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Journal of Virology
Volumn 90, Issue 13, 2016, Pages 6049-6057
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
Author keywords

[No Author keywords available]
Indexed keywords

DOUBLE STRANDED RNA; GC PROTEIN; INITIATION FACTOR 2ALPHA; PROTEIN KINASE R; PROTEIN US11; UL47 PROTEIN; UNCLASSIFIED DRUG; VIRION HOST SHUTOFF PROTEIN; VIRUS PROTEIN; INITIATION FACTOR 2; MESSENGER RNA; VIRAL PROTEIN; VIRUS RNA;
EID: 84975322626     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.03180-15     Document Type: Article
Times cited : (33)
References (73)
  • 1
    • 84939997955 scopus 로고    scopus 로고
    • Emerging roles for RNA degradation in viral replication and antiviral defense
    • Abernathy E, Glaunsinger B. 2015. Emerging roles for RNA degradation in viral replication and antiviral defense. Virology 479-480:600-608. http://dx.doi.org/10.1016/j.virol.2015.02.007.
    • (2015) Virology , vol.479-480 , pp. 600-608
    • Abernathy, E.1    Glaunsinger, B.2
  • 2
    • 84885738418 scopus 로고    scopus 로고
    • Virus-encoded endonucleases: expected and novel functions
    • Read GS. 2013. Virus-encoded endonucleases: expected and novel functions. Wiley Interdiscip Rev RNA 4:693-708. http://dx.doi.org/10.1002/wrna.1188.
    • (2013) Wiley Interdiscip Rev RNA , vol.4 , pp. 693-708
    • Read, G.S.1
  • 3
    • 0020526685 scopus 로고
    • Herpes simplex virus mutants defective in the virion-associated shutoff of host polypeptide synthesis and exhibiting abnormal synthesis of alpha (immediate early) viral polypeptides
    • Read GS, Frenkel N. 1983. Herpes simplex virus mutants defective in the virion-associated shutoff of host polypeptide synthesis and exhibiting abnormal synthesis of alpha (immediate early) viral polypeptides. J Virol 46:498-512.
    • (1983) J Virol , vol.46 , pp. 498-512
    • Read, G.S.1    Frenkel, N.2
  • 4
    • 0023866418 scopus 로고
    • Herpes simplex virus virion host shutoff function
    • Kwong AD, Kruper JA, Frenkel N. 1988. Herpes simplex virus virion host shutoff function. J Virol 62:912-921.
    • (1988) J Virol , vol.62 , pp. 912-921
    • Kwong, A.D.1    Kruper, J.A.2    Frenkel, N.3
  • 5
    • 0346373732 scopus 로고    scopus 로고
    • Herpes simplex virus virion host shutoff protein: immune evasion mediated by a viral RNase?
    • Smiley JR. 2004. Herpes simplex virus virion host shutoff protein: immune evasion mediated by a viral RNase? J Virol 78:1063-1068. http://dx.doi.org/10.1128/JVI.78.3.1063-1068.2004.
    • (2004) J Virol , vol.78 , pp. 1063-1068
    • Smiley, J.R.1
  • 6
    • 0036333951 scopus 로고    scopus 로고
    • mRNA degradation by the virion host shutoff (Vhs) protein of herpes simplex virus: genetic and biochemical evidence that Vhs is a nuclease
    • Everly J, David N, Feng P, Mian IS, Read GS. 2002. mRNA degradation by the virion host shutoff (Vhs) protein of herpes simplex virus: genetic and biochemical evidence that Vhs is a nuclease. J Virol 76:8560-8571. http://dx.doi.org/10.1128/JVI.76.17.8560-8571.2002.
    • (2002) J Virol , vol.76 , pp. 8560-8571
    • Everly, J.1    David, N.2    Feng, P.3    Mian, I.S.4    Read, G.S.5
  • 7
    • 33748511878 scopus 로고    scopus 로고
    • The virion host shutoff protein (UL41) of herpes simplex virus 1 is an endoribonuclease with a substrate specificity similar to that of RNase A
    • Taddeo B, Roizman B. 2006. 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 80:9341-9345. http://dx.doi.org/10.1128/JVI.01008-06.
    • (2006) J Virol , vol.80 , pp. 9341-9345
    • Taddeo, B.1    Roizman, B.2
  • 8
    • 33644552729 scopus 로고    scopus 로고
    • The UL41 protein of herpes simplex virus 1 degrades RNA by endonucleolytic cleavage in absence of other cellular or viral proteins
    • Taddeo B, Zhang W, Roizman B. 2006. The UL41 protein of herpes simplex virus 1 degrades RNA by endonucleolytic cleavage in absence of other cellular or viral proteins. Proc Natl Acad Sci U S A 103:2827-2832. http://dx.doi.org/10.1073/pnas.0510712103.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 2827-2832
    • Taddeo, B.1    Zhang, W.2    Roizman, B.3
  • 9
    • 0029919184 scopus 로고    scopus 로고
    • The virion host shutoff protein of herpes simplex virus type 1: messenger ribonucleolytic activity in vitro
    • Zelus BD, Stewart RS, Ross J. 1996. The virion host shutoff protein of herpes simplex virus type 1: messenger ribonucleolytic activity in vitro. J Virol 70:2411-2419.
    • (1996) J Virol , vol.70 , pp. 2411-2419
    • Zelus, B.D.1    Stewart, R.S.2    Ross, J.3
  • 10
    • 2642604294 scopus 로고
    • Herpes simplex virus-infected cells contain a function(s) that destabilizes both host and viral mRNAs
    • Kwong AD, Frenkel N. 1987. Herpes simplex virus-infected cells contain a function(s) that destabilizes both host and viral mRNAs. Proc Natl Acad Sci U S A 84:1926-1930. http://dx.doi.org/10.1073/pnas.84.7.1926.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 1926-1930
    • Kwong, A.D.1    Frenkel, N.2
  • 11
    • 0024521222 scopus 로고
    • Control of mRNA stability by the virion host shutoff function of herpes simplex virus
    • Oroskar AA, Read GS. 1989. Control of mRNA stability by the virion host shutoff function of herpes simplex virus. J Virol 63:1897-1906.
    • (1989) J Virol , vol.63 , pp. 1897-1906
    • Oroskar, A.A.1    Read, G.S.2
  • 12
    • 84866149031 scopus 로고    scopus 로고
    • A common strategy for host RNA degradation by divergent viruses
    • Gaglia MM, Covarrubias S, Wong W, Glaunsinger BA. 2012. A common strategy for host RNA degradation by divergent viruses. J Virol 86:9527-9530. http://dx.doi.org/10.1128/JVI.01230-12.
    • (2012) J Virol , vol.86 , pp. 9527-9530
    • Gaglia, M.M.1    Covarrubias, S.2    Wong, W.3    Glaunsinger, B.A.4
  • 13
    • 77953302048 scopus 로고    scopus 로고
    • The virion host shutoff endonuclease (UL41) of herpes simplex virus interacts with the cellular cap-binding complex eIF4F
    • Page HG, Read GS. 2010. The virion host shutoff endonuclease (UL41) of herpes simplex virus interacts with the cellular cap-binding complex eIF4F. J Virol 84:6886-6890. http://dx.doi.org/10.1128/JVI.00166-10.
    • (2010) J Virol , vol.84 , pp. 6886-6890
    • Page, H.G.1    Read, G.S.2
  • 14
    • 8644221609 scopus 로고    scopus 로고
    • Herpes simplex virus virion host shutoff protein is stimulated by translation initiation factors eIF4B and eIF4H
    • Doepker RC, Hsu W-L, Saffran HA, Smiley JR. 2004. Herpes simplex virus virion host shutoff protein is stimulated by translation initiation factors eIF4B and eIF4H. J Virol 78:4684-4699. http://dx.doi.org/10.1128/JVI.78.9.4684-4699.2004.
    • (2004) J Virol , vol.78 , pp. 4684-4699
    • Doepker, R.C.1    Hsu, W.-L.2    Saffran, H.A.3    Smiley, J.R.4
  • 15
    • 0034796322 scopus 로고    scopus 로고
    • mRNA decay during herpesvirus infections: interaction between a putative viral nuclease and a cellular translation factor
    • Feng P, Everly DN, Jr, Read GS. 2001. mRNA decay during herpesvirus infections: interaction between a putative viral nuclease and a cellular translation factor. J Virol 75:10272-10280. http://dx.doi.org/10.1128/JVI.75.21.10272-10280.2001.
    • (2001) J Virol , vol.75 , pp. 10272-10280
    • Feng, P.1    Everly, D.N.2    Read, G.S.3
  • 16
    • 45749139207 scopus 로고    scopus 로고
    • Small interfering RNAs that deplete the cellular translation factor eIF4H impede mRNA degradation by the virion host shutoff protein of herpes simplex virus
    • Sarma N, Agarwal D, Shiflett LA, Read GS. 2008. 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 82:6600-6609. http://dx.doi.org/10.1128/JVI.00137-08.
    • (2008) J Virol , vol.82 , pp. 6600-6609
    • Sarma, N.1    Agarwal, D.2    Shiflett, L.A.3    Read, G.S.4
  • 17
    • 22544452431 scopus 로고    scopus 로고
    • mRNA decay during herpes simplex virus (HSV) infections: protein-protein interactions involving theHSVvirion host shutoff protein and translation factors eIF4H and eIF4A
    • Feng P, Everly DN, Read GS. 2005. mRNA decay during herpes simplex virus (HSV) infections: protein-protein interactions involving theHSVvirion host shutoff protein and translation factors eIF4H and eIF4A. J Virol 79:9651-9664. http://dx.doi.org/10.1128/JVI.79.15.9651-9664.2005.
    • (2005) J Virol , vol.79 , pp. 9651-9664
    • Feng, P.1    Everly, D.N.2    Read, G.S.3
  • 18
    • 0032864835 scopus 로고    scopus 로고
    • The herpes simplex virus vhs protein induces endoribonucleolytic cleavage of target RNAs in cell extracts
    • Elgadi MM, Hayes CE, Smiley JR. 1999. The herpes simplex virus vhs protein induces endoribonucleolytic cleavage of target RNAs in cell extracts. J Virol 73:7153-7164.
    • (1999) J Virol , vol.73 , pp. 7153-7164
    • Elgadi, M.M.1    Hayes, C.E.2    Smiley, J.R.3
  • 19
    • 0032853361 scopus 로고    scopus 로고
    • Picornavirus internal ribosome entry site elements target RNA cleavage events induced by the herpes simplex virus virion host shutoff protein
    • Elgadi MM, Smiley JR. 1999. Picornavirus internal ribosome entry site elements target RNA cleavage events induced by the herpes simplex virus virion host shutoff protein. J Virol 73:9222-9231.
    • (1999) J Virol , vol.73 , pp. 9222-9231
    • Elgadi, M.M.1    Smiley, J.R.2
  • 20
    • 0033544338 scopus 로고    scopus 로고
    • The virion host shutoff function of herpes simplex virus degrades the 5' end of a target mRNA before the 3' end
    • Karr BM, Read GS. 1999. The virion host shutoff function of herpes simplex virus degrades the 5' end of a target mRNA before the 3' end. Virology 264:195-204. http://dx.doi.org/10.1006/viro.1999.9986.
    • (1999) Virology , vol.264 , pp. 195-204
    • Karr, B.M.1    Read, G.S.2
  • 21
    • 84871948027 scopus 로고    scopus 로고
    • mRNA decay during herpes simplex virus (HSV) infections: mutations that affect translation of an mRNA influence the sites at which it is cleaved by theHSVvirion host shutoff (Vhs) protein
    • Shiflett LA, Read GS. 2013. mRNA decay during herpes simplex virus (HSV) infections: mutations that affect translation of an mRNA influence the sites at which it is cleaved by theHSVvirion host shutoff (Vhs) protein. J Virol 87:94-109. http://dx.doi.org/10.1128/JVI.01557-12.
    • (2013) J Virol , vol.87 , pp. 94-109
    • Shiflett, L.A.1    Read, G.S.2
  • 22
    • 1942421835 scopus 로고    scopus 로고
    • Herpes simplex virus 2 virion host shutoff protein interferes with type I interferon production and responsiveness
    • Duerst RJ, Morrison LA. 2004. Herpes simplex virus 2 virion host shutoff protein interferes with type I interferon production and responsiveness. Virology 322:158-167. http://dx.doi.org/10.1016/j.virol.2004.01.019.
    • (2004) Virology , vol.322 , pp. 158-167
    • Duerst, R.J.1    Morrison, L.A.2
  • 23
    • 0041888287 scopus 로고    scopus 로고
    • Herpes simplex virus type 2 virion host shutoff protein regulates alpha/beta interferon but not adaptive immune responses during primary infection in vivo
    • Murphy JA, Duerst RJ, Smith TJ, Morrison LA. 2003. Herpes simplex virus type 2 virion host shutoff protein regulates alpha/beta interferon but not adaptive immune responses during primary infection in vivo. J Virol 77:9337-9345. http://dx.doi.org/10.1128/JVI.77.17.9337-9345.2003.
    • (2003) J Virol , vol.77 , pp. 9337-9345
    • Murphy, J.A.1    Duerst, R.J.2    Smith, T.J.3    Morrison, L.A.4
  • 25
    • 0033919629 scopus 로고    scopus 로고
    • The role of the UL41 gene of herpes simplex virus type 1 in evasion of non-specific host defence mechanisms during primary infection
    • Suzutani T, Nagamine M, Shibaki T, Ogasawara M, Yoshida I, Daikoku T, Nishiyama Y, Azuma M. 2000. 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 81:1763-1771. http://dx.doi.org/10.1099/0022-1317-81-7-1763.
    • (2000) J Gen Virol , vol.81 , pp. 1763-1771
    • Suzutani, T.1    Nagamine, M.2    Shibaki, T.3    Ogasawara, M.4    Yoshida, I.5    Daikoku, T.6    Nishiyama, Y.7    Azuma, M.8
  • 26
    • 0037333481 scopus 로고    scopus 로고
    • Deletion of the virion host shutoff protein (vhs) from herpes simplex virus (HSV) relieves the viral block to dendritic cell activation: potential of vhsβ HSV vectors for dendritic cell-mediated immunotherapy
    • Samady L, Costigliola E, MacCormac L, McGrath Y, Cleverley S, Lilley CE, Smith J, Latchman DS, Chain B, Coffin RS. 2003. Deletion of the virion host shutoff protein (vhs) from herpes simplex virus (HSV) relieves the viral block to dendritic cell activation: potential of vhsβ HSV vectors for dendritic cell-mediated immunotherapy. J Virol 77:3768-3776. http://dx.doi.org/10.1128/JVI.77.6.3768-3776.2003.
    • (2003) J Virol , vol.77 , pp. 3768-3776
    • Samady, L.1    Costigliola, E.2    MacCormac, L.3    McGrath, Y.4    Cleverley, S.5    Lilley, C.E.6    Smith, J.7    Latchman, D.S.8    Chain, B.9    Coffin, R.S.10
  • 27
    • 0033557288 scopus 로고    scopus 로고
    • Interferons regulate the phenotype of wild-type and mutant herpes simplex viruses in vivo
    • Leib DA, Harrison TE, Laslo KM, Machalek MA, Moorman NJ, Virgin HW. 1999. Interferons regulate the phenotype of wild-type and mutant herpes simplex viruses in vivo. J Exp Med 189:663-672. http://dx.doi.org/10.1084/jem.189.4.663.
    • (1999) J Exp Med , vol.189 , pp. 663-672
    • Leib, D.A.1    Harrison, T.E.2    Laslo, K.M.3    Machalek, M.A.4    Moorman, N.J.5    Virgin, H.W.6
  • 28
    • 60049094356 scopus 로고    scopus 로고
    • Host responses to wild-type and attenuated herpes simplex virus infection in the absence of Stat1
    • Pasieka TJ, Cilloniz C, Lu B, Teal TH, Proll SC, Katze MG, Leib DA. 2009. Host responses to wild-type and attenuated herpes simplex virus infection in the absence of Stat1. J Virol 83:2075-2087. http://dx.doi.org/10.1128/JVI.02007-08.
    • (2009) J Virol , vol.83 , pp. 2075-2087
    • Pasieka, T.J.1    Cilloniz, C.2    Lu, B.3    Teal, T.H.4    Proll, S.C.5    Katze, M.G.6    Leib, D.A.7
  • 29
    • 44949265437 scopus 로고    scopus 로고
    • Enhanced pathogenesis of an attenuated herpes simplex virus for mice lacking Stat1
    • Pasieka TJ, Lu B, Leib DA. 2008. Enhanced pathogenesis of an attenuated herpes simplex virus for mice lacking Stat1. J Virol 82:6052-6055. http://dx.doi.org/10.1128/JVI.00297-08.
    • (2008) J Virol , vol.82 , pp. 6052-6055
    • Pasieka, T.J.1    Lu, B.2    Leib, D.A.3
  • 30
    • 69449088685 scopus 로고    scopus 로고
    • Increased eIF2α phosphorylation attenuates replication of herpes simplex virus 2 vhs mutants in mouse embryonic fibroblasts and correlates with reduced accumulation of the PKR antagonist ICP34.5
    • Wylie KM, Schrimpf JE, Morrison LA. 2009. Increased eIF2α phosphorylation attenuates replication of herpes simplex virus 2 vhs mutants in mouse embryonic fibroblasts and correlates with reduced accumulation of the PKR antagonist ICP34.5. J Virol 83:9151-9162. http://dx.doi.org/10.1128/JVI.00886-09.
    • (2009) J Virol , vol.83 , pp. 9151-9162
    • Wylie, K.M.1    Schrimpf, J.E.2    Morrison, L.A.3
  • 31
    • 84874704421 scopus 로고    scopus 로고
    • 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
    • Sciortino MT, Parisi T, Siracusano G, Mastino A, Taddeo B, Roizman B. 2013. 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 87:3271-3276. http://dx.doi.org/10.1128/JVI.03049-12.
    • (2013) J Virol , vol.87 , pp. 3271-3276
    • Sciortino, M.T.1    Parisi, T.2    Siracusano, G.3    Mastino, A.4    Taddeo, B.5    Roizman, B.6
  • 32
    • 33845627785 scopus 로고    scopus 로고
    • Impact of protein kinase PKR in cell biology: from antiviral to antiproliferative action
    • Garcia MA, Gil J, Ventoso I, Guerra S, Domingo E, Rivas C, Esteban M. 2006. Impact of protein kinase PKR in cell biology: from antiviral to antiproliferative action. Microbiol Mol Biol Rev 70:1032-1060. http://dx.doi.org/10.1128/MMBR.00027-06.
    • (2006) Microbiol Mol Biol Rev , vol.70 , pp. 1032-1060
    • Garcia, M.A.1    Gil, J.2    Ventoso, I.3    Guerra, S.4    Domingo, E.5    Rivas, C.6    Esteban, M.7
  • 33
    • 0027418321 scopus 로고
    • The eIF-2 alpha protein kinases, regulators of translation in eukaryotes from yeasts to humans
    • Samuel CE. 1993. The eIF-2 alpha protein kinases, regulators of translation in eukaryotes from yeasts to humans. J Biol Chem 268:7603-7606.
    • (1993) J Biol Chem , vol.268 , pp. 7603-7606
    • Samuel, C.E.1
  • 34
    • 39949085583 scopus 로고    scopus 로고
    • Stress granules: the Tao of RNA triage
    • Anderson P, Kedersha N. 2008. Stress granules: the Tao of RNA triage. Trends Biochem Sci 33:141-150. http://dx.doi.org/10.1016/j.tibs.2007.12.003.
    • (2008) Trends Biochem Sci , vol.33 , pp. 141-150
    • Anderson, P.1    Kedersha, N.2
  • 35
    • 0031017382 scopus 로고    scopus 로고
    • The 134.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1α to dephosphorylate the α subunit of the eukaryotic translation initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNA-activated protein kinase
    • He B, Gross M, Roizman B. 1997. The 134.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1α to dephosphorylate the α subunit of the eukaryotic translation initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNA-activated protein kinase. Proc Natl Acad Sci U S A 94:843-848. http://dx.doi.org/10.1073/pnas.94.3.843.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 843-848
    • He, B.1    Gross, M.2    Roizman, B.3
  • 36
    • 0033013721 scopus 로고    scopus 로고
    • A herpesvirus ribosomeassociated, RNA-binding protein confers a growth advantage upon mutants deficient in a GADD34-related function
    • Mulvey M, Poppers J, Ladd A, Mohr I. 1999. A herpesvirus ribosomeassociated, RNA-binding protein confers a growth advantage upon mutants deficient in a GADD34-related function. J Virol 73:3375-3385.
    • (1999) J Virol , vol.73 , pp. 3375-3385
    • Mulvey, M.1    Poppers, J.2    Ladd, A.3    Mohr, I.4
  • 37
    • 0031710037 scopus 로고    scopus 로고
    • The herpes simplex virus US11 protein effectively compensates for the gamma1(34.5) gene if present before activation of protein kinase R by precluding its phosphorylation and that of the alpha subunit of eukaryotic translation initiation factor 2
    • Cassady KA, Gross M, Roizman B. 1998. The herpes simplex virus US11 protein effectively compensates for the gamma1(34.5) gene if present before activation of protein kinase R by precluding its phosphorylation and that of the alpha subunit of eukaryotic translation initiation factor 2. J Virol 72:8620-8626.
    • (1998) J Virol , vol.72 , pp. 8620-8626
    • Cassady, K.A.1    Gross, M.2    Roizman, B.3
  • 38
    • 33947428335 scopus 로고    scopus 로고
    • Maintenance of endoplasmic reticulum (ER) homeostasis in herpes simplex virus type 1-infected cells through the association of a viral glycoprotein with PERK, a cellular ER stress sensor
    • Mulvey M, Arias C, Mohr I. 2007. Maintenance of endoplasmic reticulum (ER) homeostasis in herpes simplex virus type 1-infected cells through the association of a viral glycoprotein with PERK, a cellular ER stress sensor. J Virol 81:3377-3390. http://dx.doi.org/10.1128/JVI.02191-06.
    • (2007) J Virol , vol.81 , pp. 3377-3390
    • Mulvey, M.1    Arias, C.2    Mohr, I.3
  • 39
    • 79956061719 scopus 로고    scopus 로고
    • The herpes simplex virus 1 vhs protein enhances translation of viral true late mRNAs and virus production in a cell type-dependent manner
    • Dauber B, Pelletier J, Smiley JR. 2011. 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 85:5363-5373. http://dx.doi.org/10.1128/JVI.00115-11.
    • (2011) J Virol , vol.85 , pp. 5363-5373
    • Dauber, B.1    Pelletier, J.2    Smiley, J.R.3
  • 40
    • 84907428121 scopus 로고    scopus 로고
    • The herpes simplex virus 1 virion host shutoff protein enhances translation of viral late mRNAs by preventing mRNA overload
    • Dauber B, Saffran HA, Smiley JR. 2014. The herpes simplex virus 1 virion host shutoff protein enhances translation of viral late mRNAs by preventing mRNA overload. J Virol 88:9624-9632. http://dx.doi.org/10.1128/JVI.01350-14.
    • (2014) J Virol , vol.88 , pp. 9624-9632
    • Dauber, B.1    Saffran, H.A.2    Smiley, J.R.3
  • 41
    • 0033611157 scopus 로고    scopus 로고
    • RNA-binding proteins Tia-1 and Tiar link the phosphorylation of eIF-2α to the assembly of mammalian stress granules
    • Kedersha NL, Gupta M, Li W, Miller I, Anderson P. 1999. RNA-binding proteins Tia-1 and Tiar link the phosphorylation of eIF-2α to the assembly of mammalian stress granules. J Cell Biol 147:1431-1442.
    • (1999) J Cell Biol , vol.147 , pp. 1431-1442
    • Kedersha, N.L.1    Gupta, M.2    Li, W.3    Miller, I.4    Anderson, P.5
  • 42
    • 33749493493 scopus 로고    scopus 로고
    • Inhibition of ribosome recruitment induces stress granule formation independently of eukaryotic initiation factor 2α phosphorylation
    • Mazroui R, Sukarieh R, Bordeleau M-E, Kaufman RJ, Northcote P, Tanaka J, Gallouzi I, Pelletier J. 2006. Inhibition of ribosome recruitment induces stress granule formation independently of eukaryotic initiation factor 2α phosphorylation. Mol Biol Cell 17:4212-4219. http://dx.doi.org/10.1091/mbc.E06-04-0318.
    • (2006) Mol Biol Cell , vol.17 , pp. 4212-4219
    • Mazroui, R.1    Sukarieh, R.2    Bordeleau, M.-E.3    Kaufman, R.J.4    Northcote, P.5    Tanaka, J.6    Gallouzi, I.7    Pelletier, J.8
  • 44
    • 84922520038 scopus 로고    scopus 로고
    • Antiviral innate immunity and stress granule responses
    • Onomoto K, Yoneyama M, Fung G, Kato H, Fujita T. 2014. Antiviral innate immunity and stress granule responses. Trends Immunol 35:420-428. http://dx.doi.org/10.1016/j.it.2014.07.006.
    • (2014) Trends Immunol , vol.35 , pp. 420-428
    • Onomoto, K.1    Yoneyama, M.2    Fung, G.3    Kato, H.4    Fujita, T.5
  • 45
    • 84872675863 scopus 로고    scopus 로고
    • Diversion of stress granules and P-bodies during viral infection
    • Reineke LC, Lloyd RE. 2013. Diversion of stress granules and P-bodies during viral infection. Virology 436:255-267. http://dx.doi.org/10.1016/j.virol.2012.11.017.
    • (2013) Virology , vol.436 , pp. 255-267
    • Reineke, L.C.1    Lloyd, R.E.2
  • 46
    • 84868621683 scopus 로고    scopus 로고
    • Viral modulation of stress granules
    • Valiente-Echeverría F, Melnychuk L, Mouland AJ. 2012. Viral modulation of stress granules. Virus Res 169:430-437. http://dx.doi.org/10.1016/j.virusres.2012.06.004.
    • (2012) Virus Res , vol.169 , pp. 430-437
    • Valiente-Echeverría, F.1    Melnychuk, L.2    Mouland, A.J.3
  • 47
    • 84863407268 scopus 로고    scopus 로고
    • Regulation of stress granules in virus systems
    • White JP, Lloyd RE. 2012. Regulation of stress granules in virus systems. Trends Microbiol 20:175-183. http://dx.doi.org/10.1016/j.tim.2012.02.001.
    • (2012) Trends Microbiol , vol.20 , pp. 175-183
    • White, J.P.1    Lloyd, R.E.2
  • 48
    • 0036888883 scopus 로고    scopus 로고
    • Cell proteins TIA-1 and TIAR interact with the 3' stem-loop of the West Nile virus complementary minus-strand RNA and facilitate virus replication
    • Li W, Li Y, Kedersha N, Anderson P, Emara M, Swiderek KM, Moreno GT, Brinton MA. 2002. Cell proteins TIA-1 and TIAR interact with the 3' stem-loop of the West Nile virus complementary minus-strand RNA and facilitate virus replication. J Virol 76:11989-12000. http://dx.doi.org/10.1128/JVI.76.23.11989-12000.2002.
    • (2002) J Virol , vol.76 , pp. 11989-12000
    • Li, W.1    Li, Y.2    Kedersha, N.3    Anderson, P.4    Emara, M.5    Swiderek, K.M.6    Moreno, G.T.7    Brinton, M.A.8
  • 49
    • 35848929915 scopus 로고    scopus 로고
    • Inhibition of cytoplasmic mRNA stress granule formation by a viral proteinase
    • White JP, Cardenas AM, Marissen WE, Lloyd RE. 2007. Inhibition of cytoplasmic mRNA stress granule formation by a viral proteinase. Cell Host Microbe 2:295-305. http://dx.doi.org/10.1016/j.chom.2007.08.006.
    • (2007) Cell Host Microbe , vol.2 , pp. 295-305
    • White, J.P.1    Cardenas, A.M.2    Marissen, W.E.3    Lloyd, R.E.4
  • 51
    • 84860900591 scopus 로고    scopus 로고
    • Influenza A virus inhibits cytoplasmic stress granule formation
    • Khaperskyy DA, Hatchette TF, McCormick C. 2012. Influenza A virus inhibits cytoplasmic stress granule formation. FASEB J 26:1629-1639. http://dx.doi.org/10.1096/fj.11-196915.
    • (2012) FASEB J , vol.26 , pp. 1629-1639
    • Khaperskyy, D.A.1    Hatchette, T.F.2    McCormick, C.3
  • 52
    • 84883271505 scopus 로고    scopus 로고
    • Encephalomyocarditis virus disrupts stress granules, the critical platform for triggering antiviral innate immune responses
    • Ng CS, Jogi M, Yoo JS, Onomoto K, Koike S, Iwasaki T, Yoneyama M, Kato H, Fujita T. 2013. Encephalomyocarditis virus disrupts stress granules, the critical platform for triggering antiviral innate immune responses. J Virol 87:9511-9522. http://dx.doi.org/10.1128/JVI.03248-12.
    • (2013) J Virol , vol.87 , pp. 9511-9522
    • Ng, C.S.1    Jogi, M.2    Yoo, J.S.3    Onomoto, K.4    Koike, S.5    Iwasaki, T.6    Yoneyama, M.7    Kato, H.8    Fujita, T.9
  • 54
    • 84928787115 scopus 로고    scopus 로고
    • Stress granules regulate double-stranded RNA-dependent protein kinase activation through a complex containing G3BP1 and Caprin1
    • Reineke LC, Kedersha N, Langereis MA, van Kuppeveld FJ, Lloyd RE. 2015. Stress granules regulate double-stranded RNA-dependent protein kinase activation through a complex containing G3BP1 and Caprin1. mBio 6:e02486. http://dx.doi.org/10.1128/mBio.02486-14.
    • (2015) mBio , vol.6
    • Reineke, L.C.1    Kedersha, N.2    Langereis, M.A.3    van Kuppeveld, F.J.4    Lloyd, R.E.5
  • 55
    • 84923066571 scopus 로고    scopus 로고
    • The stress granule protein G3BP1 recruits protein kinase R to promote multiple innate immune antiviral responses
    • Reineke LC, Lloyd RE. 2015. The stress granule protein G3BP1 recruits protein kinase R to promote multiple innate immune antiviral responses. J Virol 89:2575-2589. http://dx.doi.org/10.1128/JVI.02791-14.
    • (2015) J Virol , vol.89 , pp. 2575-2589
    • Reineke, L.C.1    Lloyd, R.E.2
  • 56
    • 3543058093 scopus 로고    scopus 로고
    • Herpes simplex virus 1 induces cytoplasmic accumulation of TIA-1/TIAR and both synthesis and cytoplasmic accumulation of tristetraprolin, two cellular proteins that bind and destabilize AU-rich RNAs
    • Esclatine A, Taddeo B, Roizman B. 2004. Herpes simplex virus 1 induces cytoplasmic accumulation of TIA-1/TIAR and both synthesis and cytoplasmic accumulation of tristetraprolin, two cellular proteins that bind and destabilize AU-rich RNAs. J Virol 78:8582-8592. http://dx.doi.org/10.1128/JVI.78.16.8582-8592.2004.
    • (2004) J Virol , vol.78 , pp. 8582-8592
    • Esclatine, A.1    Taddeo, B.2    Roizman, B.3
  • 57
    • 84907434194 scopus 로고    scopus 로고
    • The herpes simplex virus 2 virion-associated ribonuclease vhs interferes with stress granule formation
    • Finnen RL, Hay TJ, Dauber B, Smiley JR, Banfield BW. 2014. The herpes simplex virus 2 virion-associated ribonuclease vhs interferes with stress granule formation. J Virol 88:12727-12739. http://dx.doi.org/10.1128/JVI.01554-14.
    • (2014) J Virol , vol.88 , pp. 12727-12739
    • Finnen, R.L.1    Hay, T.J.2    Dauber, B.3    Smiley, J.R.4    Banfield, B.W.5
  • 58
    • 0027420465 scopus 로고
    • Isolation of a herpes simplex virus type 1 mutant with a deletion in the virion host shutoff gene and identification of multiple forms of the vhs (UL41) polypeptide
    • Read GS, Karr BM, Knight K. 1993. Isolation of a herpes simplex virus type 1 mutant with a deletion in the virion host shutoff gene and identification of multiple forms of the vhs (UL41) polypeptide. J Virol 67:7149-7160.
    • (1993) J Virol , vol.67 , pp. 7149-7160
    • Read, G.S.1    Karr, B.M.2    Knight, K.3
  • 59
    • 0028936838 scopus 로고
    • Reversal of the interferon-sensitive phenotype of a vaccinia virus lacking E3L by expression of the reovirus S4 gene
    • Beattie E, Denzler KL, Tartaglia J, Perkus ME, Paoletti E, Jacobs BL. 1995. Reversal of the interferon-sensitive phenotype of a vaccinia virus lacking E3L by expression of the reovirus S4 gene. J Virol 69:499-505.
    • (1995) J Virol , vol.69 , pp. 499-505
    • Beattie, E.1    Denzler, K.L.2    Tartaglia, J.3    Perkus, M.E.4    Paoletti, E.5    Jacobs, B.L.6
  • 60
    • 84951042132 scopus 로고    scopus 로고
    • Essential role of protein kinase R antagonism by TR1 in human cytomegalovirus replication
    • Braggin JE, Child SJ, Geballe AP. 2016. Essential role of protein kinase R antagonism by TR1 in human cytomegalovirus replication. Virology 489: 75-85. http://dx.doi.org/10.1016/j.virol.2015.11.032.
    • (2016) Virology , vol.489 , pp. 75-85
    • Braggin, J.E.1    Child, S.J.2    Geballe, A.P.3
  • 61
    • 84913594397 scopus 로고    scopus 로고
    • Genome editing. The new frontier of genome engineering with CRISPR-Cas9
    • Doudna JA, Charpentier E. 2014. Genome editing. The new frontier of genome engineering with CRISPR-Cas9. Science 346:1258096. http://dx.doi.org/10.1126/science.1258096.
    • (2014) Science , vol.346
    • Doudna, J.A.1    Charpentier, E.2
  • 62
    • 84896706324 scopus 로고    scopus 로고
    • Elimination of mitochondrial DNA is not required for herpes simplex virus 1 replication
    • Duguay BA, Saffran HA, Ponomarev A, Duley SA, Eaton HE, Smiley JR. 2014. Elimination of mitochondrial DNA is not required for herpes simplex virus 1 replication. J Virol 88:2967-2976. http://dx.doi.org/10.1128/JVI.03129-13.
    • (2014) J Virol , vol.88 , pp. 2967-2976
    • Duguay, B.A.1    Saffran, H.A.2    Ponomarev, A.3    Duley, S.A.4    Eaton, H.E.5    Smiley, J.R.6
  • 63
    • 0026751682 scopus 로고
    • The E3L gene of vaccinia virus encodes an inhibitor of the interferon-induced, double-stranded RNAdependent protein kinase
    • Chang HW, Watson JC, Jacobs BL. 1992. The E3L gene of vaccinia virus encodes an inhibitor of the interferon-induced, double-stranded RNAdependent protein kinase. Proc Natl Acad Sci U S A 89:4825-4829. http://dx.doi.org/10.1073/pnas.89.11.4825.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 4825-4829
    • Chang, H.W.1    Watson, J.C.2    Jacobs, B.L.3
  • 64
    • 37849041929 scopus 로고    scopus 로고
    • Loss of protein kinase PKR expression in human HeLa cells complements the vaccinia virus E3L deletion mutant phenotype by restoration of viral protein synthesis
    • Zhang P, Jacobs BL, Samuel CE. 2008. Loss of protein kinase PKR expression in human HeLa cells complements the vaccinia virus E3L deletion mutant phenotype by restoration of viral protein synthesis. J Virol 82:840-848. http://dx.doi.org/10.1128/JVI.01891-07.
    • (2008) J Virol , vol.82 , pp. 840-848
    • Zhang, P.1    Jacobs, B.L.2    Samuel, C.E.3
  • 65
    • 84864387040 scopus 로고    scopus 로고
    • Herpes simplex virus 2 infection impacts stress granule accumulation
    • Finnen RL, Pangka KR, Banfield BW. 2012. Herpes simplex virus 2 infection impacts stress granule accumulation. J Virol 86:8119-8130. http://dx.doi.org/10.1128/JVI.00313-12.
    • (2012) J Virol , vol.86 , pp. 8119-8130
    • Finnen, R.L.1    Pangka, K.R.2    Banfield, B.W.3
  • 66
    • 84871997466 scopus 로고    scopus 로고
    • Stress granule formation induced by measles virus is protein kinase PKR dependent and impaired by RNA adenosine deaminase ADAR1
    • Okonski KM, Samuel CE. 2013. Stress granule formation induced by measles virus is protein kinase PKR dependent and impaired by RNA adenosine deaminase ADAR1. J Virol 87:756-766. http://dx.doi.org/10.1128/JVI.02270-12.
    • (2013) J Virol , vol.87 , pp. 756-766
    • Okonski, K.M.1    Samuel, C.E.2
  • 67
    • 79953107370 scopus 로고    scopus 로고
    • Activation of protein kinase R is required for induction of stress granules by respiratory syncytial virus but dispensable for viral replication
    • Lindquist ME, Mainou BA, Dermody TS, Crowe JE, Jr. 2011. Activation of protein kinase R is required for induction of stress granules by respiratory syncytial virus but dispensable for viral replication. Virology 413: 103-110. http://dx.doi.org/10.1016/j.virol.2011.02.009.
    • (2011) Virology , vol.413 , pp. 103-110
    • Lindquist, M.E.1    Mainou, B.A.2    Dermody, T.S.3    Crowe, J.E.4
  • 68
    • 84869019846 scopus 로고    scopus 로고
    • Hepatitis C virus (HCV) induces formation of stress granules whose proteins regulate HCV RNA replication and virus assembly and egress
    • Garaigorta U, Heim MH, Boyd B, Wieland S, Chisari FV. 2012. Hepatitis C virus (HCV) induces formation of stress granules whose proteins regulate HCV RNA replication and virus assembly and egress. J Virol 86:11043-11056. http://dx.doi.org/10.1128/JVI.07101-11.
    • (2012) J Virol , vol.86 , pp. 11043-11056
    • Garaigorta, U.1    Heim, M.H.2    Boyd, B.3    Wieland, S.4    Chisari, F.V.5
  • 70
    • 33644916362 scopus 로고    scopus 로고
    • RNA granules
    • Anderson P, Kedersha N. 2006. RNA granules. J Cell Biol 172:803-808. http://dx.doi.org/10.1083/jcb.200512082.
    • (2006) J Cell Biol , vol.172 , pp. 803-808
    • Anderson, P.1    Kedersha, N.2
  • 72
    • 84898623891 scopus 로고    scopus 로고
    • NF90 exerts antiviral activity through regulation of PKR phosphorylation and stress granules in infected cells
    • Wen X, Huang X, Mok BW, Chen Y, Zheng M, Lau SY, Wang P, Song W, Jin DY, Yuen KY, Chen H. 2014. NF90 exerts antiviral activity through regulation of PKR phosphorylation and stress granules in infected cells. J Immunol 192:3753-3764. http://dx.doi.org/10.4049/jimmunol.1302813.
    • (2014) J Immunol , vol.192 , pp. 3753-3764
    • Wen, X.1    Huang, X.2    Mok, B.W.3    Chen, Y.4    Zheng, M.5    Lau, S.Y.6    Wang, P.7    Song, W.8    Jin, D.Y.9    Yuen, K.Y.10    Chen, H.11
  • 73
    • 81255163730 scopus 로고    scopus 로고
    • The virion host shutoff protein of herpes simplex virus 1 blocks the replication-independent activation of NF-kappaB in dendritic cells in the absence of type I interferon signaling
    • Cotter CR, Kim WK, Nguyen ML, Yount JS, Lopez CB, Blaho JA, Moran TM. 2011. The virion host shutoff protein of herpes simplex virus 1 blocks the replication-independent activation of NF-kappaB in dendritic cells in the absence of type I interferon signaling. J Virol 85:12662-12672. http://dx.doi.org/10.1128/JVI.05557-11.
    • (2011) J Virol , vol.85 , pp. 12662-12672
    • Cotter, C.R.1    Kim, W.K.2    Nguyen, M.L.3    Yount, J.S.4    Lopez, C.B.5    Blaho, J.A.6    Moran, T.M.7

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