UMMS Affiliation
Department of Biochemistry and Molecular Pharmacology; RNA Therapeutics Institute; Graduate School of Biomedical Sciences
Publication Date
2019-10-02
Document Type
Article
Disciplines
Amino Acids, Peptides, and Proteins | Biochemistry | Molecular Biology | Structural Biology | Virology | Viruses
Abstract
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.
Keywords
Cryoelectron microscopy, Virus structures
Rights and Permissions
Copyright © The Author(s) 2019. Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
DOI of Published Version
10.1038/s41467-019-12341-z
Source
Nat Commun. 2019 Oct 2;10(1):4471. doi: 10.1038/s41467-019-12341-z. Link to article on publisher's site
Journal/Book/Conference Title
Nature communications
Related Resources
PubMed ID
31578335
Repository Citation
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
Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 License.
Included in
Amino Acids, Peptides, and Proteins Commons, Biochemistry Commons, Molecular Biology Commons, Structural Biology Commons, Virology Commons, Viruses Commons