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Title2'3'-cGAMP-induced membrane shearing promotes broad antiphage immunity.
Journal, issue, pagesCell, Vol. 189, Issue 12, Page 3636-3650.e19, Year 2026
Publish dateJun 11, 2026
AuthorsYina Gao / Zhaolong Li / Yufei Zhou / Weimin Li / Quanjin Li / Jingge Wang / Miao Shi / Feng Ye / Chunqiu Zhao / Songqing Liu / Qiuyao Jiang / Yun Zhu / Fei Sun / Ang Gao / Pu Gao /
PubMed AbstractCyclic-oligonucleotide-based anti-phage signaling system (CBASS), a central prokaryotic antiviral strategy and evolutionary ancestor of the mammalian cyclic GMP-AMP synthase (cGAS)-stimulator of ...Cyclic-oligonucleotide-based anti-phage signaling system (CBASS), a central prokaryotic antiviral strategy and evolutionary ancestor of the mammalian cyclic GMP-AMP synthase (cGAS)-stimulator of interferon genes (STING) pathway, relies on cyclic-nucleotide-activated effectors to elicit immunity. The most prevalent effectors are transmembrane (TM) proteins, yet their mechanisms remain unknown. Here, we show how a representative three transmembrane (3TM)-SMODS-associated fused to various effector domains (SAVED) effector couples ligand sensing to membrane disruption. Upon binding 2'3'-cyclic GMP-AMP (cGAMP)-synthesized by bacterial cGAS/DncV-like nucleotidyltransferase (CD-NTase) with features resembling mammalian cGAS-3TM-SAVED assembles stepwise from an apo monomer through a transient dimer into extended filaments. Filament assembly employs 2'3'-cGAMP as molecular glue linking SAVED domains and reorients TM helices and amphipathic hairpins into vertically offset arrays. Both arrays bear opposing hydrophobic and hydrophilic faces, thereby driving vertical lipid shearing. This shearing generates a linear pore array that permeabilizes membranes and triggers cell death. These findings uncover the long-missing mechanism of CBASS TM effectors and establish vertical membrane shearing as an unrecognized principle of membrane disruption across domains of life.
External linksCell / PubMed:41999741
MethodsEM (single particle)
Resolution3.27 Å
Structure data

66157

9wq2

EMDB-66157, PDB-9wq2:
Structure of 3TM-SAVED dimer bound to 2'3'-cGAMP
Method: EM (single particle) / Resolution: 3.27 Å

66158

9wq3

EMDB-66158, PDB-9wq3:
Structure of 3TM-SAVED Filament bound to 2'3'-cGAMP
Method: EM (single particle) / Resolution: 3.27 Å

Chemicals

ChemComp-1SY:
cGAMP

Source
  • bacillus thuringiensis (bacteria)
KeywordsIMMUNE SYSTEM / SAVED

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