The bacterial arginine glycosyltransferase effector NleB preferentially modifies Fas-associated death domain protein (FADD).

ABSTRACT: The inhibition of host innate immunity pathways is essential for the persistence of attaching and effacing pathogens such as enteropathogenic Escherichia coli (EPEC) and Citrobacter rodentium during mammalian infections. To subvert these pathways and suppress the antimicrobial response, attaching and effacing pathogens use type III secretion systems to introduce effectors targeting key signaling pathways in host cells. One such effector is the arginine glycosyltransferase NleB1 (NleB^CR in C. rodentium) that modifies conserved arginine residues in death domain-containing host proteins with N-acetylglucosamine (GlcNAc), thereby blocking extrinsic apoptosis signaling. Ectopically expressed NleB1 modifies the host proteins Fas-associated via death domain

SUBMITTER: Scott NE 

PROVIDER: S-EPMC5655511 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature