A short prokaryotic Argonaute activates membrane effector to confer antiviral defense

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

A short prokaryotic Argonaute activates membrane effector to confer antiviral defense. / Zeng, Zhifeng; Chen, Yu; Pinilla-Redondo, Rafael; Shah, Shiraz A.; Zhao, Fen; Wang, Chen; Hu, Zeyu; Wu, Chang; Zhang, Changyi; Whitaker, Rachel J.; She, Qunxin; Han, Wenyuan.

In: Cell Host and Microbe, Vol. 30, No. 7, 2022, p. 930-943.e6.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Zeng, Z, Chen, Y, Pinilla-Redondo, R, Shah, SA, Zhao, F, Wang, C, Hu, Z, Wu, C, Zhang, C, Whitaker, RJ, She, Q & Han, W 2022, 'A short prokaryotic Argonaute activates membrane effector to confer antiviral defense', Cell Host and Microbe, vol. 30, no. 7, pp. 930-943.e6. https://doi.org/10.1016/j.chom.2022.04.015

APA

Zeng, Z., Chen, Y., Pinilla-Redondo, R., Shah, S. A., Zhao, F., Wang, C., Hu, Z., Wu, C., Zhang, C., Whitaker, R. J., She, Q., & Han, W. (2022). A short prokaryotic Argonaute activates membrane effector to confer antiviral defense. Cell Host and Microbe, 30(7), 930-943.e6. https://doi.org/10.1016/j.chom.2022.04.015

Vancouver

Zeng Z, Chen Y, Pinilla-Redondo R, Shah SA, Zhao F, Wang C et al. A short prokaryotic Argonaute activates membrane effector to confer antiviral defense. Cell Host and Microbe. 2022;30(7):930-943.e6. https://doi.org/10.1016/j.chom.2022.04.015

Author

Zeng, Zhifeng ; Chen, Yu ; Pinilla-Redondo, Rafael ; Shah, Shiraz A. ; Zhao, Fen ; Wang, Chen ; Hu, Zeyu ; Wu, Chang ; Zhang, Changyi ; Whitaker, Rachel J. ; She, Qunxin ; Han, Wenyuan. / A short prokaryotic Argonaute activates membrane effector to confer antiviral defense. In: Cell Host and Microbe. 2022 ; Vol. 30, No. 7. pp. 930-943.e6.

Bibtex

@article{e2e99f2bec9e442eba1109cf160ce78c,
title = "A short prokaryotic Argonaute activates membrane effector to confer antiviral defense",
abstract = "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.",
keywords = "abortive infection, archaea, membrane depolarization, membrane-associated toxic effector, microbial antiviral defense system, nucleic-acid recognition, phospholipids-interacting protein, prokaryotic Argonaute",
author = "Zhifeng Zeng and Yu Chen and Rafael Pinilla-Redondo and Shah, {Shiraz A.} and Fen Zhao and Chen Wang and Zeyu Hu and Chang Wu and Changyi Zhang and Whitaker, {Rachel J.} and Qunxin She and Wenyuan Han",
note = "Publisher Copyright: {\textcopyright} 2022 Elsevier Inc.",
year = "2022",
doi = "10.1016/j.chom.2022.04.015",
language = "English",
volume = "30",
pages = "930--943.e6",
journal = "Cell Host & Microbe",
issn = "1931-3128",
publisher = "Cell Press",
number = "7",

}

RIS

TY - JOUR

T1 - A short prokaryotic Argonaute activates membrane effector to confer antiviral defense

AU - Zeng, Zhifeng

AU - Chen, Yu

AU - Pinilla-Redondo, Rafael

AU - Shah, Shiraz A.

AU - Zhao, Fen

AU - Wang, Chen

AU - Hu, Zeyu

AU - Wu, Chang

AU - Zhang, Changyi

AU - Whitaker, Rachel J.

AU - She, Qunxin

AU - Han, Wenyuan

N1 - Publisher Copyright: © 2022 Elsevier Inc.

PY - 2022

Y1 - 2022

N2 - 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.

AB - 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.

KW - abortive infection

KW - archaea

KW - membrane depolarization

KW - membrane-associated toxic effector

KW - microbial antiviral defense system

KW - nucleic-acid recognition

KW - phospholipids-interacting protein

KW - prokaryotic Argonaute

U2 - 10.1016/j.chom.2022.04.015

DO - 10.1016/j.chom.2022.04.015

M3 - Journal article

C2 - 35594868

AN - SCOPUS:85131006460

VL - 30

SP - 930-943.e6

JO - Cell Host & Microbe

JF - Cell Host & Microbe

SN - 1931-3128

IS - 7

ER -

ID: 321260031