Cryo-EM structure of an active bacterial TIR-STING filament complex.

ABSTRACT: Stimulator of interferon genes (STING) is an antiviral signalling protein that is broadly conserved in both innate immunity in animals and phage defence in prokaryotes^1-4. Activation of STING requires its assembly into an oligomeric filament structure through binding of a cyclic dinucleotide^4-13, but the molecular basis of STING filament assembly and extension remains unknown. Here we use cryogenic electron microscopy to determine the structure of the active Toll/interleukin-1 receptor (TIR)-STING filament complex from a Sphingobacterium faecium cyclic-oligonucleotide-based antiphage signalling system (CBASS) defence operon. Bacterial TIR-STING filament formation is driven by STING interfaces that become exposed on high-affinity recognition of the cognate cyclic dinuc

SUBMITTER: Morehouse BR 

PROVIDER: S-EPMC9402430 | biostudies-literature | 2022 Aug

REPOSITORIES: biostudies-literature