ArticleNature communications2019
Principles for enhancing virus capsid capacity and stability from a thermophilic virus capsid structure.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 76 citations in OpenAlex.
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- Cryo-EM structure of cyanopodophage A4 reveals a pentameric pre-ejectosome in the double-stabilized capsid.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Global structural survey of the flagellotropic myophage φTE infecting agricultural pathogen Pectobacterium atrosepticum.Nature communications · 2025Article
- Stabilization mechanism accommodating genome length variation in evolutionarily related viral capsids.Nature communications · 2025Article
- Capsid transfer of the retrotransposon Copia controls structural synaptic plasticity in Drosophila.PLoS biology · 2025Article
- Atlas of Interactions Between Decoration Proteins and Major Capsid Proteins of Coliphage N4.Viruses · 2024Article
- The comparison of decay rates of infectious SARS-CoV-2 and viral RNA in environmental waters and wastewater.The Science of the total environment · 2024Article
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- Capsid structure of bacteriophage ΦKZ provides insights into assembly and stabilization of jumbo phages.Nature communications · 2024Article
- Predicting the risk of primary Sjögren's syndrome with key N7-methylguanosine-related genes: A novel XGBoost model.Heliyon · 2024Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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-Å 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.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.