Bacteria conjugate ubiquitin-like proteins to interfere with phage assembly.
Nature
; 631(8022): 850-856, 2024 Jul.
Article
in En
| MEDLINE
| ID: mdl-39020165
ABSTRACT
Several immune pathways in humans conjugate ubiquitin-like proteins to virus and host molecules as a means of antiviral defence1-5. Here we studied an antiphage defence 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 fibre, 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 defence system release a mixture of partially assembled, tailless phage particles and fully assembled phages in which the central tail fibre is obstructed by the covalently attached ubiquitin-like protein. These phages show severely impaired infectivity, explaining how the defence 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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Bacterial Proteins
/
Bacteriophages
/
Ubiquitins
/
Virus Assembly
/
Ubiquitin-Conjugating Enzymes
/
Escherichia coli
/
Deubiquitinating Enzymes
Language:
En
Journal:
Nature
Year:
2024
Document type:
Article
Affiliation country:
Israel
Country of publication:
Reino Unido