Arginine GlcNAcylation-a new form of PTM Utilized by Bacterial Pathogens to Block Host Inflammatory

来源 :湖北省细胞生物学学会2015年会员代表大会暨学术研讨会 | 被引量 : 0次 | 上传用户:sky_bj
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The tumour necrosis factor (TNF) family is crucial for immune homeostasis,cell death and inflammation.These cytokines are recognized by members of the TNF receptor (TNFR) family of death receptors,including TNFR1 and TNFR2,FAS and TNFrelated apoptosis-inducing ligand (TRAIL) receptors.We discovered that death domains in several proteins,including TRADD,FADD,RIPK1 and TNFR1,were directly inactivated by NleB,an enteropathogenic Escherichia coli (EPEC) type Ⅲ secretion system effector.NleB harbored an unprecedented N-acetylglucosamine (GlcNAc) transferase activity that specifically modified a conserved arginine in these death domains (Arg 117 in the FADD death domain) (Li et al.,Nature,2013).NleB GlcNAcylation (the addition of GlcNAc onto a protein side chain) of death domains blocked homotypic/heterotypic death domain interactions and assembly of the oligomeric TNFR1 complex,thereby disrupting TNF signalling in EPEC-infected cells,including NF-kB signalling,apoptosis and necroptosis.Type-Ⅲ secretion systemdelivered NleB also blocked FAS ligand and TRAIL-induced cell death by preventing formation of a FADD-mediated death-inducing signalling complex (DISC).
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