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Published in: Virology Journal 1/2020

01-12-2020 | Herpes Virus | Review

Host shutoff activity of VHS and SOX-like proteins: role in viral survival and immune evasion

Authors: Tianqiong He, Mingshu Wang, Anchun Cheng, Qiao Yang, Ying Wu, Renyong Jia, Mafeng Liu, Dekang Zhu, Shun Chen, Shaqiu Zhang, Xin-Xin Zhao, Juan Huang, Di Sun, Sai Mao, Xuming Ou, Yin Wang, Zhiwen Xu, Zhengli Chen, Lin Zhu, Qihui Luo, Yunya Liu, Yanling Yu, Ling Zhang, Bin Tian, Leichang Pan, Mujeeb Ur Rehman, Xiaoyue Chen

Published in: Virology Journal | Issue 1/2020

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Abstract

Background

Host shutoff refers to the widespread downregulation of host gene expression and has emerged as a key process that facilitates the reallocation of cellular resources for viral replication and evasion of host antiviral immune responses.

Main body

The Herpesviridae family uses a number of proteins that are responsible for host shutoff by directly targeting messenger RNA (mRNA), including virion host shutoff (VHS) protein and the immediate-early regulatory protein ICP27 of herpes simplex virus types 1 (HSV-1) and the SOX (shutoff and exonuclease) protein and its homologs in Gammaherpesvirinae subfamilies, although these proteins are not homologous. In this review, we highlight evidence that host shutoff is promoted by the VHS, ICP27 and SOX-like proteins and that they also contribute to immune evasion.

Conclusions

Further studies regarding the host shutoff proteins will not only contribute to provide new insights into the viral replication, expression and host immune evasion process, but also provide new molecular targets for the development of antiviral drugs and therapies.
Literature
1.
go back to reference Xie Y, Wu L, Wang M, Cheng A, Yang Q, Wu Y, et al. Alpha-Herpesvirus thymidine kinase genes mediate viral virulence and are potential therapeutic targets. Front Microbiol. 2019;10:941.PubMedPubMedCentralCrossRef Xie Y, Wu L, Wang M, Cheng A, Yang Q, Wu Y, et al. Alpha-Herpesvirus thymidine kinase genes mediate viral virulence and are potential therapeutic targets. Front Microbiol. 2019;10:941.PubMedPubMedCentralCrossRef
2.
go back to reference Osterrieder K. Cell biology of herpes Viruse. Germany: Springer International Publishing; 2017. p. 1–18.CrossRef Osterrieder K. Cell biology of herpes Viruse. Germany: Springer International Publishing; 2017. p. 1–18.CrossRef
3.
go back to reference Agut H, Bonnafous P, Gautheret-Dejean A. Update on infections with human herpesviruses 6A, 6B, and 7. Med Mal Infect. 2017;47:83–91.PubMedCrossRef Agut H, Bonnafous P, Gautheret-Dejean A. Update on infections with human herpesviruses 6A, 6B, and 7. Med Mal Infect. 2017;47:83–91.PubMedCrossRef
4.
go back to reference Foulon T. Herpesviridae: classification and structure in 1991. Comp Immunol Microbiol Infect Dis. 1992;1:13–29.CrossRef Foulon T. Herpesviridae: classification and structure in 1991. Comp Immunol Microbiol Infect Dis. 1992;1:13–29.CrossRef
5.
go back to reference Suazo PA, Ibanez FJ, Retamal-Diaz AR, Paz-Fiblas MV, Bueno SM, Kalergis AM, et al. Evasion of early antiviral responses by herpes simplex viruses. Mediat Inflamm. 2015;2015:593757.CrossRef Suazo PA, Ibanez FJ, Retamal-Diaz AR, Paz-Fiblas MV, Bueno SM, Kalergis AM, et al. Evasion of early antiviral responses by herpes simplex viruses. Mediat Inflamm. 2015;2015:593757.CrossRef
6.
go back to reference Read GS. Virus-encoded endonucleases: expected and novel functions. Wiley Interdiscip Rev RNA. 2013;4:693–708.PubMedCrossRef Read GS. Virus-encoded endonucleases: expected and novel functions. Wiley Interdiscip Rev RNA. 2013;4:693–708.PubMedCrossRef
7.
go back to reference Glaunsinger B, Ganem D. Lytic KSHV infection inhibits host gene expression by accelerating global mRNA turnover. Mol Cell. 2004;13:0–723.CrossRef Glaunsinger B, Ganem D. Lytic KSHV infection inhibits host gene expression by accelerating global mRNA turnover. Mol Cell. 2004;13:0–723.CrossRef
8.
go back to reference Covarrubias S, Richner JM, Clyde K, Lee YJ, Glaunsinger BA. Host shutoff is a conserved phenotype of gammaherpesvirus infection and is orchestrated exclusively from the cytoplasm. J Virol. 2009;83:9554–66.PubMedPubMedCentralCrossRef Covarrubias S, Richner JM, Clyde K, Lee YJ, Glaunsinger BA. Host shutoff is a conserved phenotype of gammaherpesvirus infection and is orchestrated exclusively from the cytoplasm. J Virol. 2009;83:9554–66.PubMedPubMedCentralCrossRef
9.
go back to reference Narayanan K, Ramirez SI, Lokugamage KG, Makino S. Coronavirus nonstructural protein 1: common and distinct functions in the regulation of host and viral gene expression. Virus Res. 2015;202:89–100.PubMedCrossRef Narayanan K, Ramirez SI, Lokugamage KG, Makino S. Coronavirus nonstructural protein 1: common and distinct functions in the regulation of host and viral gene expression. Virus Res. 2015;202:89–100.PubMedCrossRef
11.
go back to reference Rivas HG, Schmaling SK, Gaglia MM. Shutoff of host gene expression in influenza a virus and Herpesviruses: similar mechanisms and common themes. Viruses. 2016;8:102.PubMedPubMedCentralCrossRef Rivas HG, Schmaling SK, Gaglia MM. Shutoff of host gene expression in influenza a virus and Herpesviruses: similar mechanisms and common themes. Viruses. 2016;8:102.PubMedPubMedCentralCrossRef
12.
13.
go back to reference Hardwicke MA, Sandri-Goldin RM. The herpes simplex virus regulatory protein ICP27 contributes to the decrease in cellular mRNA levels during infection. J Virol. 1994;68:4797–810.PubMedPubMedCentralCrossRef Hardwicke MA, Sandri-Goldin RM. The herpes simplex virus regulatory protein ICP27 contributes to the decrease in cellular mRNA levels during infection. J Virol. 1994;68:4797–810.PubMedPubMedCentralCrossRef
14.
go back to reference Patel V, Dahlroth SL, Rajakannan V, Ho HT, Cornvik T, Nordlund P. Structure of the C-terminal domain of the multifunctional ICP27 protein from herpes simplex virus 1. J Virol. 2015;89:8828–39.PubMedPubMedCentralCrossRef Patel V, Dahlroth SL, Rajakannan V, Ho HT, Cornvik T, Nordlund P. Structure of the C-terminal domain of the multifunctional ICP27 protein from herpes simplex virus 1. J Virol. 2015;89:8828–39.PubMedPubMedCentralCrossRef
15.
go back to reference Zhu H, Cong J-P, Mamtora G, Gingeras T, Shenk T. Cellular gene expression altered by human cytomegalovirus: global monitoring with oligonucleotide arrays. Proc Natl Acad Sci. 1998;95:14470–5.PubMedCrossRef Zhu H, Cong J-P, Mamtora G, Gingeras T, Shenk T. Cellular gene expression altered by human cytomegalovirus: global monitoring with oligonucleotide arrays. Proc Natl Acad Sci. 1998;95:14470–5.PubMedCrossRef
17.
go back to reference Taddeo B, Roizman B. The virion host shutoff protein (UL41) of herpes simplex virus 1 is an endoribonuclease with a substrate specificity similar to that of RNase a. J Virol. 2006;80:9341–5.PubMedPubMedCentralCrossRef Taddeo B, Roizman B. The virion host shutoff protein (UL41) of herpes simplex virus 1 is an endoribonuclease with a substrate specificity similar to that of RNase a. J Virol. 2006;80:9341–5.PubMedPubMedCentralCrossRef
18.
go back to reference Lin HW, Hsu WL, Chang YY, Jan MS, Wong ML, Chang TJ. Role of the UL41 protein of pseudorabies virus in host shutoff, pathogenesis and induction of TNF-α expression. J Vet Med Sci. 2010;72:1179–87.PubMedCrossRef Lin HW, Hsu WL, Chang YY, Jan MS, Wong ML, Chang TJ. Role of the UL41 protein of pseudorabies virus in host shutoff, pathogenesis and induction of TNF-α expression. J Vet Med Sci. 2010;72:1179–87.PubMedCrossRef
19.
go back to reference Desloges N, Rahaus M, Wolff MH. The varicella-zoster virus-mediated delayed host shutoff: open reading frame 17 has no major function, whereas immediate-early 63 protein represses heterologous gene expression. Microbes Infect. 2005;7:1519–29.PubMedCrossRef Desloges N, Rahaus M, Wolff MH. The varicella-zoster virus-mediated delayed host shutoff: open reading frame 17 has no major function, whereas immediate-early 63 protein represses heterologous gene expression. Microbes Infect. 2005;7:1519–29.PubMedCrossRef
20.
go back to reference Sato H, Callanan LD, Pesnicak L, Krogmann T, Cohen JI. Varicella-zoster virus (VZV) ORF17 protein induces RNA cleavage and is critical for replication of VZV at 37 degrees C but not 33 degrees C. J Virol. 2002;76:11012–23.PubMedPubMedCentralCrossRef Sato H, Callanan LD, Pesnicak L, Krogmann T, Cohen JI. Varicella-zoster virus (VZV) ORF17 protein induces RNA cleavage and is critical for replication of VZV at 37 degrees C but not 33 degrees C. J Virol. 2002;76:11012–23.PubMedPubMedCentralCrossRef
21.
go back to reference Dauber B, Saffran HA, Smiley JR. The herpes simplex virus host shutoff (vhs) RNase limits accumulation of double stranded RNA in infected cells: evidence for accelerated decay of duplex RNA. PLoS Pathog. 2019;15:e1008111.PubMedPubMedCentralCrossRef Dauber B, Saffran HA, Smiley JR. The herpes simplex virus host shutoff (vhs) RNase limits accumulation of double stranded RNA in infected cells: evidence for accelerated decay of duplex RNA. PLoS Pathog. 2019;15:e1008111.PubMedPubMedCentralCrossRef
22.
go back to reference Sandri-Goldin RM. The many roles of the highly interactive HSV protein ICP27, a key regulator of infection. Future Microbiol. 2011;6:1261–77.PubMedCrossRef Sandri-Goldin RM. The many roles of the highly interactive HSV protein ICP27, a key regulator of infection. Future Microbiol. 2011;6:1261–77.PubMedCrossRef
23.
go back to reference Tang S, Patel A, Krause PR. Hidden regulation of herpes simplex virus 1 pre-mRNA splicing and polyadenylation by virally encoded immediate early gene ICP27. PLoS Pathog. 2019;15:e1007884.PubMedPubMedCentralCrossRef Tang S, Patel A, Krause PR. Hidden regulation of herpes simplex virus 1 pre-mRNA splicing and polyadenylation by virally encoded immediate early gene ICP27. PLoS Pathog. 2019;15:e1007884.PubMedPubMedCentralCrossRef
24.
go back to reference Tunnicliffe RB, Hu WK, Wu MY, Levy C, Mould AP, McKenzie EA, et al. Molecular mechanism of SR protein kinase 1 inhibition by the herpes virus protein ICP27. mBio. 2019;10:e02551–19.PubMedPubMedCentralCrossRef Tunnicliffe RB, Hu WK, Wu MY, Levy C, Mould AP, McKenzie EA, et al. Molecular mechanism of SR protein kinase 1 inhibition by the herpes virus protein ICP27. mBio. 2019;10:e02551–19.PubMedPubMedCentralCrossRef
25.
go back to reference Tang S, Patel A, Krause PR. Herpes simplex virus ICP27 regulates alternative pre-mRNA polyadenylation and splicing in a sequence-dependent manner. Proc Natl Acad Sci U S A. 2016;113:12256.PubMedPubMedCentralCrossRef Tang S, Patel A, Krause PR. Herpes simplex virus ICP27 regulates alternative pre-mRNA polyadenylation and splicing in a sequence-dependent manner. Proc Natl Acad Sci U S A. 2016;113:12256.PubMedPubMedCentralCrossRef
26.
go back to reference Rutkowski AJ, Erhard F, L'Hernault A, Bonfert T, Schilhabel M, Crump C, et al. Widespread disruption of host transcription termination in HSV-1 infection. Nat Commun. 2015;6:7126.PubMedPubMedCentralCrossRef Rutkowski AJ, Erhard F, L'Hernault A, Bonfert T, Schilhabel M, Crump C, et al. Widespread disruption of host transcription termination in HSV-1 infection. Nat Commun. 2015;6:7126.PubMedPubMedCentralCrossRef
27.
go back to reference Wang X, Hennig T, Whisnant AW, Erhard F, Prusty BK, Friedel CC, et al. Herpes simplex virus blocks host transcription termination via the bimodal activities of ICP27. Nat Commun. 2020;11:293.PubMedPubMedCentralCrossRef Wang X, Hennig T, Whisnant AW, Erhard F, Prusty BK, Friedel CC, et al. Herpes simplex virus blocks host transcription termination via the bimodal activities of ICP27. Nat Commun. 2020;11:293.PubMedPubMedCentralCrossRef
28.
go back to reference Rowe M, Glaunsinger B, Leeuwen DV, Zuo J, Sweetman D, Ganem D, et al. Host shutoff during productive Epstein-Barr virus infection is mediated by BGLF5 and may contribute to immune evasion. Proc Natl Acad Sci U S A. 2007;104:3366–71.PubMedPubMedCentralCrossRef Rowe M, Glaunsinger B, Leeuwen DV, Zuo J, Sweetman D, Ganem D, et al. Host shutoff during productive Epstein-Barr virus infection is mediated by BGLF5 and may contribute to immune evasion. Proc Natl Acad Sci U S A. 2007;104:3366–71.PubMedPubMedCentralCrossRef
29.
go back to reference Gaglia MM, Rycroft CH, Glaunsinger BA. Transcriptome-wide cleavage site mapping on cellular mRNAs reveals features underlying sequence-specific cleavage by the viral Ribonuclease SOX. PLoS Pathog. 2015;11:e1005305.PubMedPubMedCentralCrossRef Gaglia MM, Rycroft CH, Glaunsinger BA. Transcriptome-wide cleavage site mapping on cellular mRNAs reveals features underlying sequence-specific cleavage by the viral Ribonuclease SOX. PLoS Pathog. 2015;11:e1005305.PubMedPubMedCentralCrossRef
30.
go back to reference Covarrubias S, Gaglia MM, Kumar GR, Wong W, Jackson AO, Glaunsinger BA. Coordinated destruction of cellular messages in translation complexes by the gammaherpesvirus host shutoff factor and the mammalian exonuclease Xrn1. PLoS Pathog. 2011;7:e1002339.PubMedPubMedCentralCrossRef Covarrubias S, Gaglia MM, Kumar GR, Wong W, Jackson AO, Glaunsinger BA. Coordinated destruction of cellular messages in translation complexes by the gammaherpesvirus host shutoff factor and the mammalian exonuclease Xrn1. PLoS Pathog. 2011;7:e1002339.PubMedPubMedCentralCrossRef
31.
go back to reference Glaunsinger B, Chavez L, Ganem D. The exonuclease and host shutoff functions of the SOX protein of Kaposi\s sarcoma-associated Herpesvirus are genetically separable. J Virol. 2005;79:7396–401.PubMedPubMedCentralCrossRef Glaunsinger B, Chavez L, Ganem D. The exonuclease and host shutoff functions of the SOX protein of Kaposi\s sarcoma-associated Herpesvirus are genetically separable. J Virol. 2005;79:7396–401.PubMedPubMedCentralCrossRef
32.
33.
go back to reference Abernathy E, Clyde K, Yeasmin R, Krug LT, Burlingame A, Coscoy L, et al. Gammaherpesviral gene expression and virion composition are broadly controlled by accelerated mRNA degradation. PLoS Pathog. 2014;10:e1003882.PubMedPubMedCentralCrossRef Abernathy E, Clyde K, Yeasmin R, Krug LT, Burlingame A, Coscoy L, et al. Gammaherpesviral gene expression and virion composition are broadly controlled by accelerated mRNA degradation. PLoS Pathog. 2014;10:e1003882.PubMedPubMedCentralCrossRef
34.
go back to reference Abernathy E, Glaunsinger B. Emerging roles for RNA degradation in viral replication and antiviral defense. Virology. 2015;479-480:600–8.PubMedCrossRef Abernathy E, Glaunsinger B. Emerging roles for RNA degradation in viral replication and antiviral defense. Virology. 2015;479-480:600–8.PubMedCrossRef
35.
go back to reference Feederle R, Bannert H, Lips H, Muller-Lantzsch N, Delecluse HJ. The Epstein-Barr virus alkaline exonuclease BGLF5 serves pleiotropic functions in virus replication. J Virol. 2009;83:4952–62.PubMedPubMedCentralCrossRef Feederle R, Bannert H, Lips H, Muller-Lantzsch N, Delecluse HJ. The Epstein-Barr virus alkaline exonuclease BGLF5 serves pleiotropic functions in virus replication. J Virol. 2009;83:4952–62.PubMedPubMedCentralCrossRef
36.
go back to reference Bagneris C, Briggs LC, Savva R, Ebrahimi B, Barrett TE. Crystal structure of a KSHV-SOX-DNA complex: insights into the molecular mechanisms underlying DNase activity and host shutoff. Nucleic Acids Res. 2011;39:5744–56.PubMedPubMedCentralCrossRef Bagneris C, Briggs LC, Savva R, Ebrahimi B, Barrett TE. Crystal structure of a KSHV-SOX-DNA complex: insights into the molecular mechanisms underlying DNase activity and host shutoff. Nucleic Acids Res. 2011;39:5744–56.PubMedPubMedCentralCrossRef
37.
go back to reference Muller M, Hutin S, Marigold O, Li KH, Burlingame A, Glaunsinger BA. A ribonucleoprotein complex protects the interleukin-6 mRNA from degradation by distinct herpesviral endonucleases. PLoS Pathog. 2015;11:e1004899.PubMedPubMedCentralCrossRef Muller M, Hutin S, Marigold O, Li KH, Burlingame A, Glaunsinger BA. A ribonucleoprotein complex protects the interleukin-6 mRNA from degradation by distinct herpesviral endonucleases. PLoS Pathog. 2015;11:e1004899.PubMedPubMedCentralCrossRef
38.
go back to reference Rodriguez W, Srivastav K, Muller M. C19ORF66 broadly escapes virus-induced endonuclease cleavage and restricts Kaposi's sarcoma-associated Herpesvirus. J Virol. 93:2019, e00373–e02019. Rodriguez W, Srivastav K, Muller M. C19ORF66 broadly escapes virus-induced endonuclease cleavage and restricts Kaposi's sarcoma-associated Herpesvirus. J Virol. 93:2019, e00373–e02019.
39.
go back to reference Muller M, Glaunsinger BA. Nuclease escape elements protect messenger RNA against cleavage by multiple viral endonucleases. PLoS Pathog. 2017;13:e1006593.PubMedPubMedCentralCrossRef Muller M, Glaunsinger BA. Nuclease escape elements protect messenger RNA against cleavage by multiple viral endonucleases. PLoS Pathog. 2017;13:e1006593.PubMedPubMedCentralCrossRef
40.
go back to reference Clyde K, Glaunsinger BA. Deep sequencing reveals direct targets of gammaherpesvirus-induced mRNA decay and suggests that multiple mechanisms govern cellular transcript escape. PLoS One. 2011;6:e19655.PubMedPubMedCentralCrossRef Clyde K, Glaunsinger BA. Deep sequencing reveals direct targets of gammaherpesvirus-induced mRNA decay and suggests that multiple mechanisms govern cellular transcript escape. PLoS One. 2011;6:e19655.PubMedPubMedCentralCrossRef
41.
go back to reference Esclatine A, Taddeo B, Evans L, Roizman B. The herpes simplex virus 1 UL41 gene-dependent destabilization of cellular RNAs is selective and may be sequence-specific. Proc Natl Acad Sci U S A. 2004;101:3603–8.PubMedPubMedCentralCrossRef Esclatine A, Taddeo B, Evans L, Roizman B. The herpes simplex virus 1 UL41 gene-dependent destabilization of cellular RNAs is selective and may be sequence-specific. Proc Natl Acad Sci U S A. 2004;101:3603–8.PubMedPubMedCentralCrossRef
43.
go back to reference Sciortino MT, Parisi T, Siracusano G, Mastino A, Taddeo B, Roizman B. The virion host shutoff RNase plays a key role in blocking the activation of protein kinase R in cells infected with herpes simplex virus 1. J Virol. 2013;87:3271–6.PubMedPubMedCentralCrossRef Sciortino MT, Parisi T, Siracusano G, Mastino A, Taddeo B, Roizman B. The virion host shutoff RNase plays a key role in blocking the activation of protein kinase R in cells infected with herpes simplex virus 1. J Virol. 2013;87:3271–6.PubMedPubMedCentralCrossRef
44.
go back to reference Pasieka TJ, Lu B, Crosby SD, Wylie KM, Morrison LA, Alexander DE, et al. Herpes simplex virus virion host shutoff attenuates establishment of the antiviral state. J Virol. 2008;82:5527–35.PubMedPubMedCentralCrossRef Pasieka TJ, Lu B, Crosby SD, Wylie KM, Morrison LA, Alexander DE, et al. Herpes simplex virus virion host shutoff attenuates establishment of the antiviral state. J Virol. 2008;82:5527–35.PubMedPubMedCentralCrossRef
45.
go back to reference Sharma NR, Majerciak V, Kruhlak MJ, Zheng ZM. KSHV inhibits stress granule formation by viral ORF57 blocking PKR activation. PLoS Pathog. 2017;13:e1006677.PubMedPubMedCentralCrossRef Sharma NR, Majerciak V, Kruhlak MJ, Zheng ZM. KSHV inhibits stress granule formation by viral ORF57 blocking PKR activation. PLoS Pathog. 2017;13:e1006677.PubMedPubMedCentralCrossRef
46.
go back to reference Feng P, Everly DN Jr, Read GS. mRNA decay during herpesvirus infections: interaction between a putative viral nuclease and a cellular translation factor. J Virol. 2001;75:10272–80.PubMedPubMedCentralCrossRef Feng P, Everly DN Jr, Read GS. mRNA decay during herpesvirus infections: interaction between a putative viral nuclease and a cellular translation factor. J Virol. 2001;75:10272–80.PubMedPubMedCentralCrossRef
47.
go back to reference Doepker RC, Hsu WL, Saffran HA, Smiley JR. Herpes simplex virus Virion host shutoff protein is stimulated by translation initiation factors eIF4B and eIF4H. J Virol. 2004;78:4684–99.PubMedPubMedCentralCrossRef Doepker RC, Hsu WL, Saffran HA, Smiley JR. Herpes simplex virus Virion host shutoff protein is stimulated by translation initiation factors eIF4B and eIF4H. J Virol. 2004;78:4684–99.PubMedPubMedCentralCrossRef
48.
go back to reference Sarma N, Agarwal D, Shiflett LA, Read GS. Small interfering RNAs that deplete the cellular translation factor eIF4H impede mRNA degradation by the virion host shutoff protein of herpes simplex virus. J Virol. 2008;82:6600–9.PubMedPubMedCentralCrossRef Sarma N, Agarwal D, Shiflett LA, Read GS. Small interfering RNAs that deplete the cellular translation factor eIF4H impede mRNA degradation by the virion host shutoff protein of herpes simplex virus. J Virol. 2008;82:6600–9.PubMedPubMedCentralCrossRef
49.
go back to reference Teo CSH, O'Hare P. A bimodal switch in global protein translation coupled to eIF4H relocalisation during advancing cell-cell transmission of herpes simplex virus. PLoS Pathog. 2018;14:e1007196.PubMedPubMedCentralCrossRef Teo CSH, O'Hare P. A bimodal switch in global protein translation coupled to eIF4H relocalisation during advancing cell-cell transmission of herpes simplex virus. PLoS Pathog. 2018;14:e1007196.PubMedPubMedCentralCrossRef
50.
go back to reference Page HG, Read GS. The virion host shutoff endonuclease (UL41) of herpes simplex virus interacts with the cellular cap-binding complex eIF4F. J Virol. 2010;84:6886–90.PubMedPubMedCentralCrossRef Page HG, Read GS. The virion host shutoff endonuclease (UL41) of herpes simplex virus interacts with the cellular cap-binding complex eIF4F. J Virol. 2010;84:6886–90.PubMedPubMedCentralCrossRef
51.
go back to reference Feng P, Everly DN Jr, Read GS. mRNA decay during herpes simplex virus (HSV) infections: protein-protein interactions involving the HSV virion host shutoff protein and translation factors eIF4H and eIF4A. J Virol. 2005;79:9651–64.PubMedPubMedCentralCrossRef Feng P, Everly DN Jr, Read GS. mRNA decay during herpes simplex virus (HSV) infections: protein-protein interactions involving the HSV virion host shutoff protein and translation factors eIF4H and eIF4A. J Virol. 2005;79:9651–64.PubMedPubMedCentralCrossRef
52.
go back to reference Shu M, Taddeo B, Roizman B. Tristetraprolin recruits the herpes simplex Virion host shutoff RNase to AU-rich elements in stress response mRNAs to enable their cleavage. J Virol. 2015;89:5643–50.PubMedPubMedCentralCrossRef Shu M, Taddeo B, Roizman B. Tristetraprolin recruits the herpes simplex Virion host shutoff RNase to AU-rich elements in stress response mRNAs to enable their cleavage. J Virol. 2015;89:5643–50.PubMedPubMedCentralCrossRef
53.
go back to reference Saffran HA, Read GS, Smiley JR. Evidence for translational regulation by the herpes simplex virus virion host shutoff protein. J Virol. 2010;84:6041–9.PubMedPubMedCentralCrossRef Saffran HA, Read GS, Smiley JR. Evidence for translational regulation by the herpes simplex virus virion host shutoff protein. J Virol. 2010;84:6041–9.PubMedPubMedCentralCrossRef
54.
go back to reference Wigington CP, Williams KR, Meers MP, Bassell GJ, Corbett AH. Poly(a) RNA-binding proteins and polyadenosine RNA: new members and novel functions. Wiley Interdiscip Rev RNA. 2014;5:601–22.PubMedPubMedCentralCrossRef Wigington CP, Williams KR, Meers MP, Bassell GJ, Corbett AH. Poly(a) RNA-binding proteins and polyadenosine RNA: new members and novel functions. Wiley Interdiscip Rev RNA. 2014;5:601–22.PubMedPubMedCentralCrossRef
55.
go back to reference Dobrikova E, Shveygert M, Walters R, Gromeier M. Herpes simplex virus proteins ICP27 and UL47 associate with polyadenylate-binding protein and control its subcellular distribution. J Virol. 2010;84:270–9.PubMedCrossRef Dobrikova E, Shveygert M, Walters R, Gromeier M. Herpes simplex virus proteins ICP27 and UL47 associate with polyadenylate-binding protein and control its subcellular distribution. J Virol. 2010;84:270–9.PubMedCrossRef
56.
go back to reference Salaun C, MacDonald AI, Larralde O, Howard L, Lochtie K, Burgess HM, et al. Poly(a)-binding protein 1 partially relocalizes to the nucleus during herpes simplex virus type 1 infection in an ICP27-independent manner and does not inhibit virus replication. J Virol. 84:2010, 8539–8548. Salaun C, MacDonald AI, Larralde O, Howard L, Lochtie K, Burgess HM, et al. Poly(a)-binding protein 1 partially relocalizes to the nucleus during herpes simplex virus type 1 infection in an ICP27-independent manner and does not inhibit virus replication. J Virol. 84:2010, 8539–8548.
57.
go back to reference Kumar GR, Glaunsinger BA. Nuclear import of cytoplasmic poly(a) binding protein restricts gene expression via hyperadenylation and nuclear retention of mRNA. Mol Cell Biol. 2010;30:4996–5008.PubMedPubMedCentralCrossRef Kumar GR, Glaunsinger BA. Nuclear import of cytoplasmic poly(a) binding protein restricts gene expression via hyperadenylation and nuclear retention of mRNA. Mol Cell Biol. 2010;30:4996–5008.PubMedPubMedCentralCrossRef
58.
go back to reference Rwp S, Anderson RC, Larralde O, et al. Viral and cellular mRNA-specific activators harness PABP and eIF4G to promote translation initiation downstream of cap binding. Proc Natl Acad Sci U S A. 2017;114:6310–5.CrossRef Rwp S, Anderson RC, Larralde O, et al. Viral and cellular mRNA-specific activators harness PABP and eIF4G to promote translation initiation downstream of cap binding. Proc Natl Acad Sci U S A. 2017;114:6310–5.CrossRef
59.
go back to reference Massimelli MJ, Majerciak V, Kruhlak M, Zheng ZM. Interplay between polyadenylate-binding protein 1 and Kaposi's sarcoma-associated herpesvirus ORF57 in accumulation of polyadenylated nuclear RNA, a viral long noncoding RNA. J Virol. 2013;87:243–56.PubMedPubMedCentralCrossRef Massimelli MJ, Majerciak V, Kruhlak M, Zheng ZM. Interplay between polyadenylate-binding protein 1 and Kaposi's sarcoma-associated herpesvirus ORF57 in accumulation of polyadenylated nuclear RNA, a viral long noncoding RNA. J Virol. 2013;87:243–56.PubMedPubMedCentralCrossRef
60.
go back to reference Horst D, Burmeister WP, Boer IG, van Leeuwen D, Buisson M, Gorbalenya AE, et al. The "bridge" in the Epstein-Barr virus alkaline exonuclease protein BGLF5 contributes to shutoff activity during productive infection. J Virol. 2012;86:9175–87.PubMedPubMedCentralCrossRef Horst D, Burmeister WP, Boer IG, van Leeuwen D, Buisson M, Gorbalenya AE, et al. The "bridge" in the Epstein-Barr virus alkaline exonuclease protein BGLF5 contributes to shutoff activity during productive infection. J Virol. 2012;86:9175–87.PubMedPubMedCentralCrossRef
61.
go back to reference Dauber B, Pelletier J, Smiley JR. The herpes simplex virus 1 vhs protein enhances translation of viral true late mRNAs and virus production in a cell type-dependent manner. J Virol. 2011;85:5363–73.PubMedPubMedCentralCrossRef Dauber B, Pelletier J, Smiley JR. The herpes simplex virus 1 vhs protein enhances translation of viral true late mRNAs and virus production in a cell type-dependent manner. J Virol. 2011;85:5363–73.PubMedPubMedCentralCrossRef
62.
go back to reference Dauber B, Poon D, Dos Santos T, Duguay BA, Mehta N, Saffran HA, et al. The herpes simplex virus Virion host shutoff protein enhances translation of viral true late mRNAs independently of suppressing protein kinase R and stress granule formation. J Virol. 2016;90:6049–57.PubMedPubMedCentralCrossRef Dauber B, Poon D, Dos Santos T, Duguay BA, Mehta N, Saffran HA, et al. The herpes simplex virus Virion host shutoff protein enhances translation of viral true late mRNAs independently of suppressing protein kinase R and stress granule formation. J Virol. 2016;90:6049–57.PubMedPubMedCentralCrossRef
63.
go back to reference Taddeo B, Zhang W, Roizman B. The herpes simplex virus host shutoff RNase degrades cellular and viral mRNAs made before infection but not viral mRNA made after infection. J Virol. 2013;87:4516–22.PubMedPubMedCentralCrossRef Taddeo B, Zhang W, Roizman B. The herpes simplex virus host shutoff RNase degrades cellular and viral mRNAs made before infection but not viral mRNA made after infection. J Virol. 2013;87:4516–22.PubMedPubMedCentralCrossRef
64.
go back to reference Dauber B, Saffran HA, Smiley JR. The herpes simplex virus 1 virion host shutoff protein enhances translation of viral late mRNAs by preventing mRNA overload. J Virol. 2014;88:9624–32.PubMedPubMedCentralCrossRef Dauber B, Saffran HA, Smiley JR. The herpes simplex virus 1 virion host shutoff protein enhances translation of viral late mRNAs by preventing mRNA overload. J Virol. 2014;88:9624–32.PubMedPubMedCentralCrossRef
65.
go back to reference Sadek J, Read GS. The splicing history of an mRNA affects its level of translation and sensitivity to cleavage by the Virion host shutoff endonuclease during herpes simplex virus infections. J Virol. 2016;90:10844–56.PubMedPubMedCentralCrossRef Sadek J, Read GS. The splicing history of an mRNA affects its level of translation and sensitivity to cleavage by the Virion host shutoff endonuclease during herpes simplex virus infections. J Virol. 2016;90:10844–56.PubMedPubMedCentralCrossRef
66.
go back to reference Shu M, Taddeo B, Zhang W, Roizman B. Selective degradation of mRNAs by the HSV host shutoff RNase is regulated by the UL47 tegument protein. Proc Natl Acad Sci U S A. 2013;110:E1669–75.PubMedPubMedCentralCrossRef Shu M, Taddeo B, Zhang W, Roizman B. Selective degradation of mRNAs by the HSV host shutoff RNase is regulated by the UL47 tegument protein. Proc Natl Acad Sci U S A. 2013;110:E1669–75.PubMedPubMedCentralCrossRef
67.
go back to reference Elliott G, Pheasant K, Ebert-Keel K, Stylianou J, Franklyn A, Jones J. Multiple posttranscriptional strategies to regulate the herpes simplex virus 1 vhs Endoribonuclease. J Virol. 2018;92:e00818.PubMedPubMedCentralCrossRef Elliott G, Pheasant K, Ebert-Keel K, Stylianou J, Franklyn A, Jones J. Multiple posttranscriptional strategies to regulate the herpes simplex virus 1 vhs Endoribonuclease. J Virol. 2018;92:e00818.PubMedPubMedCentralCrossRef
68.
go back to reference Pheasant K, Moller-Levet CS, Jones J, Depledge D, Breuer J, Elliott G. Nuclear-cytoplasmic compartmentalization of the herpes simplex virus 1 infected cell transcriptome is co-ordinated by the viral endoribonuclease vhs and cofactors to facilitate the translation of late proteins. PLoS Pathog. 2018;14:e1007331.PubMedPubMedCentralCrossRef Pheasant K, Moller-Levet CS, Jones J, Depledge D, Breuer J, Elliott G. Nuclear-cytoplasmic compartmentalization of the herpes simplex virus 1 infected cell transcriptome is co-ordinated by the viral endoribonuclease vhs and cofactors to facilitate the translation of late proteins. PLoS Pathog. 2018;14:e1007331.PubMedPubMedCentralCrossRef
69.
go back to reference Shu M, Taddeo B, Roizman B. The nuclear-cytoplasmic shuttling of Virion host shutoff RNase is enabled by pUL47 and an embedded nuclear export signal and defines the sites of degradation of AU-rich and stable cellular mRNAs. J Virol. 2013;87:13569–78.PubMedPubMedCentralCrossRef Shu M, Taddeo B, Roizman B. The nuclear-cytoplasmic shuttling of Virion host shutoff RNase is enabled by pUL47 and an embedded nuclear export signal and defines the sites of degradation of AU-rich and stable cellular mRNAs. J Virol. 2013;87:13569–78.PubMedPubMedCentralCrossRef
70.
71.
go back to reference Soliman TM, Sandri-Goldin RM, Silverstein SJ. Shuttling ofthe herpes simplex virus type 1 regulatory protein ICP27 between the nucleus and cytoplasm mediates the expression of late proteins. J Virol. 1997;71:9188–97.PubMedPubMedCentralCrossRef Soliman TM, Sandri-Goldin RM, Silverstein SJ. Shuttling ofthe herpes simplex virus type 1 regulatory protein ICP27 between the nucleus and cytoplasm mediates the expression of late proteins. J Virol. 1997;71:9188–97.PubMedPubMedCentralCrossRef
73.
go back to reference Feederle R, Mehl-Lautscham AM, Bannert H, Delecluse HJ. The Epstein-Barr virus protein kinase BGLF4 and the exonuclease BGLF5 have opposite effects on the regulation of viral protein production. J Virol. 2009;83:10877–91.PubMedPubMedCentralCrossRef Feederle R, Mehl-Lautscham AM, Bannert H, Delecluse HJ. The Epstein-Barr virus protein kinase BGLF4 and the exonuclease BGLF5 have opposite effects on the regulation of viral protein production. J Virol. 2009;83:10877–91.PubMedPubMedCentralCrossRef
74.
go back to reference Tian X, Devi-Rao G, Golovanov AP, Sandri-Goldin RM. The interaction of the cellular export adaptor protein Aly/REF with ICP27 contributes to the efficiency of herpes simplex virus 1 mRNA export. J Virol. 2013;87:7210–7.PubMedPubMedCentralCrossRef Tian X, Devi-Rao G, Golovanov AP, Sandri-Goldin RM. The interaction of the cellular export adaptor protein Aly/REF with ICP27 contributes to the efficiency of herpes simplex virus 1 mRNA export. J Virol. 2013;87:7210–7.PubMedPubMedCentralCrossRef
75.
go back to reference Ote I, Piette J, Sadzot-Delvaux C. The varicella-zoster virus IE4 protein: a conserved member of the herpesviral mRNA export factors family and a potential alternative target in antiherpetic therapies. Biochem Pharmacol. 2010;80:1973–80.PubMedCrossRef Ote I, Piette J, Sadzot-Delvaux C. The varicella-zoster virus IE4 protein: a conserved member of the herpesviral mRNA export factors family and a potential alternative target in antiherpetic therapies. Biochem Pharmacol. 2010;80:1973–80.PubMedCrossRef
76.
go back to reference Amor S, Strassheim S, Dambrine G, Remy S, Rasschaert D, Laurent S. ICP27 protein of Marek's disease virus interacts with SR proteins and inhibits the splicing of cellular telomerase chTERT and viral vIL8 transcripts. J Gen Virol. 2011;92:1273–8.PubMedCrossRef Amor S, Strassheim S, Dambrine G, Remy S, Rasschaert D, Laurent S. ICP27 protein of Marek's disease virus interacts with SR proteins and inhibits the splicing of cellular telomerase chTERT and viral vIL8 transcripts. J Gen Virol. 2011;92:1273–8.PubMedCrossRef
77.
go back to reference Corbin-Lickfett KA, Rojas S, Li L, Cocco MJ, Sandri-Goldin RM. ICP27 phosphorylation site mutants display altered functional interactions with cellular export factors Aly/REF and TAP/NXF1 but are able to bind herpes simplex virus 1 RNA. J Virol. 2010;84:2212–22.PubMedCrossRef Corbin-Lickfett KA, Rojas S, Li L, Cocco MJ, Sandri-Goldin RM. ICP27 phosphorylation site mutants display altered functional interactions with cellular export factors Aly/REF and TAP/NXF1 but are able to bind herpes simplex virus 1 RNA. J Virol. 2010;84:2212–22.PubMedCrossRef
78.
go back to reference Ote I, Lebrun M, Vandevenne P, Bontems S, Medina-Palazon C, Manet E, et al. Varicella-zoster virus IE4 protein interacts with SR proteins and exports mRNAs through the TAP/NXF1 pathway. PLoS One. 2009;4:e7882.PubMedPubMedCentralCrossRef Ote I, Lebrun M, Vandevenne P, Bontems S, Medina-Palazon C, Manet E, et al. Varicella-zoster virus IE4 protein interacts with SR proteins and exports mRNAs through the TAP/NXF1 pathway. PLoS One. 2009;4:e7882.PubMedPubMedCentralCrossRef
79.
go back to reference Csabai Z, Takacs IF, Snyder M, Boldogkoi Z, Tombacz D. Evaluation of the impact of ul54 gene-deletion on the global transcription and DNA replication of pseudorabies virus. Arch Virol. 2017;162:2679–94.PubMedPubMedCentralCrossRef Csabai Z, Takacs IF, Snyder M, Boldogkoi Z, Tombacz D. Evaluation of the impact of ul54 gene-deletion on the global transcription and DNA replication of pseudorabies virus. Arch Virol. 2017;162:2679–94.PubMedPubMedCentralCrossRef
80.
go back to reference Deng L, Zeng Q, Wang M, Cheng A, Jia R, Chen S, Zhu D, Liu M, Yang Q, Wu Y, et al. Suppression of NF-kappaB activity: a viral immune evasion mechanism. Viruses. 2018;10:E409.PubMedCrossRef Deng L, Zeng Q, Wang M, Cheng A, Jia R, Chen S, Zhu D, Liu M, Yang Q, Wu Y, et al. Suppression of NF-kappaB activity: a viral immune evasion mechanism. Viruses. 2018;10:E409.PubMedCrossRef
82.
go back to reference Duerst RJ, Morrison LA. Herpes simplex virus 2 virion host shutoff protein interferes with type I interferon production and responsiveness. Virology. 2004;322:158–67.PubMedCrossRef Duerst RJ, Morrison LA. Herpes simplex virus 2 virion host shutoff protein interferes with type I interferon production and responsiveness. Virology. 2004;322:158–67.PubMedCrossRef
83.
go back to reference Leib DA, Harrison TE, Laslo KM, Machalek MA, Moorman NJ, Virgin HW. Interferons regulate the phenotype of wild-type and mutant herpes simplex viruses in vivo. J Exp Med. 1999;189:663–72.PubMedPubMedCentralCrossRef Leib DA, Harrison TE, Laslo KM, Machalek MA, Moorman NJ, Virgin HW. Interferons regulate the phenotype of wild-type and mutant herpes simplex viruses in vivo. J Exp Med. 1999;189:663–72.PubMedPubMedCentralCrossRef
84.
go back to reference da Silva LF, Sinani D, Jones C. ICP27 protein encoded by bovine herpesvirus type 1 (bICP27) interferes with promoter activity of the bovine genes encoding beta interferon 1 (IFN-beta1) and IFN-beta3. Virus Res. 2012;169:162–8.PubMedPubMedCentralCrossRef da Silva LF, Sinani D, Jones C. ICP27 protein encoded by bovine herpesvirus type 1 (bICP27) interferes with promoter activity of the bovine genes encoding beta interferon 1 (IFN-beta1) and IFN-beta3. Virus Res. 2012;169:162–8.PubMedPubMedCentralCrossRef
85.
go back to reference Su C, Zheng C. Herpes simplex virus 1 abrogates the cGAS/STING-mediated cytosolic DNA-sensing pathway via its Virion host shutoff protein, UL41. J Virol. 2017;91:e02414–6.PubMedPubMedCentral Su C, Zheng C. Herpes simplex virus 1 abrogates the cGAS/STING-mediated cytosolic DNA-sensing pathway via its Virion host shutoff protein, UL41. J Virol. 2017;91:e02414–6.PubMedPubMedCentral
86.
go back to reference Christensen MH, Jensen SB, Miettinen JJ, Luecke S, Prabakaran T, Reinert LS, et al. HSV-1 ICP27 targets the TBK1-activated STING signalsome to inhibit virus-induced type I IFN expression. EMBO J. 2016;35:1385–99.PubMedPubMedCentralCrossRef Christensen MH, Jensen SB, Miettinen JJ, Luecke S, Prabakaran T, Reinert LS, et al. HSV-1 ICP27 targets the TBK1-activated STING signalsome to inhibit virus-induced type I IFN expression. EMBO J. 2016;35:1385–99.PubMedPubMedCentralCrossRef
87.
go back to reference Guan X, Zhang M, Fu M, Luo S, Hu Q. Herpes simplex virus type 2 immediate early protein ICP27 inhibits IFN-beta production in mucosal epithelial cells by antagonizing IRF3 activation. Front Immunol. 2019;10:290.PubMedPubMedCentralCrossRef Guan X, Zhang M, Fu M, Luo S, Hu Q. Herpes simplex virus type 2 immediate early protein ICP27 inhibits IFN-beta production in mucosal epithelial cells by antagonizing IRF3 activation. Front Immunol. 2019;10:290.PubMedPubMedCentralCrossRef
88.
go back to reference Jin T, Perry A, Jiang J, Smith P, Curry JA, Unterholzner L, et al. Structures of the HIN domain: DNA complexes reveal ligand binding and activation mechanisms of the AIM2 inflammasome and IFI16 receptor. Immunity. 2012;36:561–71.PubMedPubMedCentralCrossRef Jin T, Perry A, Jiang J, Smith P, Curry JA, Unterholzner L, et al. Structures of the HIN domain: DNA complexes reveal ligand binding and activation mechanisms of the AIM2 inflammasome and IFI16 receptor. Immunity. 2012;36:561–71.PubMedPubMedCentralCrossRef
89.
go back to reference Singh VV, Kerur N, Bottero V, Dutta S, Chakraborty S, Ansari MA, et al. Kaposi's sarcoma-associated herpesvirus latency in endothelial and B cells activates gamma interferon-inducible protein 16-mediated inflammasomes. J Virol. 2013;87:4417–31.PubMedPubMedCentralCrossRef Singh VV, Kerur N, Bottero V, Dutta S, Chakraborty S, Ansari MA, et al. Kaposi's sarcoma-associated herpesvirus latency in endothelial and B cells activates gamma interferon-inducible protein 16-mediated inflammasomes. J Virol. 2013;87:4417–31.PubMedPubMedCentralCrossRef
90.
go back to reference Diner BA, Lum KK, Javitt A, Cristea IM. Interactions of the antiviral factor IFI16 mediate immune signaling and herpes simplex virus-1 immunosuppression. Mol Cell Proteomics. 2015;14:2341–56.PubMedPubMedCentralCrossRef Diner BA, Lum KK, Javitt A, Cristea IM. Interactions of the antiviral factor IFI16 mediate immune signaling and herpes simplex virus-1 immunosuppression. Mol Cell Proteomics. 2015;14:2341–56.PubMedPubMedCentralCrossRef
91.
go back to reference Orzalli MH, Broekema NM, Knipe DM. Relative contributions of herpes simplex virus 1 ICP0 and vhs to loss of cellular IFI16 vary in different human cell types. J Virol. 2016;90:8351–9.PubMedPubMedCentralCrossRef Orzalli MH, Broekema NM, Knipe DM. Relative contributions of herpes simplex virus 1 ICP0 and vhs to loss of cellular IFI16 vary in different human cell types. J Virol. 2016;90:8351–9.PubMedPubMedCentralCrossRef
92.
93.
go back to reference Yao XD, Rosenthal KL. Herpes simplex virus type 2 virion host shutoff protein suppresses innate dsRNA antiviral pathways in human vaginal epithelial cells. J Gen Virol. 2011;92:1981–93.PubMedCrossRef Yao XD, Rosenthal KL. Herpes simplex virus type 2 virion host shutoff protein suppresses innate dsRNA antiviral pathways in human vaginal epithelial cells. J Gen Virol. 2011;92:1981–93.PubMedCrossRef
94.
go back to reference Stempel M, Chan B, Brinkmann MM. Coevolution pays off: Herpesviruses have the license to escape the DNA sensing pathway. Med Microbiol Immunol. 2019;208:495–512.PubMedCrossRef Stempel M, Chan B, Brinkmann MM. Coevolution pays off: Herpesviruses have the license to escape the DNA sensing pathway. Med Microbiol Immunol. 2019;208:495–512.PubMedCrossRef
95.
go back to reference van Gent M, Griffin BD, Berkhoff EG, van Leeuwen D, Boer IG, Buisson M, et al. EBV lytic-phase protein BGLF5 contributes to TLR9 downregulation during productive infection. J Immunol. 2011;186:1694–702.PubMedCrossRef van Gent M, Griffin BD, Berkhoff EG, van Leeuwen D, Boer IG, Buisson M, et al. EBV lytic-phase protein BGLF5 contributes to TLR9 downregulation during productive infection. J Immunol. 2011;186:1694–702.PubMedCrossRef
96.
go back to reference Zheng C. Evasion of cytosolic DNA-stimulated innate immune responses by herpes simplex virus 1. J Virol. 2018;92:e00099–17.PubMedPubMedCentral Zheng C. Evasion of cytosolic DNA-stimulated innate immune responses by herpes simplex virus 1. J Virol. 2018;92:e00099–17.PubMedPubMedCentral
97.
go back to reference Crosse KM, Monson EA, Beard MR, Helbig KJ. Interferon-stimulated genes as enhancers of antiviral innate immune signaling. J Innate Immun. 2018;10:85–93.PubMedCrossRef Crosse KM, Monson EA, Beard MR, Helbig KJ. Interferon-stimulated genes as enhancers of antiviral innate immune signaling. J Innate Immun. 2018;10:85–93.PubMedCrossRef
99.
100.
101.
go back to reference Ma W, Wang H, He H. Bovine herpesvirus 1 tegument protein UL41 suppresses antiviral innate immune response via directly targeting STAT1. Vet Microbiol. 2019;239:108494.PubMedCrossRef Ma W, Wang H, He H. Bovine herpesvirus 1 tegument protein UL41 suppresses antiviral innate immune response via directly targeting STAT1. Vet Microbiol. 2019;239:108494.PubMedCrossRef
102.
103.
go back to reference Shen G, Wang K, Wang S, Cai M, Li ML, Zheng C. Herpes simplex virus 1 counteracts viperin via its virion host shutoff protein UL41. J Virol. 2014;88:12163–6.PubMedPubMedCentralCrossRef Shen G, Wang K, Wang S, Cai M, Li ML, Zheng C. Herpes simplex virus 1 counteracts viperin via its virion host shutoff protein UL41. J Virol. 2014;88:12163–6.PubMedPubMedCentralCrossRef
104.
go back to reference Zenner HL, Mauricio R, Banting G, Crump CM. Herpes simplex virus 1 counteracts tetherin restriction via its virion host shutoff activity. J Virol. 2013;87:13115–23.PubMedPubMedCentralCrossRef Zenner HL, Mauricio R, Banting G, Crump CM. Herpes simplex virus 1 counteracts tetherin restriction via its virion host shutoff activity. J Virol. 2013;87:13115–23.PubMedPubMedCentralCrossRef
105.
106.
go back to reference You H, Yuan H, Fu W, Su C, Wang W, Cheng T, Zheng C. Herpes simplex virus type 1 abrogates the antiviral activity of Ch25h via its virion host shutoff protein. Antivir Res. 2017;143:69–73.PubMedCrossRef You H, Yuan H, Fu W, Su C, Wang W, Cheng T, Zheng C. Herpes simplex virus type 1 abrogates the antiviral activity of Ch25h via its virion host shutoff protein. Antivir Res. 2017;143:69–73.PubMedCrossRef
107.
go back to reference Suzutani T, Nagamine M, Shibaki T, Ogasawara M, Yoshida I, Daikoku T, et al. The role of the UL41 gene of herpes simplex virus type 1 in evasion of non-specific host defence mechanisms during primary infection. J Gen Virol. 2000;81:1763–71.PubMedCrossRef Suzutani T, Nagamine M, Shibaki T, Ogasawara M, Yoshida I, Daikoku T, et al. The role of the UL41 gene of herpes simplex virus type 1 in evasion of non-specific host defence mechanisms during primary infection. J Gen Virol. 2000;81:1763–71.PubMedCrossRef
108.
go back to reference Jurak I, Silverstein LB, Sharma M, Coen DM. Herpes simplex virus is equipped with RNA- and protein-based mechanisms to repress expression of ATRX, an effector of intrinsic immunity. J Virol. 2012;86:10093–102.PubMedPubMedCentralCrossRef Jurak I, Silverstein LB, Sharma M, Coen DM. Herpes simplex virus is equipped with RNA- and protein-based mechanisms to repress expression of ATRX, an effector of intrinsic immunity. J Virol. 2012;86:10093–102.PubMedPubMedCentralCrossRef
109.
go back to reference van Gent M, Gram AM, Boer IG, Geerdink RJ, Lindenbergh MF, et al. Silencing the shutoff protein of Epstein-Barr virus in productively infected B cells points to (innate) targets for immune evasion. J Gen Virol. 2015;96:858–65.PubMedCrossRef van Gent M, Gram AM, Boer IG, Geerdink RJ, Lindenbergh MF, et al. Silencing the shutoff protein of Epstein-Barr virus in productively infected B cells points to (innate) targets for immune evasion. J Gen Virol. 2015;96:858–65.PubMedCrossRef
110.
go back to reference Quinn LL, Zuo J, Abbott RJ, Shannon-Lowe C, Tierney RJ, Hislop AD, Rowe M. Cooperation between Epstein-Barr virus immune evasion proteins spreads protection from CD8+ T cell recognition across all three phases of the lytic cycle. PLoS Pathog. 2014;10:e1004322.PubMedPubMedCentralCrossRef Quinn LL, Zuo J, Abbott RJ, Shannon-Lowe C, Tierney RJ, Hislop AD, Rowe M. Cooperation between Epstein-Barr virus immune evasion proteins spreads protection from CD8+ T cell recognition across all three phases of the lytic cycle. PLoS Pathog. 2014;10:e1004322.PubMedPubMedCentralCrossRef
112.
go back to reference Richner JM, Clyde K, Pezda AC, Cheng BY, Wang T, Kumar GR, et al. Global mRNA degradation during lytic gammaherpesvirus infection contributes to establishment of viral latency. PLoS Pathog. 2011;7:e1002150.PubMedPubMedCentralCrossRef Richner JM, Clyde K, Pezda AC, Cheng BY, Wang T, Kumar GR, et al. Global mRNA degradation during lytic gammaherpesvirus infection contributes to establishment of viral latency. PLoS Pathog. 2011;7:e1002150.PubMedPubMedCentralCrossRef
113.
115.
go back to reference Su A, Wang H, Li Y, Wang X, Chen D, Wu Z. Opposite roles of RNase and kinase activities of inositol-requiring enzyme 1 (IRE1) on HSV-1 replication. Viruses. 2017;9:–E235. Su A, Wang H, Li Y, Wang X, Chen D, Wu Z. Opposite roles of RNase and kinase activities of inositol-requiring enzyme 1 (IRE1) on HSV-1 replication. Viruses. 2017;9:–E235.
116.
go back to reference Zhang P, Su C, Jiang Z, Zheng C. Herpes simplex virus 1 UL41 protein suppresses the IRE1/XBP1 signal pathway of the unfolded protein response via its RNase activity. J Virol. 2017;91:e02056–16.PubMedPubMedCentral Zhang P, Su C, Jiang Z, Zheng C. Herpes simplex virus 1 UL41 protein suppresses the IRE1/XBP1 signal pathway of the unfolded protein response via its RNase activity. J Virol. 2017;91:e02056–16.PubMedPubMedCentral
117.
119.
go back to reference Johnston BP, Pringle ES, McCormick C. KSHV activates unfolded protein response sensors but suppresses downstream transcriptional responses to support lytic replication. PLoS Pathog. 2019;15:e1008185.PubMedPubMedCentralCrossRef Johnston BP, Pringle ES, McCormick C. KSHV activates unfolded protein response sensors but suppresses downstream transcriptional responses to support lytic replication. PLoS Pathog. 2019;15:e1008185.PubMedPubMedCentralCrossRef
120.
go back to reference Finnen RL, Hay TJ, Dauber B, Smiley JR, Banfield BW. The herpes simplex virus 2 virion-associated ribonuclease vhs interferes with stress granule formation. J Virol. 2014;88:12727–39.PubMedPubMedCentralCrossRef Finnen RL, Hay TJ, Dauber B, Smiley JR, Banfield BW. The herpes simplex virus 2 virion-associated ribonuclease vhs interferes with stress granule formation. J Virol. 2014;88:12727–39.PubMedPubMedCentralCrossRef
121.
go back to reference Burgess HM, Mohr I. Defining the role of stress granules in innate immune suppression by the herpes simplex virus 1 Endoribonuclease VHS. J Virol. 2018;92:e00829–18.PubMedPubMedCentralCrossRef Burgess HM, Mohr I. Defining the role of stress granules in innate immune suppression by the herpes simplex virus 1 Endoribonuclease VHS. J Virol. 2018;92:e00829–18.PubMedPubMedCentralCrossRef
123.
Metadata
Title
Host shutoff activity of VHS and SOX-like proteins: role in viral survival and immune evasion
Authors
Tianqiong He
Mingshu Wang
Anchun Cheng
Qiao Yang
Ying Wu
Renyong Jia
Mafeng Liu
Dekang Zhu
Shun Chen
Shaqiu Zhang
Xin-Xin Zhao
Juan Huang
Di Sun
Sai Mao
Xuming Ou
Yin Wang
Zhiwen Xu
Zhengli Chen
Lin Zhu
Qihui Luo
Yunya Liu
Yanling Yu
Ling Zhang
Bin Tian
Leichang Pan
Mujeeb Ur Rehman
Xiaoyue Chen
Publication date
01-12-2020
Publisher
BioMed Central
Published in
Virology Journal / Issue 1/2020
Electronic ISSN: 1743-422X
DOI
https://doi.org/10.1186/s12985-020-01336-8

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