish date | Jun 11, 2021 |
Authors | Stephan Tetter / Naohiro Terasaka / Angela Steinauer / Richard J Bingham / Sam Clark / Andrew J P Scott / Nikesh Patel / Marc Leibundgut / Emma Wroblewski / Nenad Ban / Peter G Stockley / Reidun Twarock / Donald Hilvert / |
PubMed 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 ...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. |
External links | Science / PubMed:34112695 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.04 - 7.04 Å |
Structure data | EMDB-11631, PDB-7a4f: EMDB-11632, PDB-7a4g: EMDB-11633, PDB-7a4h: EMDB-11634, PDB-7a4i: EMDB-11635, PDB-7a4j: |
Source |
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Keywords | VIRUS LIKE PARTICLE / capsid / design / virus mimic |