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TitleA virally encoded tRNA neutralizes the PARIS antiviral defence system.
Journal, issue, pagesNature, Vol. 634, Issue 8033, Page 424-431, Year 2024
Publish dateAug 7, 2024
AuthorsNathaniel Burman / Svetlana Belukhina / Florence Depardieu / Royce A Wilkinson / Mikhail Skutel / Andrew Santiago-Frangos / Ava B Graham / Alexei Livenskyi / Anna Chechenina / Natalia Morozova / Trevor Zahl / William S Henriques / Murat Buyukyoruk / Christophe Rouillon / Baptiste Saudemont / Lena Shyrokova / Tatsuaki Kurata / Vasili Hauryliuk / Konstantin Severinov / Justine Groseille / Agnès Thierry / Romain Koszul / Florian Tesson / Aude Bernheim / David Bikard / Blake Wiedenheft / Artem Isaev /
PubMed AbstractViruses compete with each other for limited cellular resources, and some deliver defence mechanisms that protect the host from competing genetic parasites. The phage antirestriction induced system ...Viruses compete with each other for limited cellular resources, and some deliver defence mechanisms that protect the host from competing genetic parasites. The phage antirestriction induced system (PARIS) is a defence system, often encoded in viral genomes, that is composed of a 55 kDa ABC ATPase (AriA) and a 35 kDa TOPRIM nuclease (AriB). However, the mechanism by which AriA and AriB function in phage defence is unknown. Here we show that AriA and AriB assemble into a 425 kDa supramolecular immune complex. We use cryo-electron microscopy to determine the structure of this complex, thereby explaining how six molecules of AriA assemble into a propeller-shaped scaffold that coordinates three subunits of AriB. ATP-dependent detection of foreign proteins triggers the release of AriB, which assembles into a homodimeric nuclease that blocks infection by cleaving host lysine transfer RNA. Phage T5 subverts PARIS immunity through expression of a lysine transfer RNA variant that is not cleaved by PARIS, thereby restoring viral infection. Collectively, these data explain how AriA functions as an ATP-dependent sensor that detects viral proteins and activates the AriB toxin. PARIS is one of an emerging set of immune systems that form macromolecular complexes for the recognition of foreign proteins, rather than foreign nucleic acids.
External linksNature / PubMed:39111359 / PubMed Central
MethodsEM (single particle)
Resolution3.2 - 4.5 Å
Structure data

42719

8ux9

EMDB-42719, PDB-8ux9:
Asymmetric unit of the PARIS Immune Complex at 3.2 Angstrom Resolution
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-43103: Structure of the PARIS immune complex with AriB subunits in C3 arrangement.
Method: EM (single particle) / Resolution: 3.71 Å

EMDB-43104: PARIS immune complex with AriB subunits in the trans arrangement.
Method: EM (single particle) / Resolution: 3.82 Å

EMDB-43105: Map of the AriA homohexamer following release of the AriB effector during PARIS-mediated defense.
Method: EM (single particle) / Resolution: 4.5 Å

Chemicals

ChemComp-AGS:
PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / ATP-gamma-S, energy-carrying molecule analogue*YM

Source
  • escherichia coli b185 (bacteria)
KeywordsIMMUNE SYSTEM / PARIS / AriA / AriB / DUF4435

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