The DOI matches its Crossref record; 51 of the 51 references it cites were found in a registry or an index.
A Vibrio cholerae viral satellite maximizes its spread and inhibits phage by remodeling hijacked phage coat proteins into small capsids
Open accessPreprint — published as 10.7554/elife.87611.3
Abstract
Abstract Phage satellites commonly remodel capsids they hijack from the phages they parasitize, but only a few mechanisms regulating the change in capsid size have been reported. Here, we investigated how a satellite from Vibrio cholerae, PLE, remodels the capsid it has been predicted to steal from the phage ICP1 (1). We identified that a PLE-encoded protein, TcaP, is both necessary and sufficient to form small capsids during ICP1 infection. Interestingly, we found that PLE is dependent on small capsids for efficient transduction of its genome, making it the first satellite to have this requirement. ICP1 isolates that escaped TcaP-mediated remodeling acquired substitutions in the coat protein, suggesting an interaction between these two proteins. With a procapsid-like-particle (PLP) assembly platform in Escherichia coli, we demonstrated that TcaP is a bona fide scaffold that regulates the assembly of small capsids. Further, we studied the structure of PLE PLPs using cryogenic electron microscopy and found that TcaP is an external scaffold, that is functionally and somewhat structurally similar to the external scaffold, Sid, encoded by the unrelated satellite P4 (2). Finally, we showed that TcaP is largely conserved across PLEs. Together, these data support a model in which TcaP directs the assembly of small capsids comprised of ICP1 coat proteins, which inhibits the complete packaging of the ICP1 genome and permits more efficient packaging of replicated PLE genomes.
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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
Features and development of Coot
Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 29,915
cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination
Punjani, A., Rubinstein, J. L., Fleet, D. J., & Brubaker, M. A. (2017) · Nature Methods · doi:10.1038/nmeth.4169 · Cited by 11,626
Liebschner, D., Afonine, P. V., Baker, M. L., Bunkóczi, G., Chen, V. B., Croll, T. I., Hintze, B., Hung, L.-W., Jain, S., McCoy, A. J., et al. (2019) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798319011471 · Cited by 7,953
New tools for automated cryo-EM single-particle analysis in RELION-4.0
Kimanius, D., Dong, L., Sharov, G., Nakane, T., & Scheres, S. H. W. (2021) · Biochemical Journal · doi:10.1042/bcj20210708 · Cited by 1,086
de la Rosa-Trevín, J. M., Quintana, A., del Cano, L., Zaldívar, A., Foche, I., Gutiérrez, J., Gómez-Blanco, J., Burguet-Castell, J., Cuenca-Alba, J., Abrishami, V., et al. (2016) · Journal of Structural Biology · doi:10.1016/j.jsb.2016.04.010 · Cited by 589
A bacteriophage encodes its own CRISPR/Cas adaptive response to evade host innate immunity
Seed, K. D., Lazinski, D. W., Calderwood, S. B., & Camilli, A. (2013) · Nature · doi:10.1038/nature11927 · Cited by 386
Self-citationAsarnow, D., Palovcak, E., & Cheng, Y. (2019) · Figshare · doi:10.5281/zenodo.3576629 · Cited by 241
Catalytic head assembling protein in virus morphogenesis
King, J. W., & Casjens, S. (1974) · Nature · doi:10.1038/251112a0 · Cited by 193
Mechanisms of DNA Packaging by Large Double-Stranded DNA Viruses
Rao, V. B., & Feiss, M. G. (2015) · Annual Review of Virology · doi:10.1146/annurev-virology-100114-055212 · Cited by 191
Research works printed but not linked: 5
- 2021, Bacteriophage ICP1: A Persistent Predator of, Annu. Rev. Virol, 12, 1
- 2022, UVC inactivation of pathogenic samples suitable for cryo-EM analysis. Commun, Biol, 5
- 2012, Assembly of bacteriophage 80α capsids in a Staphylococcus aureus expression system, Virology, 434, 242, 10.1016/j.virol.2012.08.031 · DOI
- 2020, Dominant Vibrio cholerae phage exhibits lysis inhibition sensitive to disruption by a defensive phage satellite, eLife, 9, 1
- 2019, Competition between mobile genetic elements drives optimization of a phage-encoded CRISPR-Cas system: Insights from a natural arms race, Philos. Trans. R. Soc. B Biol. Sci, 374, 1
Metadata
- Authors
- Boyd, C. M., Subramanian, S., Dunham, D. T., Parent, K. N., & Seed, K. D.
- Affiliations
- University of California, Berkeley (US)
- Michigan State University (US)
- Corresponding author
- Seed, Kimberley D.
- Venue
- eLife
- Publisher
- eLife Sciences Publications, Ltd
- Published
- 2023-11-16
- ISSN
- 2050-084X (ISSN-L)
- OpenAlex
- W4388722884
- Cited by
- 1
- References
- 51
- Citations by year
- 2024: 1
- Type
- posted content
- Language
- en
- Open access
- gold
- doi.org
- Locations
- eLife (acceptedVersion, cc-by)
- Funders
- National Institute of Allergy and Infectious Diseases (R01AI127652)
- National Institutes of Health (GM110185, GM140803, GM116789, T32 GM132022)
- National Science Foundation Graduate Research Fellowship Program (2018257700)
- National Science Foundation (1750125)
- Topics
- Life Sciences › Immunology and Microbiology › Virology › Bacteriophages and microbial interactions
- Life Sciences › Immunology and Microbiology › Virology › Plant and Fungal Interactions Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- phage satellites, Vibrio cholerae, TCAP, transduction, capsid assembly, phage packaging, phage inhibition, genome packaging
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- Boyd, C. M., Subramanian, S., Dunham, D. T., Parent, K. N., & Seed, K. D. (2023). A Vibrio cholerae viral satellite maximizes its spread and inhibits phage by remodeling hijacked phage coat proteins into small capsids. eLife. https://doi.org/10.7554/elife.87611.2
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