The expanding roles of endoplasmic reticulum stress in virus replication and pathogenesis

References

• Ambrose RL, Mackenzie JM. (2011). West Nile Virus differentially modulates the unfolded protein response to facilitate replication and immune evasion. J Virol 85:2723–32
   PubMed Web of Science ®Google Scholar
• Ammosova T, Jerebtsova M, Beullens M, et al. (2003). Nuclear protein phosphatase-1 regulates HIV-1 transcription. J Biol Chem 278:32189–94
   PubMed Web of Science ®Google Scholar
• Andrés G, García-Escudero R, Simón-Mateo C, Viñuela E. (1998). African swine fever virus is enveloped by a two-membraned collapsed cisterna derived from the endoplasmic reticulum. J Virol 72:8988–9001
   PubMed Web of Science ®Google Scholar
• Arzberger S, Hosel M, Protzer U. (2010). Apoptosis of hepatitis B virus-infected hepatocytes prevents release of infectious virus. J Virol 84:11994–2001
   PubMed Web of Science ®Google Scholar
• Baltzis D, Qu LK, Papadopoulou S, et al. (2004). Resistance to vesicular stomatitis virus infection requires a functional cross talk between the eukaryotic translation initiation factor 2alpha kinases PERK and PKR. J Virol 78:12747–61
   PubMed Web of Science ®Google Scholar
• Bamunusinghe D, Seo JK, Rao AL. (2011). Subcellular localization and rearrangement of endoplasmic reticulum by Brome mosaic virus capsid protein. J Virol 85:2953–63
   PubMed Web of Science ®Google Scholar
• Barry G, Fragkoudis R, Ferguson MC, et al. (2010). Semliki forest virus-induced endoplasmic reticulum stress accelerates apoptotic death of mammalian cells. J Virol 84:7369–77
   PubMed Web of Science ®Google Scholar
• Bechill J, Chen Z, Brewer JW, Baker SC. (2008). Coronavirus infection modulates the unfolded protein response and mediates sustained translational repression. J Virol 82:4492–501
   PubMed Web of Science ®Google Scholar
• Benali-Furet NL, Chami M, Houel L, et al. (2005). Hepatitis C virus core triggers apoptosis in liver cells by inducing ER stress and ER calcium depletion. Oncogene 24:4921–33
   PubMed Web of Science ®Google Scholar
• Berlanga JJ, Ventoso I, Harding HP, et al. (2006). Antiviral effect of the mammalian translation initiation factor 2alpha kinase GCN2 against RNA viruses. EMBO J 25:1730–40
   PubMed Web of Science ®Google Scholar
• Bernales S, Papa FR, Walter P. (2006). Intracellular signaling by the unfolded protein response. Annu Rev Cell Dev Biol 22:487–508
   PubMed Web of Science ®Google Scholar
• Bhende PM, Dickerson SJ, Sun X, et al. (2007). X-box-binding protein 1 activates lytic Epstein-Barr virus gene expression in combination with protein kinase D. J Virol 81:7363–70
   PubMed Web of Science ®Google Scholar
• Bitko V, Barik S. (2001). An endoplasmic reticulum-specific stress-activated caspase (caspase-12) is implicated in the apoptosis of A549 epithelial cells by respiratory syncytial virus. J Cell Biochem 80:441–54
   PubMed Web of Science ®Google Scholar
• Bitko V, Shulyayeva O, Mazumder B, et al. (2007). Nonstructural proteins of respiratory syncytial virus suppress premature apoptosis by an NF-kappaB-dependent, interferon-independent mechanism and facilitate virus growth. J Virol 81:1786–95
   PubMed Web of Science ®Google Scholar
• Boyce M, Bryant KF, Jousse C, et al. (2005). A selective inhibitor of eIF2alpha dephosphorylation protects cells from ER stress. Science 307:935–9
   PubMed Web of Science ®Google Scholar
• Brunner JM, Plattet P, Doucey MA, et al. (2012). Morbillivirus Glycoprotein Expression Induces ER Stress, Alters Ca Homeostasis and Results in the Release of Vasostatin. PLoS One 7:e32803
   Web of Science ®Google Scholar
• Brunner JM, Plattet P, Majcherczyk P, et al. (2007). Canine distemper virus infection of primary hippocampal cells induces increase in extracellular glutamate and neurodegeneration. J Neurochem 103:1184–95
   PubMed Web of Science ®Google Scholar
• Buchkovich NJ, Maguire TG, Yu Y, et al. (2008). Human cytomegalovirus specifically controls the levels of the endoplasmic reticulum chaperone BiP/GRP78, which is required for virion assembly. J Virol 82:31–9
   PubMed Web of Science ®Google Scholar
• Bureau C, Bernad J, Chaouche N, et al. (2001). Nonstructural 3 protein of hepatitis C virus triggers an oxidative burst in human monocytes via activation of NADPH oxidase. J Biol Chem 276:23077–83
   PubMed Web of Science ®Google Scholar
• Burnett HF, Audas TE, Liang G, Lu RR. (2012). Herpes simplex virus-1 disarms the unfolded protein response in the early stages of infection. Cell Stress Chaperones 17:473–83
   PubMed Web of Science ®Google Scholar
• Carpenter JE, Jackson W, Benetti L, Grose C. (2011). Autophagosome formation during Varicella-Zoster virus infection following endoplasmic reticulum stress and the unfolded protein response. J Virol 85:9414–24
   PubMed Web of Science ®Google Scholar
• Caselli E, Benedetti S, Gentili V, et al. (2012). Activating transcription factor 4 (ATF4) promotes HIV type 1 activation. AIDS Res Hum Retroviruses 28:907–12
   PubMed Web of Science ®Google Scholar
• Chan CP, Siu KL, Chin KT, et al. (2006). Modulation of the unfolded protein response by the severe acute respiratory syndrome coronavirus spike protein. J Virol 80:9279–87
   PubMed Web of Science ®Google Scholar
• Chan SW, Egan PA. (2005). Hepatitis C virus envelope proteins regulate CHOP via induction of the unfolded protein response. FASEB J 19:1510–12
   PubMed Web of Science ®Google Scholar
• Cheng EH, Wei MC, Weiler S, et al. (2001). BCL-2, BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis. Mol Cell 8:705–11
   PubMed Web of Science ®Google Scholar
• Cheng G, Feng Z, He B. (2005). Herpes simplex virus 1 infection activates the endoplasmic reticulum resident kinase PERK and mediates eIF-2alpha dephosphorylation by the gamma(1)34.5 protein. J Virol 79:1379–88
   PubMed Web of Science ®Google Scholar
• Cho HK, Cheong KJ, Kim HY, Cheong J. (2011). Endoplasmic reticulum stress induced by hepatitis B virus X protein enhances cyclo-oxygenase 2 expression via activating transcription factor 4. Biochem J 435:431–9
   Google Scholar
• Choukhi A, Ung S, Wychowski C, Dubuisson J. (1998). Involvement of endoplasmic reticulum chaperones in the folding of hepatitis C virus glycoproteins. J Virol 72:3851–8
   PubMed Web of Science ®Google Scholar
• Ciczora Y, Callens N, Séron K, et al. (2010). Identification of a dominant endoplasmic reticulum-retention signal in yellow fever virus pre-membrane protein. J Gen Virol 91:404–14
   PubMed Web of Science ®Google Scholar
• DeDiego ML, Nieto-Torres JL, Jimenez-Guardeno JM, et al. (2011). Severe acute respiratory syndrome coronavirus envelope protein regulates cell stress response and apoptosis. PLoS Pathog 7:e1002315
   PubMed Web of Science ®Google Scholar
• de Haan CA, Rottier PJ. (2005). Molecular interactions in the assembly of coronaviruses. Adv Virus Res 64:165–230
   PubMed Web of Science ®Google Scholar
• Dimcheff DE, Askovic S, Baker AH, et al. (2003). Endoplasmic reticulum stress is a determinant of retrovirus-induced spongiform neurodegeneration. J Virol 77:12617–29
   PubMed Web of Science ®Google Scholar
• Dimcheff DE, Faasse MA, McAtee FJ, Portis JL. (2004). Endoplasmic reticulum (ER) stress induced by a neurovirulent mouse retrovirus is associated with prolonged BiP binding and retention of a viral protein in the ER. J Biol Chem 279:33782–90
   Google Scholar
• Edgil D, Polacek C, Harris E. (2006). Dengue virus utilizes a novel strategy for translation initiation when cap-dependent translation is inhibited. J Virol 80:2976–86
   PubMed Web of Science ®Google Scholar
• Einav S, Sobol, HD, Gehrig E, Glenn JS. (2010). The Hepatitis C Virus (HCV) NS4B RNA Binding Inhibitor Clemizole Is Highly Synergistic with HCV Protease Inhibitors. J Infect Dis 202:65–74
   PubMed Web of Science ®Google Scholar
• Elgadi MM, Hayes CE, Smiley JR. (1999). The herpes simplex virus vhs protein induces endoribonucleolytic cleavage of target RNAs in cell extracts. J Virol 73:7153–64
   PubMed Web of Science ®Google Scholar
• Gaddy DF, Lyles DS. (2005). Vesicular stomatitis viruses expressing wild-type or mutant M proteins activate apoptosis through distinct pathways. J Virol 79:4170–9
   PubMed Web of Science ®Google Scholar
• Galindo I, Hernaez B, Munoz-Moreno R, et al. (2012). The ATF6 branch of unfolded protein response and apoptosis are activated to promote African swine fever virus infection. Cell Death Dis 3:e341
   Web of Science ®Google Scholar
• Galluzzi L, Brenner C, Morselli E, et al. (2008). Viral control of mitochondrial apoptosis. PLoS Pathog 4:e1000018
   PubMed Web of Science ®Google Scholar
• Garcia MA, Meurs EF, Esteban M. (2007). The dsRNA protein kinase PKR: virus and cell control. Biochimie 89:799–811
   PubMed Web of Science ®Google Scholar
• Ghendon Y, Markushin S, Heider H, et al. (1986). Haemagglutinin of Influenza A Virus Is a Target for the Antiviral Effect of NorakinR. J Gen Virol 67:1115–22
   PubMed Web of Science ®Google Scholar
• Gong G, Waris G, Tanveer R, Siddiqui A. (2001). Human hepatitis C virus NS5A protein alters intracellular calcium levels, induces oxidative stress, and activates STAT-3 and NF-κB. Proc Natl Acad Sci U S A 98: 9599–604
   Google Scholar
• Gotoh T, Terada K, Oyadomari S, Mori M. (2004). hsp70-DnaJ chaperone pair prevents nitric oxide- and CHOP-induced apoptosis by inhibiting translocation of Bax to mitochondria. Cell Death Differ 11:390–402
   PubMed Web of Science ®Google Scholar
• Harding HP, Novoa I, Zhang Y, et al. (2000). Regulated translation initiation controls stress-induced gene expression in mammalian cells. Mol Cell 6:1099–108
   PubMed Web of Science ®Google Scholar
• Hase T, Summers PL, Ray P, Asafo-Adjei E. (1992). Cytopathology of PC12 cells infected with Japanese encephalitis virus. Virchows Arch B Cell Pathol Incl Mol Pathol 63:25–36
   PubMedGoogle Scholar
• Hassan IH, Zhang MS, Powers LS, et al. (2012). Influenza A Viral replication is blocked by inhibition of the inositol-requiring enzyme 1 (IRE1) stress pathway. J Biol Chem 287:4679–89
   PubMed Web of Science ®Google Scholar
• He B. (2006). Viruses, endoplasmic reticulum stress, and interferon responses. Cell Death Differ 13:393–403
   PubMed Web of Science ®Google Scholar
• He B, Gross M, Roizman B. (1997). The gamma(1)34.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1alpha to dephosphorylate the alpha 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 94:843–8
   PubMed Web of Science ®Google Scholar
• Hegde NR, Chevalier MS, Wisner TW, et al. (2006). The role of BiP in endoplasmic reticulum-associated degradation of major histocompatibility complex class I heavy chain induced by cytomegalovirus proteins. J Biol Chem 281:20910–19
   PubMed Web of Science ®Google Scholar
• Hetz C. (2012). The unfolded protein response: controlling cell fate decisions under ER stress and beyond. Nat Rev Mol Cell Biol 13:89–102
   PubMed Web of Science ®Google Scholar
• Hollien J, Lin JH, Li H, et al. (2009). Regulated Ire1-dependent decay of messenger RNAs in mammalian cells. J Cell Biol 186:323–31
   PubMed Web of Science ®Google Scholar
• Hong JR, Gong HY, Wu JL. (2002). IPNV VP5, a novel anti-apoptosis gene of the Bcl-2 family, regulates Mcl-1 and viral protein expression. Virology 295:217–29
   PubMed Web of Science ®Google Scholar
• Hong JR, Huang LJ, Wu JL. (2005). Aquatic birnavirus induces apoptosis through activated caspase-8 and -3 in a zebrafish cell line. J Fish Dis 28:133–40
   PubMed Web of Science ®Google Scholar
• Hotamisligil GS. (2010). Endoplasmic reticulum stress and the inflammatory basis of metabolic disease. Cell 140:900–17
   PubMed Web of Science ®Google Scholar
• Huang HL, Wu JL, Chen MH, Hong JR. (2011). Aquatic birnavirus-induced ER stress-mediated death signaling contribute to downregulation of Bcl-2 family proteins in salmon embryo cells. PLoS One 6:e22935
   Web of Science ®Google Scholar
• Inoue T, Tsai B. (2013). How viruses use the endoplasmic reticulum for entry, replication, and assembly. Cold Spring Harb Perspect Biol 5, doi:10.1101/cshperspect.a013250
   PubMed Web of Science ®Google Scholar
• Isler JA, Skalet AH, Alwine JC. (2005). Human cytomegalovirus infection activates and regulates the unfolded protein response. J Virol 79:6890–99
   PubMed Web of Science ®Google Scholar
• John L, Thomas S, Herchenroder O, et al. (2011). Hepatitis E virus ORF2 protein activates the pro-apoptotic gene CHOP and anti-Apoptotic heat shock proteins. PLoS One 6:e25378
   Web of Science ®Google Scholar
• Jordan R, Wang L, Graczyk TM, et al. (2002). Replication of a cytopathic strain of bovine viral diarrhea virus activates PERK and induces endoplasmic reticulum stress-mediated apoptosis of MDBK cells. J Virol 76:9588–99
   PubMed Web of Science ®Google Scholar
• Joyce MA, Walters KA, Lamb SE, et al. (2009). HCV induces oxidative and ER stress, and sensitizes infected cells to apoptosis in SCID/Alb-uPA mice. PLoS Pathog 5:e1000291
   PubMed Web of Science ®Google Scholar
• Keay S, Baldwin BR, Smith MW, et al. (1995). Increases in [Ca2+]i mediated by the 92.5-kDa putative cell membrane receptor for HCMV gp86. Am J Physiol 269:C11–21
   Google Scholar
• Kim HT, Waters K, Stoica G, et al. (2004). Activation of endoplasmic reticulum stress signaling pathway is associated with neuronal degeneration in MoMuLV-ts1-induced spongiform encephalomyelopathy. Lab Invest 84:816–27
   PubMed Web of Science ®Google Scholar
• Knoops K, Kikkert M, Worm SH, et al. (2008). SARS-coronavirus replication is supported by a reticulovesicular network of modified endoplasmic reticulum. PLoS Biol 6:e226
   PubMed Web of Science ®Google Scholar
• Kuo CY, Tsai JI, Chou TY, et al. (2012). Apoptosis induced by hepatitis B virus X protein in a CCL13-HBx stable cell line. Oncol Rep 28:127–32
   PubMed Web of Science ®Google Scholar
• Lazar C, Macovei A, Petrescu S, Branza-Nichita N. (2012). Activation of ERAD pathway by human hepatitis B virus modulates viral and subviral particle production. PLoS One 7:e34169
   Web of Science ®Google Scholar
• Lee AH, Iwakoshi NN, Glimcher LH. (2003). XBP-1 regulates a subset of endoplasmic reticulum resident chaperone genes in the unfolded protein response. Mol Cell Biol 23:7448–59
   PubMed Web of Science ®Google Scholar
• Lee DY, Sugden B. (2008a). The latent membrane protein 1 oncogene modifies B-cell physiology by regulating autophagy. Oncogene 27:2833–42
   PubMed Web of Science ®Google Scholar
• Lee DY, Sugden B. (2008b). The LMP1 oncogene of EBV activates PERK and the unfolded protein response to drive its own synthesis. Blood 111:2280–9
   PubMed Web of Science ®Google Scholar
• Lee YH, Wei CW, Wang JJ, Chiou CT. (2011). Rana catesbeiana ribonuclease inhibits Japanese encephalitis virus (JEV) replication and enhances apoptosis of JEV-infected BHK-21 cells. Antiviral Res 89:193–8
   PubMed Web of Science ®Google Scholar
• Leung HJ, Duran EM, Kurtoglu M, et al. (2012). Activation of the unfolded protein response by 2-deoxy-D-glucose inhibits kaposi's sarcoma-associated herpesvirus replication and gene expression. Antimicrob Agents Chemother 56:5794–803
   PubMed Web of Science ®Google Scholar
• Leyssen P, De Clercq E, Neyts J. (2000). Perspectives for the treatment of infections with Flaviviridae. Clin Microbiol Rev 13:67–82
   PubMed Web of Science ®Google Scholar
• Li B, Gao B, Ye L, et al. (2007). Hepatitis B virus X protein (HBx) activates ATF6 and IRE1-XBP1 pathways of unfolded protein response. Virus Res 124:44–9
   PubMed Web of Science ®Google Scholar
• Li J, Liu Y, Wang Z, et al. (2011). Subversion of cellular autophagy machinery by hepatitis B virus for viral envelopment. J Virol 85:6319–33
   PubMed Web of Science ®Google Scholar
• Li S, Ye L, Yu X, et al. (2009). Hepatitis C virus NS4B induces unfolded protein response and endoplasmic reticulum overload response-dependent NF-kappaB activation. Virology 391:257–64
   PubMed Web of Science ®Google Scholar
• Li S, Yu X, Guo Y, Kong L. (2012). Interaction networks of hepatitis C virus NS4B: implications for antiviral therapy. Cell Microbiol 14:994–1002
   PubMed Web of Science ®Google Scholar
• Li XD, Lankinen H, Putkuri N, et al. (2005). Tula hantavirus triggers pro-apoptotic signals of ER stress in Vero E6 cells. Virology 333:180–9
   PubMed Web of Science ®Google Scholar
• Limjindaporn T, Wongwiwat W, Noisakran S, et al. (2009). Interaction of dengue virus envelope protein with endoplasmic reticulum-resident chaperones facilitates dengue virus production. Biochem Biophys Res Commun 379:196–200
   PubMed Web of Science ®Google Scholar
• Lin JH, Walter P, Yen TS. (2008). Endoplasmic reticulum stress in disease pathogenesis. Annu Rev Pathol 3:399–425
   PubMed Web of Science ®Google Scholar
• Lindl KA, Akay C, Wang Y, et al. (2007). Expression of the endoplasmic reticulum stress response marker, BiP, in the central nervous system of HIV-positive individuals. Neuropathol Appl Neurobiol 33:658–69
   PubMed Web of Science ®Google Scholar
• Liu N, Kuang X, Kim HT, et al. (2004). Possible involvement of both endoplasmic reticulum- and mitochondria-dependent pathways in MoMuLV-ts1-induced apoptosis in astrocytes. J Neurovirol 10:189–98
   Web of Science ®Google Scholar
• Machamer CE, Doms RW, Bole DG, et al. (1990). Heavy chain binding protein recognizes incompletely disulfide-bonded forms of vesicular stomatitis virus G protein. J Biol Chem 265:6879–83
   PubMed Web of Science ®Google Scholar
• Mao H, Palmer D, Rosenthal KS. (2001). Changes in BiP (GRP78) levels upon HSV-1 infection are strain dependent. Virus Res 76:127–35
   PubMed Web of Science ®Google Scholar
• Marciniak SJ, Yun CY, Oyadomari S, et al. (2004). CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum. Genes Dev 18:3066–77
   PubMed Web of Science ®Google Scholar
• Martin-Latil S, Mousson L, Autret A, et al. (2007). Bax is activated during rotavirus-induced apoptosis through the mitochondrial pathway. J Virol 81:4457–64
   PubMed Web of Science ®Google Scholar
• Medigeshi GR, Lancaster AM, Hirsch AJ, et al. (2007). West Nile virus infection activates the unfolded protein response, leading to CHOP induction and apoptosis. J Virol 81:10849–60
   PubMed Web of Science ®Google Scholar
• Merquiol E, Uzi D, Mueller T, et al. (2011). HCV causes chronic endoplasmic reticulum stress leading to adaptation and interference with the unfolded protein response. PLoS One 6:e24660
   PubMed Web of Science ®Google Scholar
• Minakshi R, Padhan K, Rani M, et al. (2009). The SARS Coronavirus 3a protein causes endoplasmic reticulum stress and induces ligand-independent downregulation of the type 1 interferon receptor. PLoS One 4:e8342
   PubMed Web of Science ®Google Scholar
• Moradpour D, Penin F, Rice CM. (2007). Replication of hepatitis C virus. Nat Rev Microbiol 5:453–63
   PubMed Web of Science ®Google Scholar
• 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 81:3377–90
   PubMed Web of Science ®Google Scholar
• Mulvey M, Poppers J, Sternberg D, Mohr I. (2003). Regulation of eIF2α Phosphorylation by Different Functions That Act during Discrete Phases in the Herpes Simplex Virus Type 1 Life Cycle. J Virol 77:10917–28
   PubMed Web of Science ®Google Scholar
• Nakhasi HL, Ramanujam M, Atreya CD, et al. (2001). Rubella virus glycoprotein interaction with the endoplasmic reticulum calreticulin and calnexin. Arch Virol 146:1–14
   PubMed Web of Science ®Google Scholar
• Netherton CL, Parsley JC, Wileman T. (2004). African swine fever virus inhibits induction of the stress-induced proapoptotic transcription factor CHOP/GADD153. J Virol 78:10825–8
   PubMed Web of Science ®Google Scholar
• Nie Z, Phenix BN, Lum JJ, et al. (2002). HIV-1 protease processes procaspase 8 to cause mitochondrial release of cytochrome c, caspase cleavage and nuclear fragmentation. Cell Death Differ 9:1172–84
   PubMed Web of Science ®Google Scholar
• Nivitchanyong T, Tsai YC, Betenbaugh MJ, Oyler GA. (2009). An improved in vitro and in vivo Sindbis virus expression system through host and virus engineering. Virus Res 141:1–12
   PubMed Web of Science ®Google Scholar
• Novoa I, Zeng H, Harding HP, Ron D. (2001). Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2alpha. J Cell Biol 153:1011–22
   PubMed Web of Science ®Google Scholar
• Ohoka N, Yoshii S, Hattori T, et al. (2005). TRB3, a novel ER stress-inducible gene, is induced via ATF4-CHOP pathway and is involved in cell death. EMBO J 24:1243–55
   PubMed Web of Science ®Google Scholar
• Oostra M, te Lintelo EG, Deijs M, et al. (2007). Localization and membrane topology of coronavirus nonstructural protein 4: involvement of the early secretory pathway in replication. J Virol 81:12323–36
   PubMed Web of Science ®Google Scholar
• Pasqual G, Burri DJ, Pasquato A, et al. (2011). Role of the host cell's unfolded protein response in arenavirus infection. J Virol 85:1662–70
   PubMed Web of Science ®Google Scholar
• Pavio N, Romano PR, Graczyk TM, et al. (2003). Protein synthesis and endoplasmic reticulum stress can be modulated by the hepatitis C virus envelope protein E2 through the eukaryotic initiation factor 2alpha kinase PERK. J Virol 77:3578–85
   PubMed Web of Science ®Google Scholar
• Pena J, Harris E. (2011). Dengue virus modulates the unfolded protein response in a time-dependent manner. J Biol Chem 286:14226–36
   PubMed Web of Science ®Google Scholar
• Perry JW, Ahmed M, Chang KO, et al. (2012). Antiviral activity of a small molecule deubiquitinase inhibitor occurs via induction of the unfolded protein response. PLoS Pathog 8:e1002783
   PubMed Web of Science ®Google Scholar
• Qian Z, Xuan B, Gualberto N, Yu D. (2011). The human cytomegalovirus protein pUL38 suppresses endoplasmic reticulum stress-mediated cell death independently of its ability to induce mTORC1 activation. J Virol 85:9103–13
   PubMed Web of Science ®Google Scholar
• Rathore AP, Ng ML, Vasudevan SG. (2013). Differential unfolded protein response during Chikungunya and Sindbis virus infection: CHIKV nsP4 suppresses eIF2alpha phosphorylation. Virol J 10:36
   PubMed Web of Science ®Google Scholar
• Rider TH, Zook CE, Boettcher TL, et al. (2011). Broad-spectrum antiviral therapeutics. PLoS One 6:e22572
   PubMed Web of Science ®Google Scholar
• Rivera J, Abrams C, Hernaez B, et al. (2007). The MyD116 African swine fever virus homologue interacts with the catalytic subunit of protein phosphatase 1 and activates its phosphatase activity. J Virol 81:2923–29
   PubMed Web of Science ®Google Scholar
• Ritzenthaler C, Laporte C, Gaire F, et al. (2002). Grapevine fanleaf virus replication occurs on endoplasmic reticulum-derived membranes. J Virol 76:8808–19
   PubMed Web of Science ®Google Scholar
• Roberson EC, Tully JE, Guala AS, et al. (2012). Influenza induces endoplasmic reticulum stress, caspase-12-dependent apoptosis, and c-Jun N-terminal kinase-mediated transforming growth factor-beta release in lung epithelial cells. Am J Respir Cell Mol Biol 46:573–81
   PubMed Web of Science ®Google Scholar
• Robert F, Kapp LD, Khan SN, et al. (2006). Initiation of protein synthesis by Hepatitis C virus Is refractory to reduced eIF2 ċ GTP ċ Met-tRNAiMet ternary complex availability. Mol Biol Cell 17:4632–44
   PubMed Web of Science ®Google Scholar
• Rodrigues R, Paranhos-Baccala G, Vernet G, Peyrefitte CN. (2012). Crimean-Congo hemorrhagic fever virus-infected hepatocytes induce ER-stress and apoptosis crosstalk. PLoS One 7:e29712
   PubMed Web of Science ®Google Scholar
• Ron D, Hampton RY. (2004). Membrane biogenesis and the unfolded protein response. J Cell Biol 167:23–5
   PubMed Web of Science ®Google Scholar
• Schroder M, Kaufman RJ. (2005). The mammalian unfolded protein response. Annu Rev Biochem 74:739–89
   PubMed Web of Science ®Google Scholar
• Schweizer M, Peterhans E. (1999). Oxidative stress in cells infected with bovine viral diarrhoea virus: a crucial step in the induction of apoptosis. J Gen Virol 80:1147–55
   PubMed Web of Science ®Google Scholar
• Shaffer AL, Shapiro-Shelef M, Iwakoshi NN, et al. (2004). XBP1, downstream of Blimp-1, expands the secretory apparatus and other organelles, and increases protein synthesis in plasma cell differentiation. Immunity 21:81–93
   PubMed Web of Science ®Google Scholar
• Shah AC, Parker JN, Shimamura M, Cassady KA. (2009). Spontaneous and engineered compensatory HSV mutants that counteract the host antiviral PKR response. Viruses 1:510–22
   PubMed Web of Science ®Google Scholar
• Sharon-Friling R, Goodhouse J, Colberg-Poley AM, Shenk T. (2006). Human cytomegalovirus pUL37x1 induces the release of endoplasmic reticulum calcium stores. Proc Natl Acad Sci U S A 103:19117–22
   PubMed Web of Science ®Google Scholar
• Sidrauski C, Walter P. (1997). The transmembrane kinase Ire1p is a site-specific endonuclease that initiates mRNA splicing in the unfolded protein response. Cell 90:1031–9
   PubMed Web of Science ®Google Scholar
• Skaletskaya A, Bartle LM, Chittenden T, et al. (2001). A cytomegalovirus-encoded inhibitor of apoptosis that suppresses caspase-8 activation. Proc Natl Acad Sci U S A 98:7829–34
   PubMed Web of Science ®Google Scholar
• Su HL, Liao CL, Lin YL. (2002). Japanese Encephalitis Virus infection initiates endoplasmic reticulum stress and an unfolded protein response. J Virol 76:4162–71
   PubMed Web of Science ®Google Scholar
• Su YC, Wu JL, Hong JR. (2011). Betanodavirus up-regulates chaperone GRP78 via ER stress: roles of GRP78 in viral replication and host mitochondria-mediated cell death. Apoptosis 16:272–87
   PubMed Web of Science ®Google Scholar
• Suhy DA, Giddings TH Jr, Kirkegaard K. (2000). Remodeling the endoplasmic reticulum by poliovirus infection and by individual viral proteins: an autophagy-like origin for virus-induced vesicles. J Virol 74:8953–65
   PubMed Web of Science ®Google Scholar
• Sun CC, Thorley-Lawson DA. (2007). Plasma cell-specific transcription factor XBP-1s binds to and transactivates the Epstein-Barr virus BZLF1 promoter. J Virol 81:13566–77
   PubMed Web of Science ®Google Scholar
• Sun M, Rothermel TA, Shuman L, et al. (2004). Conserved cysteine-rich domain of paramyxovirus simian virus 5 V protein plays an important role in blocking apoptosis. J Virol 78:5068–78
   PubMed Web of Science ®Google Scholar
• Sung SC, Chao CY, Jeng KS, et al. (2009). The 8ab protein of SARS-CoV is a luminal ER membrane-associated protein and induces the activation of ATF6. Virology 387:402–13
   PubMed Web of Science ®Google Scholar
• Szegezdi E, Logue SE, Gorman AM, Samali A. (2006). Mediators of endoplasmic reticulum stress-induced apoptosis. EMBO Rep 7:880–5
   PubMed Web of Science ®Google Scholar
• Tabas I, Ron D. (2011). Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress. Nat Cell Biol 13:184–90
   PubMed Web of Science ®Google Scholar
• Tabata Y, Takano K, Ito T, et al. (2007). Vaticanol B, a resveratrol tetramer, regulates endoplasmic reticulum stress and inflammation. Am J Physiol Cell Physiol 293:C411–8
   PubMed Web of Science ®Google Scholar
• Tardif KD, Mori K, Kaufman RJ, Siddiqui A. (2004). Hepatitis C virus suppresses the IRE1-XBP1 pathway of the unfolded protein response. J Biol Chem 279:17158–64
   PubMed Web of Science ®Google Scholar
• Taylor GM, Raghuwanshi SK, Rowe DT, et al. (2011). Endoplasmic reticulum stress causes EBV lytic replication. Blood 118:5528–39
   PubMed Web of Science ®Google Scholar
• Tirosh B, Iwakoshi NN, Lilley BN, et al. (2005). Human cytomegalovirus protein US11 provokes an unfolded protein response that may facilitate the degradation of class I major histocompatibility complex products. J Virol 79:2768–79
   PubMed Web of Science ®Google Scholar
• Tolonen N, Doglio L, Schleich S, Krijnse Locker J. (2001). Vaccinia virus DNA replication occurs in endoplasmic reticulum-enclosed cytoplasmic mini-nuclei. Mol Biol Cell 12:2031–46
   PubMed Web of Science ®Google Scholar
• Trujillo-Alonso V, Maruri-Avidal L, Arias CF, Lopez S. (2011). Rotavirus infection induces the unfolded protein response of the cell and controls it through the nonstructural protein NSP3. J Virol 85:12594–604
   PubMed Web of Science ®Google Scholar
• Umareddy I, Pluquet O, Wang QY, et al. (2007). Dengue virus serotype infection specifies the activation of the unfolded protein response. Virol J 4:91
   PubMed Web of Science ®Google Scholar
• Urano F, Wang X, Bertolotti A, et al. (2000). Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1. Science 287:664–6
   PubMed Web of Science ®Google Scholar
• Urban C, Rheme C, Maerz S, et al. (2008). Apoptosis induced by Semliki Forest virus is RNA replication dependent and mediated via Bak. Cell Death Differ 15:1396–407
   PubMed Web of Science ®Google Scholar
• van Kuppeveld FJ, Hoenderop JG, Smeets RL, et al. (1997). Coxsackievirus protein 2B modifies endoplasmic reticulum membrane and plasma membrane permeability and facilitates virus release. EMBO J 16:3519–32
   PubMed Web of Science ®Google Scholar
• Ventoso I, Sanz MA, Molina S, et al. (2006). Translational resistance of late alphavirus mRNA to eIF2alpha phosphorylation: a strategy to overcome the antiviral effect of protein kinase PKR. Genes Dev 20:87–100
   PubMed Web of Science ®Google Scholar
• Versteeg GA, van de Nes PS, Bredenbeek PJ, Spaan WJ. (2007). The coronavirus spike protein induces endoplasmic reticulum stress and upregulation of intracellular chemokine mRNA concentrations. J Virol 81:10981–90
   PubMed Web of Science ®Google Scholar
• von dem Bussche A, Machida R, Li K, et al. (2010). Hepatitis C virus NS2 protein triggers endoplasmic reticulum stress and suppresses its own viral replication. J Hepatol 53:797–804
   PubMedGoogle Scholar
• Walter P, Ron D. (2011). The unfolded protein response: from stress pathway to homeostatic regulation. Science 334:1081–6
   PubMed Web of Science ®Google Scholar
• Watowich SS, Morimoto RI, Lamb RA. (1991). Flux of the paramyxovirus hemagglutinin-neuraminidase glycoprotein through the endoplasmic reticulum activates transcription of the GRP78-BiP gene. J Virol 65:3590–7
   PubMed Web of Science ®Google Scholar
• Wu HC, Wu JL, Chu HL, et al. (2010). RGNNV induces mitochondria-mediated cell death via newly synthesized protein dependent pathway in fish cells. Fish Shellfish Immunol 29:451–63
   PubMed Web of Science ®Google Scholar
• Wu YP, Chang CM, Hung CY, et al. (2011). Japanese encephalitis virus co-opts the ER-stress response protein GRP78 for viral infectivity. Virol J 8:128
   PubMed Web of Science ®Google Scholar
• Xu X, Zhang H, Zhang Q, et al. (2013a). Porcine epidemic diarrhea virus E protein causes endoplasmic reticulum stress and up-regulates interleukin-8 expression. Virol J 10:26
   PubMed Web of Science ®Google Scholar
• Xu X, Zhang H, Zhang Q, et al. (2013b). Porcine epidemic diarrhea virus N protein prolongs S-phase cell cycle, induces endoplasmic reticulum stress, and up-regulates interleukin-8 expression. Vet Microbiol 164:212–21
   PubMed Web of Science ®Google Scholar
• Xuan B, Qian Z, Torigoi E, Yu D. (2009). Human cytomegalovirus protein pUL38 induces ATF4 expression, inhibits persistent JNK phosphorylation, and suppresses endoplasmic reticulum stress-induced cell death. J Virol 83:3463–74
   PubMed Web of Science ®Google Scholar
• Yamaguchi H, Wang HG. (2004). CHOP is involved in endoplasmic reticulum stress-induced apoptosis by enhancing DR5 expression in human carcinoma cells. J Biol Chem 279:45495–502
   PubMed Web of Science ®Google Scholar
• Yan W, Frank CL, Korth MJ, et al. (2002). Control of PERK eIF2alpha kinase activity by the endoplasmic reticulum stress-induced molecular chaperone P58IPK. Proc Natl Acad Sci U S A 99:15920–5
   PubMed Web of Science ®Google Scholar
• Ye C, Dickman MB, Whitham SA, et al. (2011). The unfolded protein response is triggered by a plant viral movement protein. Plant Physiol 156:741–55
   PubMed Web of Science ®Google Scholar
• Ye J, Rawson RB, Komuro R, et al. (2000). ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs. Mol Cell 6:1355–64
   PubMed Web of Science ®Google Scholar
• Yee J, White RE, Anderton E, Allday MJ. (2011). Latent Epstein-Barr virus can inhibit apoptosis in B cells by blocking the Induction of NOXA Expression. PLoS One 6:e28506
   Web of Science ®Google Scholar
• Yoshida H, Matsui T, Yamamoto A, et al. (2001). XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell 107:881–91
   PubMed Web of Science ®Google Scholar
• Yu CY, Hsu YW, Liao CL, Lin YL. (2006). Flavivirus infection activates the XBP1 pathway of the unfolded protein response to cope with endoplasmic reticulum stress. J Virol 80:11868–80
   PubMed Web of Science ®Google Scholar
• Yu H, Li S, Yang C, et al. (2011). Homology model and potential virus-capsid binding site of a putative HEV receptor Grp78. J Mol Model 17:987–95
   PubMed Web of Science ®Google Scholar
• Zhang HM, Ye X, Su Y, et al. (2010). Coxsackievirus B3 infection activates the unfolded protein response and induces apoptosis through downregulation of p58IPK and activation of CHOP and SREBP1. J Virol 84:8446–59
   PubMed Web of Science ®Google Scholar
• Zhang K, Kaufman RJ. (2008). From endoplasmic-reticulum stress to the inflammatory response. Nature 454:455–62
   PubMed Web of Science ®Google Scholar
• Zhong Y, Liao Y, Fang S, et al. (2012). Up-regulation of Mcl-1 and Bak by coronavirus infection of human, avian and animal cells modulates apoptosis and viral replication. PLoS One 7:e30191
   Web of Science ®Google Scholar