Dedicated bacterial esterases reverse lipopolysaccharide ubiquitylation to block immune sensing.

ABSTRACT: Pathogenic bacteria have evolved diverse mechanisms to counteract cell-autonomous immunity, which otherwise guards both immune and non-immune cells from the onset of an infection^1,2. The versatile immunity protein Ring finger protein 213 (RNF213)^3-6 mediates the non-canonical ester-linked ubiquitylation of lipopolysaccharide (LPS), marking bacteria that sporadically enter the cytosol for destruction by antibacterial autophagy⁴. However, whether cytosol-adapted pathogens are ubiquitylated on their LPS and whether they escape RNF213-mediated immunity, remains unknown. Here we show that Burkholderia deubiquitylase (DUB), TssM^7-9, is a potent esterase that directly reverses the ubiquitylation of LPS. Without TssM, cytosolic Burkholderia

SUBMITTER: Szczesna M 

PROVIDER: S-EPMC10371091 | biostudies-literature | 2023 Jul

REPOSITORIES: biostudies-literature