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Structure paper

TitleStructural mechanisms for regulation of GSDMB pore-forming activity.
Journal, issue, pagesNature, Vol. 616, Issue 7957, Page 598-605, Year 2023
Publish dateMar 29, 2023
AuthorsXiu Zhong / Huan Zeng / Zhiwei Zhou / Ya Su / Hang Cheng / Yanjie Hou / Yang She / Na Feng / Jia Wang / Feng Shao / Jingjin Ding /
PubMed AbstractCytotoxic lymphocyte-derived granzyme A (GZMA) cleaves GSDMB, a gasdermin-family pore-forming protein, to trigger target cell pyroptosis. GSDMB and the charter gasdermin family member GSDMD have been ...Cytotoxic lymphocyte-derived granzyme A (GZMA) cleaves GSDMB, a gasdermin-family pore-forming protein, to trigger target cell pyroptosis. GSDMB and the charter gasdermin family member GSDMD have been inconsistently reported to be degraded by the Shigella flexneri ubiquitin-ligase virulence factor IpaH7.8 (refs. ). Whether and how IpaH7.8 targets both gasdermins is undefined, and the pyroptosis function of GSDMB has even been questioned recently. Here we report the crystal structure of the IpaH7.8-GSDMB complex, which shows how IpaH7.8 recognizes the GSDMB pore-forming domain. We clarify that IpaH7.8 targets human (but not mouse) GSDMD through a similar mechanism. The structure of full-length GSDMB suggests stronger autoinhibition than in other gasdermins. GSDMB has multiple splicing isoforms that are equally targeted by IpaH7.8 but exhibit contrasting pyroptotic activities. Presence of exon 6 in the isoforms dictates the pore-forming, pyroptotic activity in GSDMB. We determine the cryo-electron microscopy structure of the 27-fold-symmetric GSDMB pore and depict conformational changes that drive pore formation. The structure uncovers an essential role for exon-6-derived elements in pore assembly, explaining pyroptosis deficiency in the non-canonical splicing isoform used in recent studies. Different cancer cell lines have markedly different isoform compositions, correlating with the onset and extent of pyroptosis following GZMA stimulation. Our study illustrates fine regulation of GSDMB pore-forming activity by pathogenic bacteria and mRNA splicing and defines the underlying structural mechanisms.
External linksNature / PubMed:36991125
MethodsEM (single particle) / X-ray diffraction
Resolution2.7 - 3.17 Å
Structure data

34258

8gtn

EMDB-34258, PDB-8gtn:
Cryo-EM structure of the gasdermin B pore
Method: EM (single particle) / Resolution: 3.17 Å

PDB-8gtj:
Crystal structure of IpaH7.8-LRR and GSDMB isoform-4 complex
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-8gtk:
Crystal structure of IpaH7.8-LRR and GSDMB isoform-1 complex
Method: X-RAY DIFFRACTION / Resolution: 3.1 Å

Chemicals

ChemComp-HOH:
WATER / Water

Source
  • homo sapiens (human)
  • shigella flexneri (bacteria)
KeywordsIMMUNE SYSTEM / Complex / Effector / Pyroptosis / Pore-forming

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