Optineurin is an ubiquitin-binding protein implicated in the pathogenesis of glaucoma, that can function as an autophagic receptor at the crossroad between innate immunity and destruction of cytosolic pathogens by autophagy, a process also known as xenophagy.
Upon infection, most Salmonella are sequestered into Salmonella-containing vacuoles, SCVs, but some can escape from SCVs and proliferate in the cytosol. To prevent this, cytosolic bacteria are rapidly ubiquitinated, leading to the recruitment of several autophagic receptors including NDP52 and p62 as well as that of the TANK-binding kinase 1, TBK1. In response to bacterial products such as lipopolysaccharide (LPS), the pattern recognition receptor Toll-like receptor 4, TLR4, activates TBK1 leading to the phosphorylation of optineurin. Phosphorylated OPTN has a high affinity for the autophagic protein LC3, thereby physically bridging ubiquitinated bacteria to the autophagic machinery and allowing for their elimination by xenophagy.
應(yīng)用類型
免疫原
Peptide derived from human optineurin protein (a.a. 86-96)