Gammaherpesviral Tegument Proteins, PML-Nuclear Bodies and the Ubiquitin-Proteasome System

被引：7

作者：

Full, Florian ^{[1
]}

Hahn, Alexander S. ^{[2
]}

Grosskopf, Anna K. ^{[2
]}

Ensser, Armin ^{[1
]}

机构：

[1] Friedrich Alexander Univ Erlangen Nuremberg, Univ Hosp Erlangen, Inst Clin & Mol Virol, D-91054 Erlangen, Germany

[2] Deutsch Primatenzentrum Leibniz Inst Primatenfors, Nachwuchsgruppe Herpesviren, D-37077 Gottingen, Germany

来源：

VIRUSES-BASEL | 2017年 / 9卷 / 10期

关键词：

Gammaherpesvirus; Epstein-Barr virus; Kaposi's sarcoma-associated herpesvirus; KSHV; EBV; viral FGARAT; PML nuclear bodies; ubiquitin; proteasome; deubiquitinating enzyme; SARCOMA-ASSOCIATED HERPESVIRUS; DEUBIQUITINATING ENZYME; HUMAN CYTOMEGALOVIRUS; ONCOGENIC DOMAINS; DNA-REPLICATION; RIG-I; VIRUS; DEGRADATION; BPLF1; ND10;

D O I：

10.3390/v9100308

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Gammaherpesviruses like Epstein-Barr virus (EBV) and Kaposi's sarcoma-associated herpesvirus (KSHV) subvert the ubiquitin proteasome system for their own benefit in order to facilitate viral gene expression and replication. In particular, viral tegument proteins that share sequence homology to the formylglycineamide ribonucleotide amidotransferase (FGARAT, or PFAS), an enzyme in the cellular purine biosynthesis, are important for disrupting the intrinsic antiviral response associated with Promyelocytic Leukemia (PML) protein-associated nuclear bodies (PML-NBs) by proteasome-dependent and independent mechanisms. In addition, all herpesviruses encode for a potent ubiquitin protease that can efficiently remove ubiquitin chains from proteins and thereby interfere with several different cellular pathways. In this review, we discuss mechanisms and functional consequences of virus-induced ubiquitination and deubiquitination for early events in gammaherpesviral infection.

引用

页数：11

共 63 条

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