Department of Biochemistry and Molecular Pharmacology; RNA Therapeutics Institute; Graduate School of Biomedical Sciences
Amino Acids, Peptides, and Proteins | Biochemistry | Molecular Biology | Structural Biology | Virology | Viruses
The capsids of double-stranded DNA viruses protect the viral genome from the harsh extracellular environment, while maintaining stability against the high internal pressure of packaged DNA. To elucidate how capsids maintain stability in an extreme environment, we use cryoelectron microscopy to determine the capsid structure of thermostable phage P74-26 to 2.8-A resolution. We find P74-26 capsids exhibit an overall architecture very similar to those of other tailed bacteriophages, allowing us to directly compare structures to derive the structural basis for enhanced stability. Our structure reveals lasso-like interactions that appear to function like catch bonds. This architecture allows the capsid to expand during genome packaging, yet maintain structural stability. The P74-26 capsid has T = 7 geometry despite being twice as large as mesophilic homologs. Capsid capacity is increased with a larger, flatter major capsid protein. Given these results, we predict decreased icosahedral complexity (i.e. T < /= 7) leads to a more stable capsid assembly.
Cryoelectron microscopy, Virus structures
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DOI of Published Version
Nat Commun. 2019 Oct 2;10(1):4471. doi: 10.1038/s41467-019-12341-z. Link to article on publisher's site
Stone NP, Demo G, Agnello E, Kelch BA. (2019). Principles for enhancing virus capsid capacity and stability from a thermophilic virus capsid structure. Open Access Articles. https://doi.org/10.1038/s41467-019-12341-z. Retrieved from https://escholarship.umassmed.edu/oapubs/3996
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This work is licensed under a Creative Commons Attribution 4.0 License.