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TitleMolecular mechanisms of CBASS phospholipase effector CapV mediated membrane disruption.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 8611, Year 2025
Publish dateSep 29, 2025
AuthorsJianping Kong / Wanqian Wu / Shiyue Ke / Zihan Zhou / Shenglan Xia / Jianyu Chen / Runyu Zhu / Yijia Hou / Tinashe Makanyire / Xiangru Shan / Zhuyue Zhuo / Keying Li / Hongtao Shen / Pan Yang / Pingping Huang / Jingxian Liu / Jing Li / Xiaolian Sun / Jiajia Dong / Hongbin Sun / Meirong Chen / Meiling Lu / Zhaoxing Li / Yibei Xiao /
PubMed AbstractCyclic oligonucleotide-based antiphage signaling systems (CBASS) are widespread bacterial immune systems that trigger host suicide via cyclic nucleotide-activated effectors. The predominant strategy ...Cyclic oligonucleotide-based antiphage signaling systems (CBASS) are widespread bacterial immune systems that trigger host suicide via cyclic nucleotide-activated effectors. The predominant strategy to induce cell death in CBASS is membrane disruption. Here, we demonstrate that patatin-like phospholipase CapV, the most abundant CBASS effector, relocates and cleaves membrane phospholipids at the cell pole upon 3'3'-cGAMP binding, inducing polarized membrane disruption and cell death. Using cryo-EM, we reveal that apo-CapV adopts both dimeric and tetrameric states, with its phospholipid-binding pocket occluded and locked in an inactive conformation. Binding to 3'3'-cGAMP induces filamentation and substantial conformational change of CapV, enhancing membrane binding via electrostatic interactions between its interspaced basic surfaces and the negatively charged phosphate moieties of phospholipids. Simultaneously, the rearrangement opens the phospholipid-binding pocket, enabling the accommodation of two fatty acid chains of phospholipid within distinct hydrophobic pockets. Our findings reveal a filament-dependent activation mechanism for phospholipase-mediated membrane disruption during antiviral response.
External linksNat Commun / PubMed:41022836 / PubMed Central
MethodsEM (single particle)
Resolution2.7 - 3.1 Å
Structure data

60393

8zr9

EMDB-60393: Cryo-EM structure of AbCapV filemant bound with 3',3'-cGAMP with extra phospholipid density
PDB-8zr9: Cryo-EM structure of AbCapV filemant bound with 3',3'-cGAMP
Method: EM (single particle) / Resolution: 2.7 Å

61417

9jeh

EMDB-61417, PDB-9jeh:
Cryo-EM structure of AbCapV dimer, apo form
Method: EM (single particle) / Resolution: 2.9 Å

61419

9jek

EMDB-61419, PDB-9jek:
Cryo-EM structure of AbCapV tetramer, intermediate form
Method: EM (single particle) / Resolution: 3.1 Å

62291

9kej

EMDB-62291: Cryo-EM structure of AbCapV S58A filament bound with 3'3'-cGAMP with extra phospholipid density
PDB-9kej: Cryo-EM structure of AbCapV S58A filament bound with 3'3'-cGAMP
Method: EM (single particle) / Resolution: 3.04 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

Source
  • acinetobacter baumannii (bacteria)
KeywordsHYDROLASE / CBASS / phospholipase

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