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TitleCyclic-dinucleotide-induced filamentous assembly of phospholipases governs broad CBASS immunity.
Journal, issue, pagesCell, Vol. 188, Issue 14, Page 3744-3756.e16, Year 2025
Publish dateJul 10, 2025
AuthorsJingge Wang / Zhao Li / Hao Lang / Wenfeng Fu / Yina Gao / Sen Yin / Panpan Sun / Zhaolong Li / Jiafeng Huang / Songqing Liu / Yun Zhu / Fei Sun / Dong Li / Pu Gao / Ang Gao /
PubMed AbstractCyclic-oligonucleotide-based antiphage signaling systems (CBASS), a widespread antiviral bacterial immune system homologous to the mammalian cGAS-STING pathway, synthesizes cyclic nucleotide signals ...Cyclic-oligonucleotide-based antiphage signaling systems (CBASS), a widespread antiviral bacterial immune system homologous to the mammalian cGAS-STING pathway, synthesizes cyclic nucleotide signals and triggers effector proteins to induce cell death and prevent viral propagation. Among various CBASS effectors, phospholipase effectors are the first to be discovered and are one of the most widespread families that sense cyclic dinucleotides to degrade cell membrane phospholipids. Here, we report that CBASS phospholipases assemble from a dimeric inactive state into active higher-order filamentous oligomers upon sensing cyclic dinucleotides. Using a combined approach of cryo-electron microscopy and X-ray crystallography, we have determined the structures of CBASS phospholipase in the inactive dimeric state, the cyclic-dinucleotide-bound active higher-order state, and the substrate-analog-bound catalytic mimicry state, thereby visualizing the complete conformational reorganization process. Complemented by functional assays of intermolecular binding, phospholipase enzymatic activity, in vitro membrane disruption, and in vivo antiphage efficiency, our work elucidates the mechanisms of assembly and activation of CBASS phospholipases.
External linksCell / PubMed:40345202
MethodsEM (single particle) / X-ray diffraction
Resolution1.648 - 3.33 Å
Structure data

60745

9ion

EMDB-60745, PDB-9ion:
Cryo-EM structure of cUA bound CapE filament
Method: EM (single particle) / Resolution: 3.27 Å

60746

9iop

EMDB-60746, PDB-9iop:
Cryo-EM structure of cUA and MAFP bound CapE filament
Method: EM (single particle) / Resolution: 3.33 Å

PDB-9iom:
CapE apo form
Method: X-RAY DIFFRACTION / Resolution: 1.648 Å

PDB-9ioq:
Crystal structure of CapE bound cUA
Method: X-RAY DIFFRACTION / Resolution: 1.999 Å

Chemicals

ChemComp-HOH:
WATER

PDB-1aep:
MOLECULAR STRUCTURE OF AN APOLIPOPROTEIN DETERMINED AT 2.5-ANGSTROMS RESOLUTION

ChemComp-MAY:
METHYL ARACHIDONYL FLUOROPHOSPHONATE / inhibitor*YM

Source
  • escherichia coli (E. coli)
KeywordsLIPID BINDING PROTEIN / CapE / patatin-like phospholipase protein

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