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TitleStructural mechanism of 3'3'-cGAMP-induced filamentation and phospholipid hydrolysis by CapV in bacterial antiphage defense.
Journal, issue, pagesCell Rep, Vol. 45, Issue 4, Page 117261, Year 2026
Publish dateApr 13, 2026
AuthorsYun Lv / Sheng Liu / Qihai Wang / Jing Zhu / Yingxiang Hou / Haiyan Xu / Deyan Zhu / Yu Liu / Jing Wu / Changxin Wu / Guijun Shang / Hongxiang Lou / Defen Lu / Huiqing Yuan / Deyu Zhu /
PubMed AbstractThe cyclic-oligonucleotide-based antiphage signaling system (CBASS) protects bacteria from phage infection. In Vibrio cholerae, phage infection activates CD-NTase DncV to produce 3'3'-cGAMP, which ...The cyclic-oligonucleotide-based antiphage signaling system (CBASS) protects bacteria from phage infection. In Vibrio cholerae, phage infection activates CD-NTase DncV to produce 3'3'-cGAMP, which triggers phospholipase CapV to degrade phosphatidylethanolamine and phosphatidylglycerol, the major phospholipids in the inner-membranes, thereby inducing cell death. However, how 3'3'-cGAMP activates CapV was unclear. Here we present crystal structures of inactive Acinetobacter baumannii CapV in apo and 3'3'-cGAMP-bound forms, along with cryo-EM structures of activated CapV-3'3'-cGAMP complex, with or without substrate dioleoylphosphatidyl-ethanolamine (DOPE). Apo-CapV forms symmetric dimers in a "closed" state. 3'3'-cGAMP binding drives lateral polymerization of dimers into filament assembly, inducing an "open" state that exposes the active site and substrate-binding cleft. DOPE binding further shifts CapV to an "ajar" state, where a Y-shaped cleft positions DOPE for hydrolysis via a conserved Ser/Asp catalytic dyad. This 3'3'-cGAMP-induced filamentation mirrors activation mechanisms of TIR-STING, TIR-SAVED, and mammalian STING, revealing a conserved signaling pattern across immune systems.
External linksCell Rep / PubMed:41984589
MethodsEM (single particle) / X-ray diffraction
Resolution2 - 3.0 Å
Structure data

62333

9kh6

EMDB-62333, PDB-9kh6:
cryo-EM structure of lipase/ligand/substrate complex
Method: EM (single particle) / Resolution: 2.8 Å

62334

9kh7

EMDB-62334: Cryo-EM structure of lipase/ligand complex
PDB-9kh7: cryo-EM structure of lipase/ligand complex
Method: EM (single particle) / Resolution: 3.0 Å

PDB-9wn0:
Crystal structure of phospholipase A2
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-9wn1:
PhospholipaseA2 with a ligand
Method: X-RAY DIFFRACTION / Resolution: 2.76 Å

Chemicals

ChemComp-4BW:
2-amino-9-[(2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-9-(6-amino-9H-purin-9-yl)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecin-2-yl]-1,9-dihydro-6H-purin-6-one

ChemComp-PEE:
1,2-dioleoyl-sn-glycero-3-phosphoethanolamine / DOPE, phospholipid*YM

ChemComp-HOH:
WATER

Source
  • acinetobacter baumannii (bacteria)
KeywordsHYDROLASE / lipase / LIPID BINDING PROTEIN / phospholipase / crystal sturcure / phospholipid / phospholipasec2 / ligand

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