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Scientists have long dreamt of being able to track and analyse each step in the assembly of a virus’s protein shell. An ingenious experiment shows how this can be done.
By
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Charlotte Uetrecht
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Charlotte Uetrecht is at the Centre for Structural Systems Biology, Deutsches Elektronen-Synchrotron (DESY) and the Leibniz Institute of Virology and the University of Lübeck, 22607 Hamburg, Germany. She is also at the Institute of Chemistry and Metabolomics, University of Lübeck, Lübeck, Germany.
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Imagine watching a simple building being constructed from identical blocks. The blocks are assembled by interacting through tiny contact areas and can move with respect to each other during assembly, yet the fully formed structure is stable and rigid. Nevertheless, the completed construction can come apart in response to a trigger. Viruses have protein shells that assemble and behave in this way — protecting the viral genome and then releasing it during the infection of a cell. Observing the assembly of these shells has been difficult, and measuring the kinetics and energetics of the process to deduce the underlying principles of the process has been even harder. Writing in Nature, Asor et al.1 report a method that has achieved all of this for a virus-like particle (VLP), a system that replicates the shells of natural viruses.
Nature 657, 606-608 (2026)
doi: https://doi.org/10.1038/d41586-026-02644-9
References
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Competing Interests
The author declares no competing interests.
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