An E1-E2 fusion protein primes antiviral immune signalling in bacteria.

ABSTRACT: In all organisms, innate immune pathways sense infection and rapidly activate potent immune responses while avoiding inappropriate activation (autoimmunity). In humans, the innate immune receptor cyclic GMP-AMP synthase (cGAS) detects viral infection to produce the nucleotide second messenger cyclic GMP-AMP (cGAMP), which initiates stimulator of interferon genes (STING)-dependent antiviral signalling¹. Bacteria encode evolutionary predecessors of cGAS called cGAS/DncV-like nucleotidyltransferases² (CD-NTases), which detect bacteriophage infection and produce diverse nucleotide second messengers³. How bacterial CD-NTase activation is controlled remains unknown. Here we show that CD-NTase-associated protein 2 (Cap2) primes bacterial CD-NTases for activation t

SUBMITTER: Ledvina HE 

PROVIDER: S-EPMC10292035 | biostudies-literature | 2023 Apr

REPOSITORIES: biostudies-literature