ArticleNature chemistry2013
Probing the biophysical interplay between a viral genome and its capsid.
Article in Nature chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed, 127 citations in OpenAlex.
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- Physical and Chemical Barriers in the Larval Midgut Confer Developmental Resistance to Virus Infection inViruses · 2021Article
- Virion structure andJournal of virology · 2021Article
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- Fluctuating nonlinear spring theory: Strength, deformability, and toughness of biological nanoparticles from theoretical reconstruction of force-deformation spectra.Acta biomaterialia · 2021Article
- Complete and cooperative in vitro assembly of computationally designed self-assembling protein nanomaterials.Nature communications · 2021Article
- Reversibly Photo-Modulating Mechanical Stiffness and Toughness of Bioengineered Protein Fibers.Angewandte Chemie (International ed. in English) · 2021Article
- Ion Imaging of Native Protein Complexes Using Orthogonal Time-of-Flight Mass Spectrometry and a Timepix Detector.Journal of the American Society for Mass Spectrometry · 2021Article
- Mass Spectrometry-Based Structural Virology.Analytical chemistry · 2021Review
- Physics of viral dynamics.Nature reviews. Physics · 2021Review
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Authors and funding
10 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The interaction between a viral capsid and its genome governs crucial steps in the life cycle of a virus, such as assembly and genome uncoating. Tuning cargo-capsid interactions is also essential for successful design and cargo delivery in engineered viral systems. Here we investigate the interplay between cargo and capsid for the picorna-like Triatoma virus using a combined native mass spectrometry and atomic force microscopy approach. We propose a topology and assembly model in which heterotrimeric pentons that consist of five copies of structural proteins VP1, VP2 and VP3 are the free principal units of assembly. The interpenton contacts are established primarily by VP2. The dual role of the genome is first to stabilize the densely packed virion and, second, on an increase in pH to trigger uncoating by relaxing the stabilizing interactions with the capsid. Uncoating occurs through a labile intermediate state of the virion that reversibly disassembles into pentons with the concomitant release of protein VP4.
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