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首页> 外文期刊>PLoS Genetics >Inhibition of the oligosaccharyl transferase in Caenorhabditis elegans that compromises ER proteostasis suppresses p38-dependent protection against pathogenic bacteria
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Inhibition of the oligosaccharyl transferase in Caenorhabditis elegans that compromises ER proteostasis suppresses p38-dependent protection against pathogenic bacteria

机译：抑制寡糖转移酶<斜视> caenorhabdise elegans 抑制ER蛋白质的抑制了对致病性细菌的P38依赖性保护

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The oligosaccharyl transferase (OST) protein complex mediates the N-linked glycosylation of substrate proteins in the endoplasmic reticulum (ER), which regulates stability, activity, and localization of its substrates. Although many OST substrate proteins have been identified, the physiological role of the OST complex remains incompletely understood. Here we show that the OST complex in C . elegans is crucial for ER protein homeostasis and defense against infection with pathogenic bacteria Pseudomonas aeruginosa (PA14), via immune-regulatory PMK-1/p38 MAP kinase. We found that genetic inhibition of the OST complex impaired protein processing in the ER, which in turn up-regulated ER unfolded protein response (UPR ~(ER)). We identified vitellogenin VIT-6 as an OST-dependent glycosylated protein, critical for maintaining survival on PA14. We also showed that the OST complex was required for up-regulation of PMK-1 signaling upon infection with PA14. Our study demonstrates that an evolutionarily conserved OST complex, crucial for ER homeostasis, regulates host defense mechanisms against pathogenic bacteria.
机译：寡核酸转移酶（OST）蛋白质复合物在内质网（ER）中介导底物蛋白的N-连接的糖基化，该网状蛋白（ER）调节其基材的稳定性，活性和定位。虽然已经鉴定了许多OST底物蛋白，但OST复合物的生理作用仍然不完全理解。在这里，我们展示了C中的OST复杂。 elegans对ER蛋白质稳态和防御感染感染的杆菌，通过免疫调节PMK-1 / P38 Map激酶对抗毒性稳态和防御感染。我们发现，ET中的OST复合物受损蛋白质加工的遗传抑制，其逆向调节的ER展开蛋白反应（UPR〜（ER））。我们将vallogenin vit-6鉴定为依赖于OST依赖性糖基化蛋白，用于维持PA14的存活至关重要。我们还表明，对PA14感染时PMK-1信号传导的上调需要ost复合物。我们的研究表明，进化保守的OST复合物对ER稳态至关重要，调节对致病细菌的宿主防御机制。

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