Structure and assembly of a bacterial gasdermin pore.

ABSTRACT: In response to pathogen infection, gasdermin (GSDM) proteins form membrane pores that induce a host cell death process called pyroptosis^1-33. Studies of human and mouse GSDM pores reveal the functions and architectures of 24-33 protomers assemblies^4-9, but the mechanism and evolutionary origin of membrane targeting and GSDM pore formation remain unknown. Here we determine a structure of a bacterial GSDM (bGSDM) pore and define a conserved mechanism of pore assembly. Engineering a panel of bGSDMs for site-specific proteolytic activation, we demonstrate that diverse bGSDMs form distinct pore sizes that range from smaller mammalian-like assemblies to exceptionally large pores containing >50 protomers. We determine a 3.3 Å cryo-EM structure of a Vitiosangium bGSDM

SUBMITTER: Johnson AG 

PROVIDER: S-EPMC10153256 | biostudies-literature | 2023 Oct

REPOSITORIES: biostudies-literature