A structural dendrogram of the actinobacteriophage major capsid proteins provides important structural insights into the evolution of capsid stability
Open accessPublished version of a preprint
Abstract
Many double-stranded DNA viruses, including tailed bacteriophages (phages) and herpesviruses, use the HK97-fold in their major capsid protein to make the capsomers of the icosahedral viral capsid. After the genome packaging at near-crystalline densities, the capsid is subjected to a major expansion and stabilization step that allows it to withstand environmental stresses and internal high pressure. Several different mechanisms for stabilizing the capsid have been structurally characterized, but how these mechanisms have evolved is still not understood. Using cryo-EM structure determination of 10 capsids, structural comparisons, phylogenetic analyses, and Alphafold predictions, we have constructed a detailed structural dendrogram describing the evolution of capsid structural stability within the actinobacteriophages. We show that the actinobacteriophage major capsid proteins can be classified into 15 groups based upon their HK97-fold.
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Cites
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764 · see citing works
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- Authors
- Podgorski, J. M., Freeman, K., Gosselin, S., Huet, A., Conway, J. F., Bird, M., Grecco, J., Patel, S., Jacobs-Sera, D., Hatfull, G., Gogarten, J. P., Ravantti, J., & White, S. J.
- Affiliations
- University of Connecticut (US)
- University of Pittsburgh (US)
- University of Helsinki (FI)
- Corresponding author
- White, Simon J.
- ORCID
- Venue
- Structure
- Publisher
- Elsevier BV
- Published
- 2023-03
- Volume
- 31
- Issue
- 3
- Pages
- 282-294.e5
- ISSN
- 0969-2126 (ISSN-L)
- PMC
- PMC10071307
- OpenAlex
- W4316495397
- Cited by
- 32
- References
- 1
- Citations by year
- 2026: 9 · 2025: 18 · 2024: 2 · 2023: 3
- FWCI
- 5.18
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 367 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Structure (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Työväentutkimus Vuosikirja (submittedVersion)
- Funders
- Howard Hughes Medical Institute (GT12053)
- U.S. Department of Energy
- Purdue University
- Oregon Health and Science University (436923)
- University of Connecticut
- University of Pittsburgh
- University of North Texas
- Inyuvesi Yakwazulu-Natali
- National Institutes of Health (1s10od019995-01, 1s10od025009-01, GT12053)
- Office of Science
- National Institute of General Medical Sciences (U24GM129547, R35GM131729)
- Biological and Environmental Research
- Topics
- Physical Sciences › Environmental Science › Ecology › Bacteriophages and microbial interactions
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
- Keywords
- capsid stability, icosahedral capsid, tailed bacteriophages, herpesvirus
- MeSH terms
- Bacteriophages, Capsid, Phylogeny, Virus Assembly, Cryoelectron Microscopy, Capsid Proteins
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