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1
Point mutations in the herpes simplex virus type 1 Vmw110 RING finger helix affect activation of gene expression, viral growth, and interaction with PML-containing nuclear structures.单纯疱疹病毒1型Vmw110环指螺旋中的点突变影响基因表达的激活、病毒生长以及与含早幼粒细胞白血病蛋白的核结构的相互作用。
J Virol. 1995 Nov;69(11):7339-44. doi: 10.1128/JVI.69.11.7339-7344.1995.
2
The cellular RING finger protein PML is not a functional counterpart of the herpes simplex virus type 1 RING finger protein Vmw110.细胞环状结构域蛋白PML不是单纯疱疹病毒1型环状结构域蛋白Vmw110的功能对应物。
J Gen Virol. 1995 Apr;76 ( Pt 4):791-8. doi: 10.1099/0022-1317-76-4-791.
3
A novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory protein.一种新型泛素特异性蛋白酶与早幼粒细胞白血病（PML）核体动态相关，并与一种疱疹病毒调节蛋白结合。
EMBO J. 1997 Apr 1;16(7):1519-30. doi: 10.1093/emboj/16.7.1519.
4
A novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory protein.一种新型泛素特异性蛋白酶与早幼粒细胞白血病（PML）核体动态相关，并与一种疱疹病毒调节蛋白结合。
EMBO J. 1997 Feb 3;16(3):566-77. doi: 10.1093/emboj/16.3.566.
5
HSV-1 IE protein Vmw110 causes redistribution of PML.单纯疱疹病毒1型即刻早期蛋白Vmw110导致早幼粒细胞白血病蛋白的重新分布。
EMBO J. 1994 Nov 1;13(21):5062-9. doi: 10.1002/j.1460-2075.1994.tb06835.x.
6
Alphaherpesvirus proteins related to herpes simplex virus type 1 ICP0 affect cellular structures and proteins.与单纯疱疹病毒1型ICP0相关的α疱疹病毒蛋白会影响细胞结构和蛋白质。
J Virol. 2000 Nov;74(21):10006-17. doi: 10.1128/jvi.74.21.10006-10017.2000.
7
Separation of sequence requirements for HSV-1 Vmw110 multimerisation and interaction with a 135-kDa cellular protein.单纯疱疹病毒1型Vmw110多聚化及与一种135 kDa细胞蛋白相互作用的序列要求的分离
Virology. 1995 May 10;209(1):174-87. doi: 10.1006/viro.1995.1241.
8
The disruption of ND10 during herpes simplex virus infection correlates with the Vmw110- and proteasome-dependent loss of several PML isoforms.单纯疱疹病毒感染期间ND10的破坏与几种PML亚型的Vmw110和蛋白酶体依赖性缺失相关。
J Virol. 1998 Aug;72(8):6581-91. doi: 10.1128/JVI.72.8.6581-6591.1998.
9
The nuclear location of PML, a cellular member of the C3HC4 zinc-binding domain protein family, is rearranged during herpes simplex virus infection by the C3HC4 viral protein ICP0.PML是C3HC4锌结合结构域蛋白家族的一个细胞成员，其核定位在单纯疱疹病毒感染期间被C3HC4病毒蛋白ICP0重新排列。
J Gen Virol. 1994 Jun;75 ( Pt 6):1223-33. doi: 10.1099/0022-1317-75-6-1223.
10
Sequences related to SUMO interaction motifs in herpes simplex virus 1 protein ICP0 act cooperatively to stimulate virus infection.单纯疱疹病毒1型蛋白ICP0中与小泛素样修饰蛋白相互作用基序相关的序列协同作用以刺激病毒感染。
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1
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2
Advancing Our Understanding of Corneal Herpes Simplex Virus-1 Immune Evasion Mechanisms and Future Therapeutics.深入了解单纯疱疹病毒-1 角膜免疫逃逸机制和未来的治疗方法。
Viruses. 2021 Sep 17;13(9):1856. doi: 10.3390/v13091856.
3
Herpes simplex virus 1 targets IRF7 via ICP0 to limit type I IFN induction.单纯疱疹病毒 1 通过 ICP0 靶向 IRF7 以限制 I 型 IFN 的诱导。
Sci Rep. 2020 Dec 17;10(1):22216. doi: 10.1038/s41598-020-77725-4.
4
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J Virol. 2018 Nov 12;92(23). doi: 10.1128/JVI.01452-18. Print 2018 Dec 1.
5
Interaction between the cellular E3 ubiquitin ligase SIAH-1 and the viral immediate-early protein ICP0 enables efficient replication of Herpes Simplex Virus type 2 in vivo.细胞 E3 泛素连接酶 SIAH-1 与病毒早期即刻蛋白 ICP0 的相互作用使单纯疱疹病毒 2 能够在体内有效地复制。
PLoS One. 2018 Aug 6;13(8):e0201880. doi: 10.1371/journal.pone.0201880. eCollection 2018.
6
Spatial and Temporal Resolution of Global Protein Synthesis during HSV Infection Using Bioorthogonal Precursors and Click Chemistry.使用生物正交前体和点击化学技术对单纯疱疹病毒感染期间全球蛋白质合成的时空分辨率研究
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7
A Tale of Two PMLs: Elements Regulating a Differential Substrate Recognition by the ICP0 E3 Ubiquitin Ligase of Herpes Simplex Virus 1.两种进行性多灶性白质脑病的故事：调控单纯疱疹病毒1的ICP0 E3泛素连接酶对不同底物识别的因素
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8
Infected cell protein 0 functional domains and their coordination in herpes simplex virus replication.单纯疱疹病毒复制中感染细胞蛋白0的功能结构域及其协同作用
World J Virol. 2016 Feb 12;5(1):1-13. doi: 10.5501/wjv.v5.i1.1.
9
Regulation and function of phosphorylation on VP8, the major tegument protein of bovine herpesvirus 1.牛疱疹病毒1主要被膜蛋白VP8磷酸化的调控与功能
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10
Bovine Herpes Virus 1 (BHV-1) and Herpes Simplex Virus Type 1 (HSV-1) Promote Survival of Latently Infected Sensory Neurons, in Part by Inhibiting Apoptosis.牛疱疹病毒1型（BHV-1）和单纯疱疹病毒1型（HSV-1）部分通过抑制细胞凋亡促进潜伏感染感觉神经元的存活。
J Cell Death. 2013 Apr 9;6:1-16. doi: 10.4137/JCD.S10803. eCollection 2013.

本文引用的文献

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The RR1 gene of herpes simplex virus type 1 is uniquely trans activated by ICP0 during infection.单纯疱疹病毒1型的RR1基因在感染期间由ICP0独特地反式激活。
J Virol. 1993 Oct;67(10):6125-35. doi: 10.1128/JVI.67.10.6125-6135.1993.
2
The RING finger. A novel protein sequence motif related to the zinc finger.环状结构域。一种与锌指结构相关的新型蛋白质序列基序。
Ann N Y Acad Sci. 1993 Jun 11;684:174-92. doi: 10.1111/j.1749-6632.1993.tb32280.x.
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Retinoic acid regulates aberrant nuclear localization of PML-RAR alpha in acute promyelocytic leukemia cells.维甲酸调节急性早幼粒细胞白血病细胞中PML-RARα的异常核定位。
Cell. 1994 Jan 28;76(2):345-56. doi: 10.1016/0092-8674(94)90341-7.
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A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein.一种新型大分子结构是早幼粒细胞-视黄酸受体癌蛋白的作用靶点。
Cell. 1994 Jan 28;76(2):333-43. doi: 10.1016/0092-8674(94)90340-9.
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Modification of discrete nuclear domains induced by herpes simplex virus type 1 immediate early gene 1 product (ICP0).单纯疱疹病毒1型立即早期基因1产物（ICP0）诱导的离散核结构域的修饰。
J Gen Virol. 1993 Dec;74 ( Pt 12):2679-90. doi: 10.1099/0022-1317-74-12-2679.
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A novel arrangement of zinc-binding residues and secondary structure in the C3HC4 motif of an alpha herpes virus protein family.α疱疹病毒蛋白家族C3HC4基序中锌结合残基和二级结构的一种新排列
J Mol Biol. 1993 Dec 20;234(4):1038-47. doi: 10.1006/jmbi.1993.1657.
7
The herpes simplex virus type 1 regulatory protein ICP0 enhances virus replication during acute infection and reactivation from latency.单纯疱疹病毒1型调节蛋白ICP0在急性感染和潜伏激活过程中增强病毒复制。
J Virol. 1993 Dec;67(12):7501-12. doi: 10.1128/JVI.67.12.7501-7512.1993.
8
The nuclear location of PML, a cellular member of the C3HC4 zinc-binding domain protein family, is rearranged during herpes simplex virus infection by the C3HC4 viral protein ICP0.PML是C3HC4锌结合结构域蛋白家族的一个细胞成员，其核定位在单纯疱疹病毒感染期间被C3HC4病毒蛋白ICP0重新排列。
J Gen Virol. 1994 Jun;75 ( Pt 6):1223-33. doi: 10.1099/0022-1317-75-6-1223.
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The t(15;17) translocation alters a nuclear body in a retinoic acid-reversible fashion.t(15;17)易位以视黄酸可逆的方式改变一个核体。
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单纯疱疹病毒1型Vmw110环指螺旋中的点突变影响基因表达的激活、病毒生长以及与含早幼粒细胞白血病蛋白的核结构的相互作用。

Point mutations in the herpes simplex virus type 1 Vmw110 RING finger helix affect activation of gene expression, viral growth, and interaction with PML-containing nuclear structures.

作者信息

Everett R, O'Hare P, O'Rourke D, Barlow P, Orr A

机构信息

Medical Research Council Virology Unit, Glasgow, Scotland.

出版信息

J Virol. 1995 Nov;69(11):7339-44. doi: 10.1128/JVI.69.11.7339-7344.1995.

DOI:10.1128/JVI.69.11.7339-7344.1995
PMID:7474166
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC189666/
Abstract

Herpes simplex virus type 1 immediate-early protein Vmw110 (also known as ICP0) has been implicated in the control of the balance between the lytic and latent states, but the precise mechanisms by which it exerts its effects are unknown. Vmw110 includes a characteristic zinc binding domain, termed the C3HC4 domain or RING finger, which is essential for its function. The solution structure of a related herpesvirus RING finger domain suggested that an amphipathic alpha helix might be an important functional component of the RING finger. In this paper, we show that the equivalent region of Vmw110 is important for virus growth in tissue culture and for the normal interaction of Vmw110 with nuclear structures which include the PML protein.

摘要

单纯疱疹病毒I型立即早期蛋白Vmw110（也称为ICP0）与裂解状态和潜伏状态之间平衡的控制有关，但其发挥作用的确切机制尚不清楚。Vmw110包含一个特征性的锌结合结构域，称为C3HC4结构域或环指结构域，这对其功能至关重要。一种相关疱疹病毒环指结构域的溶液结构表明，两亲性α螺旋可能是环指结构域的重要功能成分。在本文中，我们表明Vmw110的等效区域对于病毒在组织培养中的生长以及Vmw110与包括PML蛋白在内的核结构的正常相互作用很重要。