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Bacteria conjugate ubiquitin-like proteins to interfere with phage assembly
Open accessPreprint — published as 10.1038/s41586-024-07616-5
Abstract
Multiple immune pathways in humans conjugate ubiquitin-like proteins to virus and host molecules as a means of antiviral defense. Here we studied an anti-phage defense system in bacteria, comprising a ubiquitin-like protein, ubiquitin-conjugating enzymes E1 and E2, and a deubiquitinase. We show that during phage infection, this system specifically conjugates the ubiquitin-like protein to the phage central tail fiber, a protein at the tip of the tail that is essential for tail assembly as well as for recognition of the target host receptor. Following infection, cells encoding this defense system release a mixture of partially assembled, tailless phage particles, and fully assembled phages in which the central tail fiber is obstructed by the covalently attached ubiquitin-like protein. These phages exhibit severely impaired infectivity, explaining how the defense system protects the bacterial population from the spread of phage infection. Our findings demonstrate that conjugation of ubiquitin-like proteins is an antiviral strategy conserved across the tree of life.
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Metadata
- Authors
- Hör, J., Wolf, S. G., & Sorek, R.
- Affiliations
- Helmholtz Centre for Infection Research (DE)
- Weizmann Institute of Science (IL)
- Corresponding author
- Sorek, Rotem
- Venue
- Nature
- Publisher
- openRxiv
- Published
- 2023-09-04
- Volume
- 631
- Issue
- 8022
- Pages
- 850-856
- ISSN
- 0028-0836 (ISSN-L)
- OpenAlex
- W4400729407
- Cited by
- 46
- References
- 1
- Citations by year
- 2026: 16 · 2025: 12 · 2024: 16 · 2023: 2
- FWCI
- 12.04
- Type
- journal article
- Language
- en
- Open access
- green
- doi.org
- Licence
- cc-by-nc-nd
- Locations
- Nature (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- Deutsche Forschungsgemeinschaft (464312965, SPP2330, 466645764)
- Weizmann Institute of Science
- Council for Higher Education
- Institute for Advanced Studies in the Humanities, University of Edinburgh
- Division of Chemistry
- Topics
- Life Sciences › Immunology and Microbiology › Virology › Bacteriophages and microbial interactions
- Life Sciences › Immunology and Microbiology › Immunology › Invertebrate Immune Response Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- ubiquitin-like proteins, conjugation, phage assembly, E2 ubiquitin-conjugating enzyme, deubiquitinase, phage infectivity, bacterial immunity
- MeSH terms
- Deubiquitinating Enzymes, Bacterial Proteins, Bacteriophages, Escherichia coli, Ubiquitins, Conserved Sequence, Viral Tail Proteins, Virus Assembly, Evolution, Molecular, Ubiquitin-Conjugating Enzymes, Ubiquitin-Activating Enzymes
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