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首页> 外文期刊>Nature cell biology >A bacterial E3 ubiquitin ligase IpaH9.8 targets NEMO/IKKgamma to dampen the host NF-kappaB-mediated inflammatory response.
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A bacterial E3 ubiquitin ligase IpaH9.8 targets NEMO/IKKgamma to dampen the host NF-kappaB-mediated inflammatory response.

机译：细菌E3泛素连接酶IpaH9.8靶向NEMO / IKKgamma，以抑制宿主NF-κB介导的炎症反应。

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摘要

NF-kappaB (nuclear factor kappaB) has a pivotal role in many cellular processes, including the inflammatory and immune responses and, therefore, its activation is tightly regulated by the IKK (IkappaB kinase) complex and by IkappaBalpha degradation. When Shigella bacteria multiply within epithelial cells they release peptidoglycans, which are recognized by Nod1 and stimulate the NF-kappaB pathway, thus leading to a severe inflammatory response. Here, we show that IpaH9.8, a Shigella effector possessing E3 ligase activity, dampens the NF-kappaB-mediated inflammatory response to the bacterial infection in a unique way. IpaH9.8 interacts with NEMO/IKKgamma and ABIN-1, a ubiquitin-binding adaptor protein, promoting ABIN-1-dependent polyubiquitylation of NEMO. Consequently, polyubiquitylated NEMO undergoes proteasome-dependent degradation, which perturbs NF-kappaB activation. As NEMO is essential for NF-kappaB activation, we propose that the polyubiquitylation and degradation of NEMO during Shigella infection is a new bacterial strategy to modulate host inflammatory responses.
机译：NF-κB（核因子κB）在包括炎症和免疫反应在内的许多细胞过程中都具有举足轻重的作用，因此，其活化受IKK（IkappaB激酶）复合物和IkappaBalpha降解的严格调控。当志贺氏菌细菌在上皮细胞内繁殖时，它们会释放肽聚糖，被Nod1识别并刺激NF-κB途径，从而导致严重的炎症反应。在这里，我们显示IpaH9.8，一种具有E3连接酶活性的志贺氏菌效应物，以独特的方式抑制了NF-κB介导的细菌感染的炎症反应。 IpaH9.8与NEMO / IKKgamma和ABIN-1（一种遍在蛋白结合的衔接蛋白）相互作用，促进NEMO的ABIN-1依赖性多泛素化。因此，多泛素化的NEMO经历了蛋白酶体依赖性降解，从而扰乱了NF-κB的活化。由于NEMO对于NF-κB的激活至关重要，因此我们提出，志贺氏菌感染期间NEMO的多泛素化和降解是调节宿主炎症反应的新细菌策略。

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