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Volumn 37, Issue , 2017, Pages 17-27

Interaction of the innate immune system with positive-strand RNA virus replication organelles

Author keywords

+RNA virus; GTPases; Interferon; Replication organelles

Indexed keywords

ANTIVIRUS AGENT; CYTOKINE; GUANOSINE TRIPHOSPHATASE; INTERFERON; MICROTUBULE ASSOCIATED PROTEIN 1; PATHOGEN ASSOCIATED MOLECULAR PATTERN; UBIQUITIN; VIRAL PROTEIN; VIRUS RNA;

EID: 85022201891     PISSN: 13596101     EISSN: 18790305     Source Type: Journal    
DOI: 10.1016/j.cytogfr.2017.05.007     Document Type: Short Survey
Times cited : (52)

References (146)
  • 1
    • 84982170421 scopus 로고    scopus 로고
    • Innate immune evasion strategies of DNA and RNA viruses
    • Beachboard, D.C., Horner, S.M., Innate immune evasion strategies of DNA and RNA viruses. Curr. Opin. Microbiol. 32 (2016), 113–119, 10.1016/j.mib.2016.05.015.
    • (2016) Curr. Opin. Microbiol. , vol.32 , pp. 113-119
    • Beachboard, D.C.1    Horner, S.M.2
  • 2
    • 31344461659 scopus 로고    scopus 로고
    • Innate immune recognition of viral infection
    • Kawai, T., Akira, S., Innate immune recognition of viral infection. Nat. Immunol. 7 (2006), 131–137, 10.1038/ni1303.
    • (2006) Nat. Immunol. , vol.7 , pp. 131-137
    • Kawai, T.1    Akira, S.2
  • 3
    • 34548129595 scopus 로고    scopus 로고
    • The response of mammalian cells to double-stranded RNA
    • Gantier, M.P., Williams, B.R.G., The response of mammalian cells to double-stranded RNA. Cytokine Growth Factor Rev. 18 (2007), 363–371, 10.1016/j.cytogfr.2007.06.016.
    • (2007) Cytokine Growth Factor Rev. , vol.18 , pp. 363-371
    • Gantier, M.P.1    Williams, B.R.G.2
  • 4
    • 84927639135 scopus 로고    scopus 로고
    • Innate immune pattern recognition: a cell biological perspective
    • Brubaker, S.W., Bonham, K.S., Zanoni, I., Kagan, J.C., Innate immune pattern recognition: a cell biological perspective. Annu. Rev. Immunol. 33 (2015), 257–290, 10.1146/annurev-immunol-032414-112240.
    • (2015) Annu. Rev. Immunol. , vol.33 , pp. 257-290
    • Brubaker, S.W.1    Bonham, K.S.2    Zanoni, I.3    Kagan, J.C.4
  • 5
    • 84933677563 scopus 로고    scopus 로고
    • Emerging complexity and new roles for the RIG-I-like receptors in innate antiviral immunity
    • Errett, J.S., Gale, M., Emerging complexity and new roles for the RIG-I-like receptors in innate antiviral immunity. Virol. Sin. 30 (2015), 163–173, 10.1007/s12250-015-3604-5.
    • (2015) Virol. Sin. , vol.30 , pp. 163-173
    • Errett, J.S.1    Gale, M.2
  • 6
    • 84904967279 scopus 로고    scopus 로고
    • New functions of mitochondria associated membranes in cellular signaling
    • van Vliet, A.R., Verfaillie, T., Agostinis, P., New functions of mitochondria associated membranes in cellular signaling. Biochim. Biophys. Acta Mol. Cell Res. 1843 (2014), 2253–2262, 10.1016/j.bbamcr.2014.03.009.
    • (2014) Biochim. Biophys. Acta Mol. Cell Res. , vol.1843 , pp. 2253-2262
    • van Vliet, A.R.1    Verfaillie, T.2    Agostinis, P.3
  • 7
    • 84976272220 scopus 로고    scopus 로고
    • The coming of age of the mitochondria–ER contact: a matter of thickness
    • Giacomello, M., Pellegrini, L., The coming of age of the mitochondria–ER contact: a matter of thickness. Cell Death Differ. 23 (2016), 1417–1427, 10.1038/cdd.2016.52.
    • (2016) Cell Death Differ. , vol.23 , pp. 1417-1427
    • Giacomello, M.1    Pellegrini, L.2
  • 8
    • 84925723974 scopus 로고    scopus 로고
    • Mechanisms of innate immune evasion in re-emerging RNA viruses
    • Ma, D.Y., Suthar, M.S., Mechanisms of innate immune evasion in re-emerging RNA viruses. Curr. Opin. Virol. 12 (2015), 26–37, 10.1016/j.coviro.2015.02.005.
    • (2015) Curr. Opin. Virol. , vol.12 , pp. 26-37
    • Ma, D.Y.1    Suthar, M.S.2
  • 9
    • 84967215091 scopus 로고    scopus 로고
    • Viral evasion of intracellular DNA and RNA sensing
    • Kai Chan, Y., Gack, M.U., Viral evasion of intracellular DNA and RNA sensing. Nat. Publ. Gr. 14 (2016), 360–373, 10.1038/nrmicro.2016.45.
    • (2016) Nat. Publ. Gr. , vol.14 , pp. 360-373
    • Kai Chan, Y.1    Gack, M.U.2
  • 10
    • 42349086670 scopus 로고    scopus 로고
    • Modification of intracellular membrane structures for virus replication
    • Miller, S., Krijnse-Locker, J., Modification of intracellular membrane structures for virus replication. Nat. Rev. Microbiol. 6 (2008), 363–374, 10.1038/nrmicro1890.
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 363-374
    • Miller, S.1    Krijnse-Locker, J.2
  • 11
    • 77958176122 scopus 로고    scopus 로고
    • Cytoplasmic viral replication complexes
    • Den Boon, J.A., Diaz, A., Ahlquist, P., Cytoplasmic viral replication complexes. Cell Host Microbe. 8 (2010), 77–85, 10.1016/j.chom.2010.06.010.
    • (2010) Cell Host Microbe. , vol.8 , pp. 77-85
    • Den Boon, J.A.1    Diaz, A.2    Ahlquist, P.3
  • 12
    • 84904631176 scopus 로고    scopus 로고
    • Membranous replication factories induced by plus-strand RNA viruses
    • Romero-Brey, I., Bartenschlager, R., Membranous replication factories induced by plus-strand RNA viruses. Viruses 6 (2014), 2826–2857, 10.3390/v6072826.
    • (2014) Viruses , vol.6 , pp. 2826-2857
    • Romero-Brey, I.1    Bartenschlager, R.2
  • 13
    • 84927034590 scopus 로고    scopus 로고
    • Does form meet function in the coronavirus replicative organelle?
    • Neuman, B.W., Angelini, M.M., Buchmeier, M.J., Does form meet function in the coronavirus replicative organelle?. Trends Microbiol. 22 (2014), 642–647, 10.1016/j.tim.2014.06.003.
    • (2014) Trends Microbiol. , vol.22 , pp. 642-647
    • Neuman, B.W.1    Angelini, M.M.2    Buchmeier, M.J.3
  • 15
    • 0242720705 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome: global initiatives for disease diagnosis
    • Groneberg, D.A., Zhang, L., Welte, T., Zabel, P., Chung, K.F., Severe acute respiratory syndrome: global initiatives for disease diagnosis. QJM 96 (2003), 845–852 http://www.ncbi.nlm.nih.gov/pubmed/14566040.
    • (2003) QJM , vol.96 , pp. 845-852
    • Groneberg, D.A.1    Zhang, L.2    Welte, T.3    Zabel, P.4    Chung, K.F.5
  • 16
    • 85008414667 scopus 로고    scopus 로고
    • Outbreak of Middle East respiratory syndrome coronavirus in Saudi Arabia: a retrospective study
    • Aleanizy, F.S., Mohmed, N., Alqahtani, F.Y., El Hadi Mohamed, R.A., Outbreak of Middle East respiratory syndrome coronavirus in Saudi Arabia: a retrospective study. BMC Infect. Dis., 17, 2017, 23, 10.1186/s12879-016-2137-3.
    • (2017) BMC Infect. Dis. , vol.17 , pp. 23
    • Aleanizy, F.S.1    Mohmed, N.2    Alqahtani, F.Y.3    El Hadi Mohamed, R.A.4
  • 17
    • 84986209043 scopus 로고    scopus 로고
    • Zika: the origin and spread of a mosquito-borne virus
    • Kay, M., Allen, T., Frank, V., Santhana, S., Dye, C., Zika: the origin and spread of a mosquito-borne virus. World Heal. Organ., 2016, 1–18, 10.2471/BLT.16.171082.
    • (2016) World Heal. Organ. , pp. 1-18
    • Kay, M.1    Allen, T.2    Frank, V.3    Santhana, S.4    Dye, C.5
  • 18
    • 84971389562 scopus 로고    scopus 로고
    • (+) RNA virus replication compartments: a safe home for (most) viral replication
    • Shulla, A., Randall, G., (+) RNA virus replication compartments: a safe home for (most) viral replication. Curr. Opin. Microbiol. 32 (2016), 82–88, 10.1016/j.mib.2016.05.003.
    • (2016) Curr. Opin. Microbiol. , vol.32 , pp. 82-88
    • Shulla, A.1    Randall, G.2
  • 19
    • 84885998217 scopus 로고    scopus 로고
    • Architecture and biogenesis of plus-strand RNA virus replication factories
    • Paul, D., Bartenschlager, R., Architecture and biogenesis of plus-strand RNA virus replication factories. World J. Virol. May 12 (2013), 32–48, 10.5501/wjv.v2.i2.32.
    • (2013) World J. Virol. May , vol.12 , pp. 32-48
    • Paul, D.1    Bartenschlager, R.2
  • 20
    • 84930039894 scopus 로고    scopus 로고
    • New insights on the role of paired membrane structures in coronavirus replication
    • V'kovski, P., Al-Mulla, H., Thiel, V., Neuman, B.W., New insights on the role of paired membrane structures in coronavirus replication. Virus Res. 202 (2015), 33–40, 10.1016/j.virusres.2014.12.021.
    • (2015) Virus Res. , vol.202 , pp. 33-40
    • V'kovski, P.1    Al-Mulla, H.2    Thiel, V.3    Neuman, B.W.4
  • 22
    • 0014350984 scopus 로고
    • Cytoplasmic structures associated with an arbovirus infection: loci of viral ribonucleic acid synthesis
    • Grimley, P.M., Berezesky, I.K., Friedman, R.M., Cytoplasmic structures associated with an arbovirus infection: loci of viral ribonucleic acid synthesis. J. Virol. 2 (1968), 1326–1338.
    • (1968) J. Virol. , vol.2 , pp. 1326-1338
    • Grimley, P.M.1    Berezesky, I.K.2    Friedman, R.M.3
  • 23
    • 0035082679 scopus 로고    scopus 로고
    • Biogenesis of the Semliki Forest virus RNA replication complex
    • Kujala, P., Ikaheimonen, A., Ehsani, N., Vihinen, H., Auvinen, P., Kaariainen, L., Biogenesis of the Semliki Forest virus RNA replication complex. J. Virol. 75 (2001), 3873–3884, 10.1128/JVI.75.8.3873-3884.2001.
    • (2001) J. Virol. , vol.75 , pp. 3873-3884
    • Kujala, P.1    Ikaheimonen, A.2    Ehsani, N.3    Vihinen, H.4    Auvinen, P.5    Kaariainen, L.6
  • 24
    • 34548679815 scopus 로고    scopus 로고
    • Three-dimensional analysis of a viral RNA replication complex reveals a virus-induced mini-organelle
    • (07-PLBI-RA-0823 [pii]\r10.1371/journal.pbio.0050220)
    • Kopek, B.G., Perkins, G., Miller, D.J., Ellisman, M.H., Ahlquist, P., Three-dimensional analysis of a viral RNA replication complex reveals a virus-induced mini-organelle. PLoS Biol., 5, 2007, e220 (07-PLBI-RA-0823 [pii]\r10.1371/journal.pbio.0050220).
    • (2007) PLoS Biol. , vol.5 , pp. e220
    • Kopek, B.G.1    Perkins, G.2    Miller, D.J.3    Ellisman, M.H.4    Ahlquist, P.5
  • 25
    • 0024237292 scopus 로고
    • Alphavirus RNA replicase is located on the cytoplasmic surface of endosomes and lysosomes
    • Froshauer, S., Kartenbeck, J., Helenius, A., Alphavirus RNA replicase is located on the cytoplasmic surface of endosomes and lysosomes. J. Cell Biol. 107 (1988), 2075–2086, 10.1371/journal.pbio.0050220.
    • (1988) J. Cell Biol. , vol.107 , pp. 2075-2086
    • Froshauer, S.1    Kartenbeck, J.2    Helenius, A.3
  • 26
    • 84897546853 scopus 로고    scopus 로고
    • Ultrastructural characterization and three-dimensional architecture of replication sites in dengue virus-infected mosquito cells
    • Junjhon, J., Pennington, J.G., Edwards, T.J., Perera, R., Lanman, J., Kuhn, R.J., Ultrastructural characterization and three-dimensional architecture of replication sites in dengue virus-infected mosquito cells. J. Virol. 88 (2014), 4687–4697, 10.1128/JVI. 00118-14.
    • (2014) J. Virol. , vol.88 , pp. 4687-4697
    • Junjhon, J.1    Pennington, J.G.2    Edwards, T.J.3    Perera, R.4    Lanman, J.5    Kuhn, R.J.6
  • 28
    • 84921676359 scopus 로고    scopus 로고
    • Mutations across murine hepatitis virus nsp4 alter virus fitness and membrane modifications
    • Beachboard, D.C., Anderson-Daniels, J.M., Denison, M.R., Mutations across murine hepatitis virus nsp4 alter virus fitness and membrane modifications. J. Virol. 89 (2015), 2080–2089, 10.1128/JVI.02776-14.
    • (2015) J. Virol. , vol.89 , pp. 2080-2089
    • Beachboard, D.C.1    Anderson-Daniels, J.M.2    Denison, M.R.3
  • 29
    • 84899705424 scopus 로고    scopus 로고
    • Competitive fitness in coronaviruses is not correlated with size or number of double-membrane vesicles under reduced-temperature growth conditions
    • Al-Mulla, H.M.N., Turrell, L., Smith, N.M., Payne, L., Baliji, S., Züst, R., Thiel, V., Baker, S.C., Siddell, S.G., Neuman, B.W., Competitive fitness in coronaviruses is not correlated with size or number of double-membrane vesicles under reduced-temperature growth conditions. MBio, 5, 2014, 10.1128/mBio.01107-13.
    • (2014) MBio , vol.5
    • Al-Mulla, H.M.N.1    Turrell, L.2    Smith, N.M.3    Payne, L.4    Baliji, S.5    Züst, R.6    Thiel, V.7    Baker, S.C.8    Siddell, S.G.9    Neuman, B.W.10
  • 31
    • 84857815535 scopus 로고    scopus 로고
    • Ultrastructural characterization of arterivirus replication structures: reshaping the endoplasmic reticulum to accommodate viral RNA synthesis
    • Knoops, K., Barcena, M., Limpens, R.W. a. L., Koster, a. J., Mommaas, a. M., Snijder, E.J., Ultrastructural characterization of arterivirus replication structures: reshaping the endoplasmic reticulum to accommodate viral RNA synthesis. J. Virol. 86 (2012), 2474–2487, 10.1128/JVI.06677-11.
    • (2012) J. Virol. , vol.86 , pp. 2474-2487
    • Knoops, K.1    Barcena, M.2    Limpens, R.W.A.L.3    Koster, A.J.4    Mommaas, A.M.5    Snijder, E.J.6
  • 32
    • 0036100578 scopus 로고    scopus 로고
    • Expression of hepatitis C virus proteins induces distinct membrane alterations including a candidate viral replication complex
    • Egger, D., Wölk, B., Gosert, R., Bianchi, L., Blum, H.E., Moradpour, D., Bienz, K., Expression of hepatitis C virus proteins induces distinct membrane alterations including a candidate viral replication complex. J. Virol. 76 (2002), 5974–5984, 10.1128/JVI.76.12.5974.
    • (2002) J. Virol. , vol.76 , pp. 5974-5984
    • Egger, D.1    Wölk, B.2    Gosert, R.3    Bianchi, L.4    Blum, H.E.5    Moradpour, D.6    Bienz, K.7
  • 33
    • 0035008260 scopus 로고    scopus 로고
    • Non-structural proteins 2 and 3 interact to modify host cell membranes during the formation of the arterivirus replication complex
    • Snijder, E.J., Van Tol, H., Roos, N., Pedersen, K.W., Non-structural proteins 2 and 3 interact to modify host cell membranes during the formation of the arterivirus replication complex. J. Gen. Virol. 82 (2001), 985–994, 10.1099/vir.0.17499-0.
    • (2001) J. Gen. Virol. , vol.82 , pp. 985-994
    • Snijder, E.J.1    Van Tol, H.2    Roos, N.3    Pedersen, K.W.4
  • 34
    • 84883321889 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome coronavirus nonstructural proteins 3, 4, and 6 Induce double-membrane vesicles
    • Editor.
    • Angelini, M., Akhlaghpour, M., Severe acute respiratory syndrome coronavirus nonstructural proteins 3, 4, and 6 Induce double-membrane vesicles. MBio 4 (2013), 1–10, 10.1128/mBio.00524-13 Editor.
    • (2013) MBio , vol.4 , pp. 1-10
    • Angelini, M.1    Akhlaghpour, M.2
  • 37
    • 35549003579 scopus 로고    scopus 로고
    • Regulation of interferon-γ during innate and adaptive immune responses
    • Schoenborn, J.R., Wilson, C.B., Regulation of interferon-γ during innate and adaptive immune responses. Adv. Immunol. 96 (2007), 41–101, 10.1016/S0065-2776(07)96002-2.
    • (2007) Adv. Immunol. , vol.96 , pp. 41-101
    • Schoenborn, J.R.1    Wilson, C.B.2
  • 38
    • 77955872789 scopus 로고    scopus 로고
    • Mechanisms of type III interferon expression
    • Iversen, M.B., Paludan, S.R., Mechanisms of type III interferon expression. J. Interferon Cytokine Res. 30 (2010), 573–578, 10.1089/jir.2010.0063.
    • (2010) J. Interferon Cytokine Res. , vol.30 , pp. 573-578
    • Iversen, M.B.1    Paludan, S.R.2
  • 39
    • 42949160129 scopus 로고    scopus 로고
    • IFN-lambda (IFN-??) is expressed in a tissue-dependent fashion and primarily acts on epithelial cells in vivo
    • Sommereyns, C., Paul, S., Staeheli, P., Michiels, T., IFN-lambda (IFN-??) is expressed in a tissue-dependent fashion and primarily acts on epithelial cells in vivo. PLoS Pathog., 4, 2008, 10.1371/journal.ppat.1000017.
    • (2008) PLoS Pathog. , vol.4
    • Sommereyns, C.1    Paul, S.2    Staeheli, P.3    Michiels, T.4
  • 40
  • 41
    • 5144219591 scopus 로고    scopus 로고
    • Interferon-beta and interferon-gamma synergistically inhibit the replication of severe acute respiratory syndrome-associated coronavirus (SARS-CoV)
    • Sainz, B., Mossel, E.C., Peters, C.J., Garry, R.F., Interferon-beta and interferon-gamma synergistically inhibit the replication of severe acute respiratory syndrome-associated coronavirus (SARS-CoV). Virology 329 (2004), 11–17, 10.1016/j.virol.2004.08.011.
    • (2004) Virology , vol.329 , pp. 11-17
    • Sainz, B.1    Mossel, E.C.2    Peters, C.J.3    Garry, R.F.4
  • 42
    • 33845445764 scopus 로고    scopus 로고
    • Evaluation of immunomodulators, interferons and known in vitro SARS-CoV inhibitors for inhibition of SARS-CoV replication in BALB/c mice, Antivir
    • Barnard, D.L., Day, C.W., Bailey, K., Heiner, M., Montgomery, R., Lauridsen, L., Chan, P.K.S., Sidwell, R.W., Evaluation of immunomodulators, interferons and known in vitro SARS-CoV inhibitors for inhibition of SARS-CoV replication in BALB/c mice, Antivir. Chem. Chemother. 17 (2006), 275–284.
    • (2006) Chem. Chemother. , vol.17 , pp. 275-284
    • Barnard, D.L.1    Day, C.W.2    Bailey, K.3    Heiner, M.4    Montgomery, R.5    Lauridsen, L.6    Chan, P.K.S.7    Sidwell, R.W.8
  • 43
    • 78650964144 scopus 로고    scopus 로고
    • Single-dose intranasal administration with mDEF201 (adenovirus vectored mouse interferon-alpha) confers protection from mortality in a lethal SARS-CoV BALB/c mouse model
    • Kumaki, Y., Ennis, J., Rahbar, R., Turner, J.D., Wandersee, M.K., Smith, A.J., Bailey, K.W., Vest, Z.G., Madsen, J.R., Li, J.K.K., Barnard, D.L., Single-dose intranasal administration with mDEF201 (adenovirus vectored mouse interferon-alpha) confers protection from mortality in a lethal SARS-CoV BALB/c mouse model. Antiviral Res. 89 (2011), 75–82, 10.1016/j.antiviral.2010.11.007.
    • (2011) Antiviral Res. , vol.89 , pp. 75-82
    • Kumaki, Y.1    Ennis, J.2    Rahbar, R.3    Turner, J.D.4    Wandersee, M.K.5    Smith, A.J.6    Bailey, K.W.7    Vest, Z.G.8    Madsen, J.R.9    Li, J.K.K.10    Barnard, D.L.11
  • 44
    • 79956314622 scopus 로고    scopus 로고
    • Immune signaling by RIG-I-like receptors
    • Loo, Y.M., Gale, M., Immune signaling by RIG-I-like receptors. Immunity 34 (2011), 680–692, 10.1016/j.immuni.2011.05.003.
    • (2011) Immunity , vol.34 , pp. 680-692
    • Loo, Y.M.1    Gale, M.2
  • 45
    • 84924981384 scopus 로고    scopus 로고
    • Intracellular detection of viral nucleic acids
    • Sparrer, K.M.J., Gack, M.U., Intracellular detection of viral nucleic acids. Curr. Opin. Microbiol. 26 (2015), 1–9, 10.1016/j.mib.2015.03.001.
    • (2015) Curr. Opin. Microbiol. , vol.26 , pp. 1-9
    • Sparrer, K.M.J.1    Gack, M.U.2
  • 47
    • 27144440476 scopus 로고    scopus 로고
    • Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus
    • Meylan, E., Curran, J., Hofmann, K., Moradpour, D., Binder, M., Bartenschlager, R., Tschopp, J., Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus. Nature 437 (2005), 1167–1172, 10.1038/nature04193.
    • (2005) Nature , vol.437 , pp. 1167-1172
    • Meylan, E.1    Curran, J.2    Hofmann, K.3    Moradpour, D.4    Binder, M.5    Bartenschlager, R.6    Tschopp, J.7
  • 48
    • 24144461689 scopus 로고    scopus 로고
    • Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-??B and IRF3
    • Seth, R.B., Sun, L., Ea, C.K., Chen, Z.J., Identification and characterization of MAVS, a mitochondrial antiviral signaling protein that activates NF-??B and IRF3. Cell 122 (2005), 669–682, 10.1016/j.cell.2005.08.012.
    • (2005) Cell , vol.122 , pp. 669-682
    • Seth, R.B.1    Sun, L.2    Ea, C.K.3    Chen, Z.J.4
  • 49
    • 24944538819 scopus 로고    scopus 로고
    • VISA is an adapter protein required for virus-triggered IFN-?.?. signaling
    • Xu, L.G., Wang, Y.Y., Han, K.J., Li, L.Y., Zhai, Z., Shu, H.B., VISA is an adapter protein required for virus-triggered IFN-?.?. signaling. Mol. Cell. 19 (2005), 727–740, 10.1016/j.molcel.2005.08.014.
    • (2005) Mol. Cell. , vol.19 , pp. 727-740
    • Xu, L.G.1    Wang, Y.Y.2    Han, K.J.3    Li, L.Y.4    Zhai, Z.5    Shu, H.B.6
  • 50
    • 79957597757 scopus 로고    scopus 로고
    • Mitochondria in innate immune responses
    • West, A.P., Shadel, G.S., Ghosh, S., Mitochondria in innate immune responses. Nat. Rev. Immunol. 11 (2011), 389–402, 10.1038/nri2975.
    • (2011) Nat. Rev. Immunol. , vol.11 , pp. 389-402
    • West, A.P.1    Shadel, G.S.2    Ghosh, S.3
  • 51
    • 84894585119 scopus 로고    scopus 로고
    • Toll-like receptors in antiviral innate immunity
    • Lester, S.N., Li, K., Toll-like receptors in antiviral innate immunity. J. Mol. Biol. 426 (2014), 1246–1264, 10.1016/j.jmb.2013.11.024.
    • (2014) J. Mol. Biol. , vol.426 , pp. 1246-1264
    • Lester, S.N.1    Li, K.2
  • 52
    • 84971597229 scopus 로고    scopus 로고
    • Immune evasion of porcine enteric coronaviruses and viral modulation of antiviral innate signaling
    • Zhang, Q., Yoo, D., Immune evasion of porcine enteric coronaviruses and viral modulation of antiviral innate signaling. Virus Res., 2016, 10.1016/j.virusres.2016.05.015.
    • (2016) Virus Res.
    • Zhang, Q.1    Yoo, D.2
  • 54
    • 82955187705 scopus 로고    scopus 로고
    • Interferon-stimulated genes and their antiviral effector functions
    • Schoggins, J.W., Rice, C.M., Interferon-stimulated genes and their antiviral effector functions. Curr. Opin. Virol. 1 (2011), 519–525, 10.1016/j.coviro.2011.10.008.
    • (2011) Curr. Opin. Virol. , vol.1 , pp. 519-525
    • Schoggins, J.W.1    Rice, C.M.2
  • 55
    • 46249115827 scopus 로고    scopus 로고
    • Interferon-inducible antiviral effectors
    • Sadler, A.J., Williams, B.R.G., Interferon-inducible antiviral effectors. Nat. Rev. Immunol. 8 (2008), 559–568, 10.1038/nri2314.
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 559-568
    • Sadler, A.J.1    Williams, B.R.G.2
  • 56
    • 78651506340 scopus 로고    scopus 로고
    • Interferon-stimulated genes and their protein products: what and how?
    • Borden, E.C., Williams, B.R., Interferon-stimulated genes and their protein products: what and how?. J. Interferon Cytokine Res. 31 (2011), 1–4, 10.1089/jir.2010.0129.
    • (2011) J. Interferon Cytokine Res. , vol.31 , pp. 1-4
    • Borden, E.C.1    Williams, B.R.2
  • 57
    • 66649109939 scopus 로고    scopus 로고
    • ERIS, an endoplasmic reticulum IFN stimulator, activates innate immune signaling through dimerization
    • (0900850106 [pii]\r10.1073/pnas.0900850106)
    • Sun, W., Li, Y., Chen, L., Chen, H., You, F., Zhou, X., Zhou, Y., Zhai, Z., Chen, D., Jiang, Z., ERIS, an endoplasmic reticulum IFN stimulator, activates innate immune signaling through dimerization. Proc. Natl. Acad. Sci. U. S. A. 106 (2009), 8653–8658 (0900850106 [pii]\r10.1073/pnas.0900850106).
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 8653-8658
    • Sun, W.1    Li, Y.2    Chen, L.3    Chen, H.4    You, F.5    Zhou, X.6    Zhou, Y.7    Zhai, Z.8    Chen, D.9    Jiang, Z.10
  • 58
    • 80052281413 scopus 로고    scopus 로고
    • Mitochondrial-associated endoplasmic reticulum membranes {(MAM)} form innate immune synapses and are targeted by hepatitis C virus
    • Horner, S.M., Liu, H.M., Park, H.S., Briley, J., Gale, M., Mitochondrial-associated endoplasmic reticulum membranes {(MAM)} form innate immune synapses and are targeted by hepatitis C virus. Proc. Natl. Acad. Sci. {U.S.A.}. 108 (2011), 14590–14595, 10.1073/pnas.1110133108.
    • (2011) Proc. Natl. Acad. Sci. {U.S.A.}. , vol.108 , pp. 14590-14595
    • Horner, S.M.1    Liu, H.M.2    Park, H.S.3    Briley, J.4    Gale, M.5
  • 61
    • 85013489264 scopus 로고    scopus 로고
    • Organelle dynamics: connections, connections, connections
    • Strzyz, P., Organelle dynamics: connections, connections, connections. Nat Rev. Mol. Cell Biol., 18, 2017, 139, 10.1038/nrm.2017.14.
    • (2017) Nat Rev. Mol. Cell Biol. , vol.18 , pp. 139
    • Strzyz, P.1
  • 63
    • 84922520038 scopus 로고    scopus 로고
    • Antiviral innate immunity and stress granule responses
    • Onomoto, K., Yoneyama, M., Fung, G., Kato, H., Fujita, T., Antiviral innate immunity and stress granule responses. Trends Immunol. 35 (2014), 420–428, 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
  • 66
    • 84883271505 scopus 로고    scopus 로고
    • Encephalomyocarditis virus disrupts stress granules, the critical platform for triggering antiviral innate immune responses
    • Ng, C.S., Jogi, M., Yoo, J.-S., Onomoto, K., Koike, S., Iwasaki, T., Yoneyama, M., Kato, H., Fujita, T., Encephalomyocarditis virus disrupts stress granules, the critical platform for triggering antiviral innate immune responses. J. Virol. 87 (2013), 9511–9522, 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
  • 67
    • 84878171308 scopus 로고    scopus 로고
    • MDA5 localizes to stress granules, but this localization is not required for the induction of type I interferon
    • Langereis, M.A., Feng, Q., van Kuppeveld, F.J., MDA5 localizes to stress granules, but this localization is not required for the induction of type I interferon. J. Virol. 87 (2013), 6314–6325, 10.1128/JVI.03213-12.
    • (2013) J. Virol. , vol.87 , pp. 6314-6325
    • Langereis, M.A.1    Feng, Q.2    van Kuppeveld, F.J.3
  • 68
    • 0037444183 scopus 로고    scopus 로고
    • Characterization of RNA synthesis, replication mechanism, and in vitro RNA-dependent RNA polymerase activity of Japanese encephalitis virus
    • (S0042682202001307 [pii])
    • Uchil, P.D., Satchidanandam, V., Characterization of RNA synthesis, replication mechanism, and in vitro RNA-dependent RNA polymerase activity of Japanese encephalitis virus. Virology 307 (2003), 358–371 (S0042682202001307 [pii]).
    • (2003) Virology , vol.307 , pp. 358-371
    • Uchil, P.D.1    Satchidanandam, V.2
  • 69
    • 0042591335 scopus 로고    scopus 로고
    • Architecture of the flaviviral replication complex: protease, nuclease, and detergents reveal encasement within double-layered membrane compartments
    • Uchil, P.D., Satchidanandam, V., Architecture of the flaviviral replication complex: protease, nuclease, and detergents reveal encasement within double-layered membrane compartments. J. Biol. Chem. 278 (2003), 24388–24398, 10.1074/jbc.M301717200.
    • (2003) J. Biol. Chem. , vol.278 , pp. 24388-24398
    • Uchil, P.D.1    Satchidanandam, V.2
  • 70
    • 44449098281 scopus 로고    scopus 로고
    • SARS-coronavirus replication/transcription complexes are membrane-protected and need a host factor for activity in vitro
    • Van Hemert, M.J., Van Den Worm, S.H.E., Knoops, K., Mommaas, A.M., Gorbalenya, A.E., Snijder, E.J., SARS-coronavirus replication/transcription complexes are membrane-protected and need a host factor for activity in vitro. PLoS Pathog., 4, 2008, 10.1371/journal.ppat.1000054.
    • (2008) PLoS Pathog. , vol.4
    • Van Hemert, M.J.1    Van Den Worm, S.H.E.2    Knoops, K.3    Mommaas, A.M.4    Gorbalenya, A.E.5    Snijder, E.J.6
  • 71
    • 47749135896 scopus 로고    scopus 로고
    • The in vitro RNA synthesizing activity of the isolated arterivirus replication/transcription complex is dependent on a host factor
    • Van Hemert, M.J., De Wilde, A.H., Gorbalenya, A.E., Snijder, E.J., The in vitro RNA synthesizing activity of the isolated arterivirus replication/transcription complex is dependent on a host factor. J. Biol. Chem. 283 (2008), 16525–16536, 10.1074/jbc.M708136200.
    • (2008) J. Biol. Chem. , vol.283 , pp. 16525-16536
    • Van Hemert, M.J.1    De Wilde, A.H.2    Gorbalenya, A.E.3    Snijder, E.J.4
  • 77
    • 29144462494 scopus 로고    scopus 로고
    • Hepatitis C virus protease NS3/4A cleaves mitochondrial antiviral signaling protein off the mitochondria to evade innate immunity
    • Li, X.-D., Sun, L., Seth, R.B., Pineda, G., Chen, Z.J., Hepatitis C virus protease NS3/4A cleaves mitochondrial antiviral signaling protein off the mitochondria to evade innate immunity. Proc. Natl. Acad. Sci. U. S. A. 102 (2005), 17717–17722, 10.1073/pnas.0508531102.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 17717-17722
    • Li, X.-D.1    Sun, L.2    Seth, R.B.3    Pineda, G.4    Chen, Z.J.5
  • 78
    • 0037687422 scopus 로고    scopus 로고
    • Regulation of interferon regulatory factor-3 by the hepatitis C virus serine protease
    • Foy, E., Li, K., Wang, C., Sumpter, R., Ikeda, M., Lemon, S.M., Gale, M., Regulation of interferon regulatory factor-3 by the hepatitis C virus serine protease. Science 300 (2003), 1145–1148, 10.1126/science.1082604.
    • (2003) Science , vol.300 , pp. 1145-1148
    • Foy, E.1    Li, K.2    Wang, C.3    Sumpter, R.4    Ikeda, M.5    Lemon, S.M.6    Gale, M.7
  • 81
    • 34247848008 scopus 로고    scopus 로고
    • The non-structural protein 4A of dengue virus is an integral membrane protein inducing membrane alterations in a 2K-regulated manner
    • Miller, S., Kastner, S., Krijnse-Locker, J., Bühler, S., Bartenschlager, R., The non-structural protein 4A of dengue virus is an integral membrane protein inducing membrane alterations in a 2K-regulated manner. J. Biol. Chem. 282 (2007), 8873–8882, 10.1074/jbc.M609919200.
    • (2007) J. Biol. Chem. , vol.282 , pp. 8873-8882
    • Miller, S.1    Kastner, S.2    Krijnse-Locker, J.3    Bühler, S.4    Bartenschlager, R.5
  • 83
    • 77956859036 scopus 로고    scopus 로고
    • Inhibition of the type I interferon response in human dendritic cells by dengue virus infection requires a catalytically active NS2B3 complex
    • Rodriguez-Madoz, J.R., Belicha-Villanueva, A., Bernal-Rubio, D., Ashour, J., Ayllon, J., Fernandez-Sesma, A., Inhibition of the type I interferon response in human dendritic cells by dengue virus infection requires a catalytically active NS2B3 complex. J. Virol. 84 (2010), 9760–9774, 10.1128/JVI.01051-10.
    • (2010) J. Virol. , vol.84 , pp. 9760-9774
    • Rodriguez-Madoz, J.R.1    Belicha-Villanueva, A.2    Bernal-Rubio, D.3    Ashour, J.4    Ayllon, J.5    Fernandez-Sesma, A.6
  • 84
    • 84864036246 scopus 로고    scopus 로고
    • Dengue virus targets the adaptor protein MITA to subvert host innate immunity
    • Yu, C.Y., Chang, T.H., Liang, J.J., Chiang, R.L., Lee, Y.L., Liao, C.L., Lin, Y.L., Dengue virus targets the adaptor protein MITA to subvert host innate immunity. PLoS Pathog., 8, 2012, 10.1371/journal.ppat.1002780.
    • (2012) PLoS Pathog. , vol.8
    • Yu, C.Y.1    Chang, T.H.2    Liang, J.J.3    Chiang, R.L.4    Lee, Y.L.5    Liao, C.L.6    Lin, Y.L.7
  • 86
    • 84879173207 scopus 로고    scopus 로고
    • Hepatitis C virus NS4 B blocks the interaction of STING and TBK1 to evade host innate immunity
    • Ding, Q., Cao, X., Lu, J., Huang, B., Liu, Y.J., Kato, N., Shu, H.B., Zhong, J., Hepatitis C virus NS4 B blocks the interaction of STING and TBK1 to evade host innate immunity. J. Hepatol. 59 (2013), 52–58, 10.1016/j.jhep.2013.03.019.
    • (2013) J. Hepatol. , vol.59 , pp. 52-58
    • Ding, Q.1    Cao, X.2    Lu, J.3    Huang, B.4    Liu, Y.J.5    Kato, N.6    Shu, H.B.7    Zhong, J.8
  • 88
    • 84920671962 scopus 로고    scopus 로고
    • Nidovirus papain-like proteases: multifunctional enzymes with protease, deubiquitinating and deISGylating activities
    • Mielech, A.M., Chen, Y., Mesecar, A.D., Baker, S.C., Nidovirus papain-like proteases: multifunctional enzymes with protease, deubiquitinating and deISGylating activities. Virus Res. 194 (2014), 184–190, 10.1016/j.virusres.2014.01.025.
    • (2014) Virus Res. , vol.194 , pp. 184-190
    • Mielech, A.M.1    Chen, Y.2    Mesecar, A.D.3    Baker, S.C.4
  • 90
    • 84918528852 scopus 로고    scopus 로고
    • Crystal structure of the middle east respiratory syndrome coronavirus (MERS-CoV) papain-like protease bound to ubiquitin facilitates targeted disruption of deubiquitinating activity to demonstrate its role in innate immune suppression
    • Bailey-Elkin, B.A., Knaap, R.C.M., Johnson, G.G., Dalebout, T.J., Ninaber, D.K., Van Kasteren, P.B., Bredenbeek, P.J., Snijder, E.J., Kikkert, M., Mark, B.L., Crystal structure of the middle east respiratory syndrome coronavirus (MERS-CoV) papain-like protease bound to ubiquitin facilitates targeted disruption of deubiquitinating activity to demonstrate its role in innate immune suppression. J. Biol. Chem. 289 (2014), 34667–34682, 10.1074/jbc.M114.609644.
    • (2014) J. Biol. Chem. , vol.289 , pp. 34667-34682
    • Bailey-Elkin, B.A.1    Knaap, R.C.M.2    Johnson, G.G.3    Dalebout, T.J.4    Ninaber, D.K.5    Van Kasteren, P.B.6    Bredenbeek, P.J.7    Snijder, E.J.8    Kikkert, M.9    Mark, B.L.10
  • 91
    • 84892164414 scopus 로고    scopus 로고
    • Dengue virus subverts the interferon induction pathway via NS2B/3 protease-I(B kinase (interaction
    • Angleró-Rodríguez, Y.I., Pantoja, P., Sariol, C.A., Dengue virus subverts the interferon induction pathway via NS2B/3 protease-I(B kinase (interaction. Clin. Vaccine Immunol. 21 (2014), 29–38, 10.1128/CVI.00500-13.
    • (2014) Clin. Vaccine Immunol. , vol.21 , pp. 29-38
    • Angleró-Rodríguez, Y.I.1    Pantoja, P.2    Sariol, C.A.3
  • 92
  • 93
    • 33846104528 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome coronavirus open reading frame (ORF) 3b, ORF 6, and nucleocapsid proteins function as interferon antagonists
    • Kopecky-Bromberg, S.a., Martínez-Sobrido, L., Frieman, M., Baric, R.a., Palese, P., Severe acute respiratory syndrome coronavirus open reading frame (ORF) 3b, ORF 6, and nucleocapsid proteins function as interferon antagonists. J. Virol. 81 (2007), 548–557, 10.1128/JVI.01782-06.
    • (2007) J. Virol. , vol.81 , pp. 548-557
    • Kopecky-Bromberg, S.A.1    Martínez-Sobrido, L.2    Frieman, M.3    Baric, R.A.4    Palese, P.5
  • 94
    • 84890049888 scopus 로고    scopus 로고
    • The structural and accessory proteins M, ORF 4a, ORF 4b, and ORF 5 of Middle East respiratory syndrome coronavirus (MERS-CoV) are potent interferon antagonists
    • Yang, Y., Zhang, L., Geng, H., Deng, Y., Huang, B., Guo, Y., Zhao, Z., Tan, W., The structural and accessory proteins M, ORF 4a, ORF 4b, and ORF 5 of Middle East respiratory syndrome coronavirus (MERS-CoV) are potent interferon antagonists. Protein Cell. 4 (2013), 951–961, 10.1007/s13238-013-3096-8.
    • (2013) Protein Cell. , vol.4 , pp. 951-961
    • Yang, Y.1    Zhang, L.2    Geng, H.3    Deng, Y.4    Huang, B.5    Guo, Y.6    Zhao, Z.7    Tan, W.8
  • 95
    • 77957555067 scopus 로고    scopus 로고
    • Transcriptional upregulation of SOCS 1 and suppressors of cytokine signaling 3 mRNA in the absence of suppressors of cytokine signaling 2 mRNA after infection with West Nile virus or tick-borne encephalitis virus
    • Mansfield, K.L., Johnson, N., Cosby, S.L., Solomon, T., Fooks, A.R., Transcriptional upregulation of SOCS 1 and suppressors of cytokine signaling 3 mRNA in the absence of suppressors of cytokine signaling 2 mRNA after infection with West Nile virus or tick-borne encephalitis virus. Vector Borne Zoonotic Dis. 10 (2010), 649–653, 10.1089/vbz.2009.0259.
    • (2010) Vector Borne Zoonotic Dis. , vol.10 , pp. 649-653
    • Mansfield, K.L.1    Johnson, N.2    Cosby, S.L.3    Solomon, T.4    Fooks, A.R.5
  • 96
    • 84859435371 scopus 로고    scopus 로고
    • Expression profile of immune response genes during acute myopathy induced by chikungunya virus in a mouse model
    • Patil, D.R., Hundekar, S.L., Arankalle, V.A., Expression profile of immune response genes during acute myopathy induced by chikungunya virus in a mouse model. Microbes Infect. 14 (2012), 457–469, 10.1016/j.micinf.2011.12.008.
    • (2012) Microbes Infect. , vol.14 , pp. 457-469
    • Patil, D.R.1    Hundekar, S.L.2    Arankalle, V.A.3
  • 97
    • 84886732794 scopus 로고    scopus 로고
    • Japanese encephalitis virus infection modulates the expression of suppressors of cytokine signaling (SOCS) in macrophages: implications for the hosts’ innate immune response
    • Kundu, K., Dutta, K., Nazmi, A., Basu, A., Japanese encephalitis virus infection modulates the expression of suppressors of cytokine signaling (SOCS) in macrophages: implications for the hosts’ innate immune response. Cell. Immunol. 285 (2013), 100–110, 10.1016/j.cellimm.2013.09.005.
    • (2013) Cell. Immunol. , vol.285 , pp. 100-110
    • Kundu, K.1    Dutta, K.2    Nazmi, A.3    Basu, A.4
  • 98
    • 13744259524 scopus 로고    scopus 로고
    • West Nile virus inhibits the signal transduction pathway of alpha interferon
    • Guo, J.-T., Hayashi, J., Seeger, C., West Nile virus inhibits the signal transduction pathway of alpha interferon. J. Virol. 79 (2005), 1343–1350, 10.1128/JVI.79.3.1343-1350.2005.
    • (2005) J. Virol. , vol.79 , pp. 1343-1350
    • Guo, J.-T.1    Hayashi, J.2    Seeger, C.3
  • 99
    • 33744943788 scopus 로고    scopus 로고
    • Blocking of interferon-induced Jak-Stat signaling by Japanese encephalitis virus NS5 through a protein tyrosine phosphatase-mediated mechanism
    • Lin, R.J., Chang, B.L., Yu, H.P., Liao, C.L., Lin, Y.L., Blocking of interferon-induced Jak-Stat signaling by Japanese encephalitis virus NS5 through a protein tyrosine phosphatase-mediated mechanism. J. Virol. 80 (2006), 5908–5918, 10.1128/JVI.02714-05.
    • (2006) J. Virol. , vol.80 , pp. 5908-5918
    • Lin, R.J.1    Chang, B.L.2    Yu, H.P.3    Liao, C.L.4    Lin, Y.L.5
  • 100
    • 35448939321 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome coronavirus evades antiviral signaling: role of nsp1 and rational design of an attenuated strain
    • Wathelet, M.G., Orr, M., Frieman, M.B., Baric, R.S., Severe acute respiratory syndrome coronavirus evades antiviral signaling: role of nsp1 and rational design of an attenuated strain. J. Virol. 81 (2007), 11620–11633, 10.1128/JVI.00702-07.
    • (2007) J. Virol. , vol.81 , pp. 11620-11633
    • Wathelet, M.G.1    Orr, M.2    Frieman, M.B.3    Baric, R.S.4
  • 101
    • 35348845802 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome coronavirus ORF6 antagonizes STAT1 function by sequestering nuclear import factors on the rough endoplasmic reticulum/Golgi membrane
    • Frieman, M., Yount, B., Heise, M., Kopecky-Bromberg, S.A., Palese, P., Baric, R.S., Severe acute respiratory syndrome coronavirus ORF6 antagonizes STAT1 function by sequestering nuclear import factors on the rough endoplasmic reticulum/Golgi membrane. J. Virol. 81 (2007), 9812–9824, 10.1128/JVI.01012-07.
    • (2007) J. Virol. , vol.81 , pp. 9812-9824
    • Frieman, M.1    Yount, B.2    Heise, M.3    Kopecky-Bromberg, S.A.4    Palese, P.5    Baric, R.S.6
  • 102
    • 79955624337 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome coronavirus papain-like protease suppressed alpha interferon-induced responses through downregulation of extracellular signal-regulated kinase 1-mediated signalling pathways
    • Li, S.W., Lai, C.C., Ping, J.F., Tsai, F.J., Wan, L., Lin, Y.J., Kung, S.H., Lin, C.W., Severe acute respiratory syndrome coronavirus papain-like protease suppressed alpha interferon-induced responses through downregulation of extracellular signal-regulated kinase 1-mediated signalling pathways. J. Gen. Virol. 92 (2011), 1127–1140, 10.1099/vir.0.028936-0.
    • (2011) J. Gen. Virol. , vol.92 , pp. 1127-1140
    • Li, S.W.1    Lai, C.C.2    Ping, J.F.3    Tsai, F.J.4    Wan, L.5    Lin, Y.J.6    Kung, S.H.7    Lin, C.W.8
  • 103
    • 35848929915 scopus 로고    scopus 로고
    • Inhibition of cytoplasmic mRNA stress granule formation by a viral proteinase
    • White, J.P., Cardenas, A.M., Marissen, W.E., Lloyd, R.E., Inhibition of cytoplasmic mRNA stress granule formation by a viral proteinase. Cell Host Microbe. 2 (2007), 295–305, 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
  • 104
    • 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, M.H., Boyd, B., Wieland, S., Chisari, F.V., Hepatitis C virus (HCV) induces formation of stress granules whose proteins regulate HCV RNA replication and virus assembly and egress. J. Virol. 86 (2012), 11043–11056, 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
  • 105
    • 84871954468 scopus 로고    scopus 로고
    • Japanese encephalitis virus core protein inhibits stress granule formation through an interaction with Caprin-1 and facilitates viral propagation
    • Katoh, H., Okamoto, T., Fukuhara, T., Kambara, H., Morita, E., Mori, Y., Kamitani, W., Matsuura, Y., Japanese encephalitis virus core protein inhibits stress granule formation through an interaction with Caprin-1 and facilitates viral propagation. J. Virol. 87 (2013), 489–502, 10.1128/JVI.02186-12.
    • (2013) J. Virol. , vol.87 , pp. 489-502
    • Katoh, H.1    Okamoto, T.2    Fukuhara, T.3    Kambara, H.4    Morita, E.5    Mori, Y.6    Kamitani, W.7    Matsuura, Y.8
  • 106
    • 34547456097 scopus 로고    scopus 로고
    • Interaction of TIA-1/TIAR with West Nile and dengue virus products in infected cells interferes with stress granule formation and processing body assembly
    • Emara, M.M., Brinton, M.A., Interaction of TIA-1/TIAR with West Nile and dengue virus products in infected cells interferes with stress granule formation and processing body assembly. Proc. Natl. Acad. Sci. U. S. A. 104 (2007), 9041–9046, 10.1073/pnas.0703348104.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 9041-9046
    • Emara, M.M.1    Brinton, M.A.2
  • 108
    • 84925386816 scopus 로고    scopus 로고
    • Stress granule components G3BP1 and G3BP2 play a proviral role early in Chikungunya virus replication
    • Scholte, F.E.M., Tas, A., Albulescu, I.C., Žusinaite, E., Merits, A., Snijder, E.J., van Hemert, M.J., Stress granule components G3BP1 and G3BP2 play a proviral role early in Chikungunya virus replication. J. Virol. 89 (2015), 4457–4469, 10.1128/JVI.03612-14.
    • (2015) J. Virol. , vol.89 , pp. 4457-4469
    • Scholte, F.E.M.1    Tas, A.2    Albulescu, I.C.3    Žusinaite, E.4    Merits, A.5    Snijder, E.J.6    van Hemert, M.J.7
  • 111
    • 84959562427 scopus 로고    scopus 로고
    • The hepatitis C virus-induced membranous web and associated nuclear transport machinery limit access of pattern recognition receptors to viral replication sites
    • Neufeldt, C.J., Joyce, M.A., Van Buuren, N., Levin, A., Kirkegaard, K., Gale, M., Tyrrell, D.L.J., Wozniak, R.W., The hepatitis C virus-induced membranous web and associated nuclear transport machinery limit access of pattern recognition receptors to viral replication sites. PLoS Pathog., 12, 2016, 10.1371/journal.ppat.1005428.
    • (2016) PLoS Pathog. , vol.12
    • Neufeldt, C.J.1    Joyce, M.A.2    Van Buuren, N.3    Levin, A.4    Kirkegaard, K.5    Gale, M.6    Tyrrell, D.L.J.7    Wozniak, R.W.8
  • 113
    • 80055046485 scopus 로고    scopus 로고
    • The antiviral protein viperin inhibits hepatitis C virus replication via interaction with nonstructural protein 5A
    • Helbig, K.J., Eyre, N.S., Yip, E., Narayana, S., Li, K., Fiches, G., Mccartney, E.M., Jangra, R.K., Lemon, S.M., Beard, M.R., The antiviral protein viperin inhibits hepatitis C virus replication via interaction with nonstructural protein 5A. Hepatology 54 (2011), 1506–1517, 10.1002/hep.24542.
    • (2011) Hepatology , vol.54 , pp. 1506-1517
    • Helbig, K.J.1    Eyre, N.S.2    Yip, E.3    Narayana, S.4    Li, K.5    Fiches, G.6    Mccartney, E.M.7    Jangra, R.K.8    Lemon, S.M.9    Beard, M.R.10
  • 114
    • 85007521321 scopus 로고    scopus 로고
    • Antiviral innate immune response interferes with the formation of replication-associated membrane structures induced by a +RNA virus
    • Oudshoorn, D., Van der Hoeven, B., Limpens, R.W.A.L., Beugeling, C., Snijder, E.J., Bárcena, M., Kikkert, M., Antiviral innate immune response interferes with the formation of replication-associated membrane structures induced by a +RNA virus. MBio 7 (2016), 1–11, 10.1128/mBio.01991-16.
    • (2016) MBio , vol.7 , pp. 1-11
    • Oudshoorn, D.1    Van der Hoeven, B.2    Limpens, R.W.A.L.3    Beugeling, C.4    Snijder, E.J.5    Bárcena, M.6    Kikkert, M.7
  • 115
    • 84884688909 scopus 로고    scopus 로고
    • Self and non-self discrimination of intracellular membranes by the innate immune system
    • Coers, J., Self and non-self discrimination of intracellular membranes by the innate immune system. PLoS Pathog. 9 (2013), 10–13, 10.1371/journal.ppat.1003538.
    • (2013) PLoS Pathog. , vol.9 , pp. 10-13
    • Coers, J.1
  • 116
    • 84969579633 scopus 로고    scopus 로고
    • Interferon-inducible GTPases in host resistance, inflammation and disease
    • Pilla-Moffett, D., Barber, M.F., Taylor, G.A., Coers, J., Interferon-inducible GTPases in host resistance, inflammation and disease. J. Mol. Biol. 428 (2016), 3495–3513, 10.1016/j.jmb.2016.04.032.
    • (2016) J. Mol. Biol. , vol.428 , pp. 3495-3513
    • Pilla-Moffett, D.1    Barber, M.F.2    Taylor, G.A.3    Coers, J.4
  • 118
    • 84879547102 scopus 로고    scopus 로고
    • IRG and GBP host resistance factors target aberrant, non-self vacuoles characterized by the missing of self IRGM proteins
    • Haldar, A.K., Saka, H.A., Piro, A.S., Da Dunn, J., Henry, S.C., Taylor, G.A., Frickel, E.M., Valdivia, R.H., Coers, J., IRG and GBP host resistance factors target aberrant, non-self vacuoles characterized by the missing of self IRGM proteins. PLoS Pathog., 9, 2013, 10.1371/journal.ppat.1003414.
    • (2013) PLoS Pathog. , vol.9
    • Haldar, A.K.1    Saka, H.A.2    Piro, A.S.3    Da Dunn, J.4    Henry, S.C.5    Taylor, G.A.6    Frickel, E.M.7    Valdivia, R.H.8    Coers, J.9
  • 120
    • 84908330381 scopus 로고    scopus 로고
    • Identification of the microsporidian encephalitozoon cuniculi as a new target of the IFN-γ inducible IRG resistance system
    • da Fonseca Ferreira-da-Silva, M., Springer-Frauenhoff, H.M., Bohne, W., Howard, J.C., Identification of the microsporidian encephalitozoon cuniculi as a new target of the IFN-γ inducible IRG resistance system. PLoS Pathog., 10, 2014, 10.1371/journal.ppat.1004449.
    • (2014) PLoS Pathog. , vol.10
    • da Fonseca Ferreira-da-Silva, M.1    Springer-Frauenhoff, H.M.2    Bohne, W.3    Howard, J.C.4
  • 121
    • 80051792857 scopus 로고    scopus 로고
    • The IRG protein-based resistance mechanism in mice and its relation to virulence in Toxoplasma gondii
    • Howard, J.C., Hunn, J.P., Steinfeldt, T., The IRG protein-based resistance mechanism in mice and its relation to virulence in Toxoplasma gondii. Curr. Opin. Microbiol. 14 (2011), 414–421, 10.1016/j.mib.2011.07.002.
    • (2011) Curr. Opin. Microbiol. , vol.14 , pp. 414-421
    • Howard, J.C.1    Hunn, J.P.2    Steinfeldt, T.3
  • 124
    • 84981502098 scopus 로고    scopus 로고
    • Quo vadis?. Interferon-inducible GTPases go to their target membranes via the LC3-conjugation system of autophagy
    • Choi, J., Biering, S.B., Hwang, S., Quo vadis?. Interferon-inducible GTPases go to their target membranes via the LC3-conjugation system of autophagy. Small GTPases 0 (2016), 1–9, 10.1080/21541248.2016.1213090.
    • (2016) Small GTPases , pp. 1-9
    • Choi, J.1    Biering, S.B.2    Hwang, S.3
  • 125
    • 84979036004 scopus 로고    scopus 로고
    • Targeting by AutophaGy proteins (TAG): Targeting of IFNG-inducible GTPases to membranes by the LC3 conjugation system of autophagy
    • Park, S., Choi, J., Biering, S.B., Dominici, E., Williams, L.E., Hwang, S., Targeting by AutophaGy proteins (TAG): Targeting of IFNG-inducible GTPases to membranes by the LC3 conjugation system of autophagy. Autophagy 12 (2016), 1153–1167, 10.1080/15548627.2016.1178447.
    • (2016) Autophagy , vol.12 , pp. 1153-1167
    • Park, S.1    Choi, J.2    Biering, S.B.3    Dominici, E.4    Williams, L.E.5    Hwang, S.6
  • 126
    • 34548077575 scopus 로고    scopus 로고
    • Dissection of the autophagosome maturation process by a novel reporter protein, tandem fluorescent-tagged LC3
    • (4451 [pii])
    • Kimura, S., Noda, T., Yoshimori, T., Dissection of the autophagosome maturation process by a novel reporter protein, tandem fluorescent-tagged LC3. Autophagy 3 (2007), 452–460 (4451 [pii]).
    • (2007) Autophagy , vol.3 , pp. 452-460
    • Kimura, S.1    Noda, T.2    Yoshimori, T.3
  • 127
    • 84896992565 scopus 로고    scopus 로고
    • Selective autophagy against membranous compartments: canonical and unconventional purposes and mechanisms
    • Pimentel-Muiños, F.X., Boada-Romero, E., Selective autophagy against membranous compartments: canonical and unconventional purposes and mechanisms. Autophagy 10 (2014), 397–407, 10.4161/auto.27244.
    • (2014) Autophagy , vol.10 , pp. 397-407
    • Pimentel-Muiños, F.X.1    Boada-Romero, E.2
  • 128
    • 84883655855 scopus 로고    scopus 로고
    • Hidden behind autophagy: the unconventional roles of ATG proteins
    • Bestebroer, J., V'kovski, P., Mauthe, M., Reggiori, F., Hidden behind autophagy: the unconventional roles of ATG proteins. Traffic 14 (2013), 1029–1041, 10.1111/tra.12091.
    • (2013) Traffic , vol.14 , pp. 1029-1041
    • Bestebroer, J.1    V'kovski, P.2    Mauthe, M.3    Reggiori, F.4
  • 129
    • 23144449208 scopus 로고    scopus 로고
    • Ubiquitin and ubiquitin-like proteins as multifunctional signals
    • Welchman, R.L., Gordon, C., Mayer, R.J., Ubiquitin and ubiquitin-like proteins as multifunctional signals. Nat. Rev. Mol. Cell Biol. 6 (2005), 599–609, 10.1038/nrm1700.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 599-609
    • Welchman, R.L.1    Gordon, C.2    Mayer, R.J.3
  • 131
    • 65449163019 scopus 로고    scopus 로고
    • Virulent toxoplasma gondii evade immunity-related GTPase (IRG)-Mediated parasite vacuole disruption within primed macrophages
    • Zhao, Y., Ferguson, D.J.P., Wilson, D., Howard, J.C., Sibley, L.D., Yap, G.S., Virulent toxoplasma gondii evade immunity-related GTPase (IRG)-Mediated parasite vacuole disruption within primed macrophages. J. Immunol. 182 (2010), 3775–3781, 10.4049/jimmunol.0804190.Virulent.
    • (2010) J. Immunol. , vol.182 , pp. 3775-3781
    • Zhao, Y.1    Ferguson, D.J.P.2    Wilson, D.3    Howard, J.C.4    Sibley, L.D.5    Yap, G.S.6
  • 136
    • 43949143804 scopus 로고    scopus 로고
    • The Atg16L complex specifies the site of LC3 lipidation for membrane biogenesis in autophagy
    • Fujita, N., Itoh, T., Omori, H., Fukuda, M., Noda, T., Yoshimori, T., The Atg16L complex specifies the site of LC3 lipidation for membrane biogenesis in autophagy. Mol. Biol. Cell 19 (2008), 2092–2100, 10.1091/mbc.E07-12-1257\rE07-12-1257[pii].
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2092-2100
    • Fujita, N.1    Itoh, T.2    Omori, H.3    Fukuda, M.4    Noda, T.5    Yoshimori, T.6
  • 137
    • 3242888703 scopus 로고    scopus 로고
    • LC3, GABARAP and GATE16 localize to autophagosomal membrane depending on form-II formation
    • (pii)
    • Kabeya, Y., Mizushima, N., Yamamoto, A., Oshitani-Okamoto, S., Ohsumi, Y., Yoshimori, T., LC3, GABARAP and GATE16 localize to autophagosomal membrane depending on form-II formation. J. Cell Sci. 117 (2004), 2805–2812, 10.1242/jcs.01131\r117/13/2805 (pii).
    • (2004) J. Cell Sci. , vol.117 , pp. 2805-2812
    • Kabeya, Y.1    Mizushima, N.2    Yamamoto, A.3    Oshitani-Okamoto, S.4    Ohsumi, Y.5    Yoshimori, T.6
  • 138
    • 9144224360 scopus 로고    scopus 로고
    • Human light chain 3/MAP1LC3 B Is cleaved at its carboxyl-terminal Met 121 to expose Gly120 for lipidation and targeting to autophagosomal membranes
    • Tanida, I., Ueno, T., Kominami, E., Human light chain 3/MAP1LC3 B Is cleaved at its carboxyl-terminal Met 121 to expose Gly120 for lipidation and targeting to autophagosomal membranes. J. Biol. Chem. 279 (2004), 47704–47710, 10.1074/jbc.M407016200.
    • (2004) J. Biol. Chem. , vol.279 , pp. 47704-47710
    • Tanida, I.1    Ueno, T.2    Kominami, E.3
  • 139
    • 4344604111 scopus 로고    scopus 로고
    • HsAtg4B/HsApg4B/autophagin-1 cleaves the carboxyl termini of three human Atg8 homologues and delipidates microtubule-associated protein light chain 3- and GABAA receptor-associated protein-phospholipid conjugates
    • Tanida, I., Sou, Y.S., Ezaki, J., Minematsu-Ikeguchi, N., Ueno, T., Kominami, E., HsAtg4B/HsApg4B/autophagin-1 cleaves the carboxyl termini of three human Atg8 homologues and delipidates microtubule-associated protein light chain 3- and GABAA receptor-associated protein-phospholipid conjugates. J. Biol. Chem. 279 (2004), 36268–36276, 10.1074/jbc.M401461200.
    • (2004) J. Biol. Chem. , vol.279 , pp. 36268-36276
    • Tanida, I.1    Sou, Y.S.2    Ezaki, J.3    Minematsu-Ikeguchi, N.4    Ueno, T.5    Kominami, E.6
  • 142
    • 84953211349 scopus 로고    scopus 로고
    • Evolutionary analyses suggest a function of MxB immunity proteins beyond lentivirus restriction
    • Mitchell, P.S., Young, J.M., Emerman, M., Malik, H.S., Evolutionary analyses suggest a function of MxB immunity proteins beyond lentivirus restriction. PLoS Pathog., 11, 2015, 10.1371/journal.ppat.1005304.
    • (2015) PLoS Pathog. , vol.11
    • Mitchell, P.S.1    Young, J.M.2    Emerman, M.3    Malik, H.S.4
  • 146
    • 33646826348 scopus 로고    scopus 로고
    • Parallels among positive-strand RNA viruses, reverse-transcribing viruses and double-stranded RNA viruses
    • Ahlquist, P., Parallels among positive-strand RNA viruses, reverse-transcribing viruses and double-stranded RNA viruses. Nat. Rev. Microbiol. 4 (2006), 371–382, 10.1038/nrmicro1389.
    • (2006) Nat. Rev. Microbiol. , vol.4 , pp. 371-382
    • Ahlquist, P.1


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