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N 端乙酰转移酶 6 通过调节 PI4KB 的表达和复制细胞器的生物发生促进肠道病毒 71 型的复制。

N-terminal acetyltransferase 6 facilitates enterovirus 71 replication by regulating PI4KB expression and replication organelle biogenesis.

作者信息

Yang Hang, Fan Tingting, Xun Meng, Wu Bo, Guo Shangrui, Li Xinyu, Zhao Xiaohui, Yao Haoyan, Wang Hongliang

机构信息

Department of Pathogen Biology and Immunology, Xi'an Jiaotong University Health Science Center, Xi'an, China.

Department of Gynecology and Obstetrics, The First Affiliated Hospital of Xi'an Jiaotong University, Xi'an, China.

出版信息

J Virol. 2024 Feb 20;98(2):e0174923. doi: 10.1128/jvi.01749-23. Epub 2024 Jan 8.

Abstract

Enterovirus 71 (EV71) is one of the major pathogens causing hand, foot, and mouth disease in children under 5 years old, which can result in severe neurological complications and even death. Due to limited treatments for EV71 infection, the identification of novel host factors and elucidation of mechanisms involved will help to counter this viral infection. N-terminal acetyltransferase 6 (NAT6) was identified as an essential host factor for EV71 infection with genome-wide CRISPR/Cas9 screening. NAT6 facilitates EV71 viral replication depending on its acetyltransferase activity but has little effect on viral release. In addition, NAT6 is also required for Echovirus 7 and coxsackievirus B5 infection, suggesting it might be a pan-enterovirus host factor. We further demonstrated that NAT6 is required for Golgi integrity and viral replication organelle (RO) biogenesis. NAT6 knockout significantly inhibited phosphatidylinositol 4-kinase IIIβ (PI4KB) expression and PI4P production, both of which are key host factors for enterovirus infection and RO biogenesis. Further mechanism studies confirmed that NAT6 formed a complex with its substrate actin and one of the PI4KB recruiters-acyl-coenzyme A binding domain containing 3 (ACBD3). Through modulating actin dynamics, NAT6 maintained the integrity of the Golgi and the stability of ACBD3, thereby enhancing EV71 infection. Collectively, these results uncovered a novel mechanism of N-acetyltransferase supporting EV71 infection.IMPORTANCEEnterovirus 71 (EV71) is an important pathogen for children under the age of five, and currently, no effective treatment is available. Elucidating the mechanism of novel host factors supporting viral infection will reveal potential antiviral targets and aid antiviral development. Here, we demonstrated that a novel N-acetyltransferase, NAT6, is an essential host factor for EV71 replication. NAT6 could promote viral replication organelle (RO) formation to enhance viral replication. The formation of enterovirus ROs requires numerous host factors, including acyl-coenzyme A binding domain containing 3 (ACBD3) and phosphatidylinositol 4-kinase IIIβ (PI4KB). NAT6 could stabilize the PI4KB recruiter, ACBD3, by inhibiting the autophagy degradation pathway. This study provides a fresh insight into the relationship between N-acetyltransferase and viral infection.

摘要

肠道病毒71型(EV71)是导致5岁以下儿童手足口病的主要病原体之一,可引发严重的神经并发症甚至死亡。由于针对EV71感染的治疗方法有限,鉴定新的宿主因子并阐明其相关机制将有助于对抗这种病毒感染。通过全基因组CRISPR/Cas9筛选,N-末端乙酰转移酶6(NAT6)被鉴定为EV71感染所必需的宿主因子。NAT6依赖其乙酰转移酶活性促进EV71病毒复制,但对病毒释放影响不大。此外,NAT6也是埃可病毒7型和柯萨奇病毒B5感染所必需的,这表明它可能是一种泛肠道病毒宿主因子。我们进一步证明,NAT6是高尔基体完整性和病毒复制细胞器(RO)生物发生所必需的。NAT6基因敲除显著抑制磷脂酰肌醇4激酶IIIβ(PI4KB)的表达和PI4P的产生,这两者都是肠道病毒感染和RO生物发生的关键宿主因子。进一步的机制研究证实,NAT6与其底物肌动蛋白以及PI4KB募集因子之一——含酰基辅酶A结合结构域3(ACBD3)形成复合物。通过调节肌动蛋白动力学,NAT6维持高尔基体的完整性和ACBD3的稳定性,从而增强EV71感染。总的来说,这些结果揭示了N-乙酰转移酶支持EV71感染的新机制。

重要性

肠道病毒71型(EV71)是5岁以下儿童的重要病原体,目前尚无有效的治疗方法。阐明支持病毒感染的新宿主因子的机制将揭示潜在的抗病毒靶点并有助于抗病毒药物的研发。在此,我们证明了一种新的N-乙酰转移酶NAT6是EV71复制所必需的宿主因子。NAT能促进病毒复制细胞器(RO)的形成以增强病毒复制。肠道病毒RO的形成需要多种宿主因子,包括含酰基辅酶A结合结构域3(ACBD3)和磷脂酰肌醇4激酶IIIβ(PI4KB)。NAT6可通过抑制自噬降解途径来稳定PI4KB募集因子ACBD3。本研究为N-乙酰转移酶与病毒感染之间的关系提供了新的见解。

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