A short prokaryotic Argonaute activates membrane effector to confer antiviral defense
Research output: Contribution to journal › Journal article › peer-review
Documents
- Fulltext
Accepted author manuscript, 4.92 MB, PDF document
Argonaute (Ago) proteins are widespread nucleic-acid-guided enzymes that recognize targets through complementary base pairing. Although, in eukaryotes, Agos are involved in RNA silencing, the functions of prokaryotic Agos (pAgos) remain largely unknown. In particular, a clade of truncated and catalytically inactive pAgos (short pAgos) lacks characterization. Here, we reveal that a short pAgo protein in the archaeon Sulfolobus islandicus, together with its two genetically associated proteins, Aga1 and Aga2, provide robust antiviral protection via abortive infection. Aga2 is a toxic transmembrane effector that binds anionic phospholipids via a basic pocket, resulting in membrane depolarization and cell killing. Ago and Aga1 form a stable complex that exhibits nucleic-acid-directed nucleic-acid-recognition ability and directly interacts with Aga2, pointing to an immune sensing mechanism. Together, our results highlight the cooperation between pAgos and their widespread associated proteins, suggesting an uncharted diversity of pAgo-derived immune systems.
Original language | English |
---|---|
Journal | Cell Host and Microbe |
Volume | 30 |
Issue number | 7 |
Pages (from-to) | 930-943.e6 |
Number of pages | 21 |
ISSN | 1931-3128 |
DOIs | |
Publication status | Published - 2022 |
Bibliographical note
Publisher Copyright:
© 2022 Elsevier Inc.
- abortive infection, archaea, membrane depolarization, membrane-associated toxic effector, microbial antiviral defense system, nucleic-acid recognition, phospholipids-interacting protein, prokaryotic Argonaute
Research areas
ID: 321260031