WDR5在VISA信号复合物组装及细胞抗病毒反应中的作用机制
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摘要
长期以来,病毒感染是人类健康的一大威胁。近年来,对机体抗病毒免疫反应的研究已经成为生物学领域的热点之一。以往的研究表明,病毒感染细胞后能够被天然免疫的模式识别受体(pattern- recognition receptor, PRR)识别,激活一系列信号通路,最终诱导包括IRF3和NF-κB在内的多个转录因子的激活。活化的转录因子进入细胞核,协同诱导Ⅰ型干扰素、炎症因子等多种细胞因子的表达和分泌。Ⅰ型干扰素通过与细胞膜上的干扰素受体相互作用,诱导一系列抗病毒蛋白的表达,这些抗病毒蛋白协同作用,通过抑制病毒复制或诱导被感染细胞的凋亡,实现细胞的抗病毒反应。炎症因子所引发的炎症反应能够激活天然免疫细胞,并诱导适应性免疫应答的启动。由此可见,Ⅰ型干扰素等细胞因子对机体的抗病毒免疫反应具有至关重要的作用。
近年来的研究表明,病毒在感染与复制过程中所产生的病毒保守组分,如病毒RNA,能够被细胞内的PRRs,如RIG-I (retinoic acid-inducible geneⅠ)和MDA5 (melanoma differentiation- associated gene 5)所识别并结合。识别病毒RNA后,RIG-I和MDA5通过下游的接头蛋白VISA招募多个信号分子,共同组成一个信号复合物,向下游传递信号。VISA信号复合物的成功组装是病毒诱导Ⅰ型干扰素表达所不可或缺的。目前为止,关于VISA信号复合物中的蛋白组成,以及这些蛋白在复合物的形成及信号转导过程中所发挥的作用还不完全清楚。为了进一步探明VISA信号复合物的潜在成员及其在抗病毒信号通路中的功能,我们用串联亲和纯化的方法筛选了可能与VISA相互作用的蛋白。通过筛选,我们得到了一个与VISA特异性相互作用的蛋白WDR5 (WD repeat 5)。我们的研究结果显示,内源性WDR5与VISA之间的相互作用依赖于病毒感染。病毒感染细胞后,WDR5转移到线粒体上,与线粒体外膜上的VISA相互作用。利用RNAi干扰技术降低细胞内WDR5的表达能够阻碍病毒诱导的VISA信号复合物的装配。同时,降低WDR5的表达量还会抑制病毒诱导的IRF3和NF-κB的激活,以及IFNB1基因的转录。综上所述,这些发现表明WDR5在VISA信号复合物的装配过程中至关重要,同时在病毒诱导Ⅰ型干扰素产生的过程中发挥重要作用。该项研究增加了对抗病毒天然免疫信号转导分子机制的了解。
Viral infection could be detected by the pattern recognition receptors of the innate immune system, leading to activation of signaling transduction, results in activation of the transcription factors NF-κB and IRF3. These transcription factors collaborate to induce typeⅠinterferons (IFNs). TypeⅠinterferons further induce expression of the Anti-Viral Proteins. AVPs inhibit viral replication as well as induce the apoptosis of infected cells, therefore mediate cellular antiviral response. It is well admitted that the typeⅠinterferons play a very important role in antiviral immunity.
Recent studies have demonstrated that, RIG-I and MDA5, two cytosolic PRRs, specifically detect viral RNAs that are produced during viral replication. Binding of RIG-I/MDA5 to viral RNA leads to recruitment of a downstream adaptor protein VISA. The mitochondrial outer membrane protein VISA acts as a critical adapter for assembling a virus-induced complex that signals NF-κB and IRF3 activation. However, the components of the VISA-associated complex and their roles in antiviral response are not fully understood yet.
Using a biochemical purification approach, we identified the WD repeat protein WDR5 as a VISA-associated protein. WDR5 was recruited to VISA in a viral infection dependent manner. Viral infection also caused translocation of WDR5 from the nucleus to mitochondria. Knockdown of WDR5 impaired the formation of virus-induced VISA-associated complex. Consistently, knockdown of WDR5 inhibited virus-triggered activation of IRF3 and NF-κB as well as transcription of the IFNB1 gene. These findings suggest that WDR5 is essential in assembling a virus-induced VISA-associated complex and plays an important role in virus-triggered induction of typeⅠIFNs.
近年来的研究表明,病毒在感染与复制过程中所产生的病毒保守组分,如病毒RNA,能够被细胞内的PRRs,如RIG-I (retinoic acid-inducible geneⅠ)和MDA5 (melanoma differentiation- associated gene 5)所识别并结合。识别病毒RNA后,RIG-I和MDA5通过下游的接头蛋白VISA招募多个信号分子,共同组成一个信号复合物,向下游传递信号。VISA信号复合物的成功组装是病毒诱导Ⅰ型干扰素表达所不可或缺的。目前为止,关于VISA信号复合物中的蛋白组成,以及这些蛋白在复合物的形成及信号转导过程中所发挥的作用还不完全清楚。为了进一步探明VISA信号复合物的潜在成员及其在抗病毒信号通路中的功能,我们用串联亲和纯化的方法筛选了可能与VISA相互作用的蛋白。通过筛选,我们得到了一个与VISA特异性相互作用的蛋白WDR5 (WD repeat 5)。我们的研究结果显示,内源性WDR5与VISA之间的相互作用依赖于病毒感染。病毒感染细胞后,WDR5转移到线粒体上,与线粒体外膜上的VISA相互作用。利用RNAi干扰技术降低细胞内WDR5的表达能够阻碍病毒诱导的VISA信号复合物的装配。同时,降低WDR5的表达量还会抑制病毒诱导的IRF3和NF-κB的激活,以及IFNB1基因的转录。综上所述,这些发现表明WDR5在VISA信号复合物的装配过程中至关重要,同时在病毒诱导Ⅰ型干扰素产生的过程中发挥重要作用。该项研究增加了对抗病毒天然免疫信号转导分子机制的了解。
Viral infection could be detected by the pattern recognition receptors of the innate immune system, leading to activation of signaling transduction, results in activation of the transcription factors NF-κB and IRF3. These transcription factors collaborate to induce typeⅠinterferons (IFNs). TypeⅠinterferons further induce expression of the Anti-Viral Proteins. AVPs inhibit viral replication as well as induce the apoptosis of infected cells, therefore mediate cellular antiviral response. It is well admitted that the typeⅠinterferons play a very important role in antiviral immunity.
Recent studies have demonstrated that, RIG-I and MDA5, two cytosolic PRRs, specifically detect viral RNAs that are produced during viral replication. Binding of RIG-I/MDA5 to viral RNA leads to recruitment of a downstream adaptor protein VISA. The mitochondrial outer membrane protein VISA acts as a critical adapter for assembling a virus-induced complex that signals NF-κB and IRF3 activation. However, the components of the VISA-associated complex and their roles in antiviral response are not fully understood yet.
Using a biochemical purification approach, we identified the WD repeat protein WDR5 as a VISA-associated protein. WDR5 was recruited to VISA in a viral infection dependent manner. Viral infection also caused translocation of WDR5 from the nucleus to mitochondria. Knockdown of WDR5 impaired the formation of virus-induced VISA-associated complex. Consistently, knockdown of WDR5 inhibited virus-triggered activation of IRF3 and NF-κB as well as transcription of the IFNB1 gene. These findings suggest that WDR5 is essential in assembling a virus-induced VISA-associated complex and plays an important role in virus-triggered induction of typeⅠIFNs.
引文
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