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Probing the biophysical interplay between a viral genome and its capsid
Open accessAbstract
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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“As many capsid proteins self-assemble in vitro, native ion mobility MS can monitor the dynamics of capsid morphology and stability as a function of pH and ionic strength (28, 29).”
From The Impact of Mass Spectrometry–Based Proteomics on Fundamental Discoveries in Virology (2014) · cites this paper as [29]
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“For example, native MS and atomic force microscopy have demonstrated that the single-stranded RNA genome of the picorna-like Triatoma virus stabilizes or triggers uncoating of the capsid in a pH-dependent fashion through electrostatic genome-capsid interactions (29).”
From The Impact of Mass Spectrometry–Based Proteomics on Fundamental Discoveries in Virology (2014) · cites this paper as [29]
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BackgroundA strain of mycovirus AaVV1 mediates hypovirulence of Alternaria species
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“For example, changes in the protonation state of CCMV (Michel et al., 2006; Wilts et al., 2010), NV (Cuellar et al., 2010), Triatoma virus (TrV) (Snijder et al., 2013a), AdV (P ´ erez-Illana et al., 2021), and phage C22 (Sae-Ueng et al., 2020, 2022) particles resulted in significant changes in…”
Metadata
- Authors
- Snijder, J., Uetrecht, C., Rose, R. J., Sanchez-Eugenia, R., Marti, G. A., Agirre, J., Guérin, D. M. A., Wuite, G. J. L., Heck, A. J. R., & Roos, W. H.
- Affiliations
- Utrecht University (NL)
- Consejo Superior de Investigaciones Científicas (ES)
- Vrije Universiteit Amsterdam (NL)
- Corresponding author
- Heck, A. J. R.
- Roos, W. H.
- ORCID
- Venue
- Nature Chemistry
- Published
- 2013-04-28
- Volume
- 5
- Issue
- 6
- Pages
- 502-509
- ISSN
- 1755-4330 (ISSN-L)
- 1755-4349
- OpenAlex
- W2128588803
- Cited by
- 127
- References
- 50
- Citations by year
- 2026: 1 · 2025: 4 · 2024: 5 · 2023: 5 · 2022: 4 · 2021: 15 · 2020: 15 · 2019: 15 · 2018: 11 · 2017: 11 · 2016: 13 · 2015: 15 · 2014: 8 · 2013: 5
- FWCI
- 6.13
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Chemistry (publishedVersion)
- PubMed (publishedVersion)
- Utrecht University Repository (Utrecht University) (submittedVersion)
- VU Research Portal (submittedVersion)
- CONICET Digital (CONICET) (submittedVersion, cc-by-nc-sa)
- University of Groningen research database (University of Groningen / Centre for Information Technology) (submittedVersion)
- Data Archiving and Networked Services (DANS) (submittedVersion)
- Funders
- Nederlandse Organisatie voor Wetenschappelijk Onderzoek (819.02.10)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Immunology and Microbiology › Virology › Bacteriophages and microbial interactions
- Keywords
- picorna-like virus, viral capsid, viral genome, capsid assembly, VP2, VP4, capsid stability, cargo delivery
- MeSH terms
- Animals, Biomechanical Phenomena, Capsid, Hydrogen-Ion Concentration, Insect Viruses, Models, Molecular, Protein Conformation, Triatoma, Genome, Viral, Biophysical Phenomena, Virus Uncoating
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