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Phage anti-CBASS protein simultaneously sequesters cyclic trinucleotides and dinucleotides.
Xueli Cao1,2, Yu Xiao3,2, Erin Huiting4,2
1Beijing Advanced Innovation Center for Soft Matter Science and Engineering, State Key Laboratory of Chemical Resource Engineering, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing 100029, China.
Biorxiv : the Preprint Server for Biology
|July 3, 2023
Summary
Phage protein Acb2 acts as a broad-spectrum inhibitor of cyclic GMP-AMP synthase (cGAS)-based immunity. It sequesters diverse cyclic nucleotide signals, protecting phages from bacterial cyclic oligonucleotide-based antiphage signaling (CBASS) systems.
Area of Science:
- Molecular Biology
- Immunology
- Virology
Background:
- Cyclic oligonucleotide-based antiphage signaling (CBASS) is a key bacterial defense against phages.
- Phages encode anti-CBASS (Acb) proteins to counteract these systems.
- Acb2 is a recently identified phage anti-CBASS protein known to bind cyclic dinucleotides.
Conclusions:
- Acb2 functions as a potent, broad-spectrum inhibitor of cGAS-based immunity by sequestering diverse cyclic oligonucleotide signals.
- The dual-pocket structure of Acb2 enables simultaneous neutralization of multiple signaling molecules, highlighting an advanced phage counter-defense strategy.
- Acb2 represents a significant target for understanding and potentially manipulating bacterial anti-phage immunity.
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