메뉴 건너뛰기




Volumn 59, Issue SUPPL.2, 2012, Pages 116-131

How Ebola Virus Counters the Interferon System

Author keywords

Ebola virus; IFITM; Interferon system; Tetherin; VP24; VP35

Indexed keywords

ALPHA INTERFERON RECEPTOR; GAMMA INTERFERON RECEPTOR; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERFERON; INTERLEUKIN 1 RECEPTOR ASSOCIATED KINASE; JANUS KINASE 1; SMALL INTERFERING RNA; STAT1 PROTEIN; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 6; UNCLASSIFIED DRUG; VIRUS PROTEIN; VP24 PROTEIN; VP35 PROTEIN;

EID: 84866033647     PISSN: 18631959     EISSN: 18632378     Source Type: Journal    
DOI: 10.1111/j.1863-2378.2012.01454.x     Document Type: Article
Times cited : (30)

References (111)
  • 4
    • 77954754505 scopus 로고    scopus 로고
    • Induction of type I interferon by RNA viruses: cellular receptors and their substrates
    • Baum, A., and A. García-Sastre, 2010: Induction of type I interferon by RNA viruses: cellular receptors and their substrates. Amino Acids 38, 1283-1299.
    • (2010) Amino Acids , vol.38 , pp. 1283-1299
    • Baum, A.1    García-Sastre, A.2
  • 5
    • 79952910124 scopus 로고    scopus 로고
    • Differential recognition of viral RNA by RIG-I
    • Baum, A., and A. García-Sastre, 2011: Differential recognition of viral RNA by RIG-I. Virulence 2, 166-169.
    • (2011) Virulence , vol.2 , pp. 166-169
    • Baum, A.1    García-Sastre, A.2
  • 7
    • 78650575533 scopus 로고    scopus 로고
    • Viral RNA silencing suppressors (RSS): novel strategy of viruses to ablate the host RNA interference (RNAi) defense system
    • Bivalkar-Mehla, S., J. Vakharia, R. Mehla, M. Abreha, J. R. Kanwar, A. Tikoo, and A. Chauhan, 2011: Viral RNA silencing suppressors (RSS): novel strategy of viruses to ablate the host RNA interference (RNAi) defense system. Virus Res. 155, 1-9.
    • (2011) Virus Res. , vol.155 , pp. 1-9
    • Bivalkar-Mehla, S.1    Vakharia, J.2    Mehla, R.3    Abreha, M.4    Kanwar, J.R.5    Tikoo, A.6    Chauhan, A.7
  • 9
    • 0034993883 scopus 로고    scopus 로고
    • The role of the Type I interferon response in the resistance of mice to filovirus infection
    • Bray, M., 2001: The role of the Type I interferon response in the resistance of mice to filovirus infection. J. Gen. Virol. 82, 1365-1373.
    • (2001) J. Gen. Virol. , vol.82 , pp. 1365-1373
    • Bray, M.1
  • 10
    • 0031688699 scopus 로고    scopus 로고
    • A mouse model for evaluation of prophylaxis and therapy of Ebola hemorrhagic fever
    • Bray, M., K. Davis, T. Geisbert, C. Schmaljohn, and J. Huggins, 1998: A mouse model for evaluation of prophylaxis and therapy of Ebola hemorrhagic fever. J. Infect. Dis. 178, 651-661.
    • (1998) J. Infect. Dis. , vol.178 , pp. 651-661
    • Bray, M.1    Davis, K.2    Geisbert, T.3    Schmaljohn, C.4    Huggins, J.5
  • 14
    • 19144365133 scopus 로고    scopus 로고
    • Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection
    • Chandran, K., N. J. Sullivan, U. Felbor, S. P. Whelan, and J. M. Cunningham, 2005: Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection. Science 308, 1643-1645.
    • (2005) Science , vol.308 , pp. 1643-1645
    • Chandran, K.1    Sullivan, N.J.2    Felbor, U.3    Whelan, S.P.4    Cunningham, J.M.5
  • 15
    • 67650866693 scopus 로고    scopus 로고
    • Ebola Zaire virus blocks type I interferon production by exploiting the host SUMO modification machinery
    • Chang, T. H., T. Kubota, M. Matsuoka, S. Jones, S. B. Bradfute, M. Bray, and K. Ozato, 2009: Ebola Zaire virus blocks type I interferon production by exploiting the host SUMO modification machinery. PLoS Pathog. 5, e1000493.
    • (2009) PLoS Pathog. , vol.5
    • Chang, T.H.1    Kubota, T.2    Matsuoka, M.3    Jones, S.4    Bradfute, S.B.5    Bray, M.6    Ozato, K.7
  • 19
    • 0345167006 scopus 로고    scopus 로고
    • A recombinant influenza A virus expressing an RNA-binding-defective NS1 protein induces high levels of beta interferon and is attenuated in mice
    • Donelan, N. R., C. F. Basler, and A. García-Sastre, 2003: A recombinant influenza A virus expressing an RNA-binding-defective NS1 protein induces high levels of beta interferon and is attenuated in mice. J. Virol. 77, 13257-13266.
    • (2003) J. Virol. , vol.77 , pp. 13257-13266
    • Donelan, N.R.1    Basler, C.F.2    García-Sastre, A.3
  • 20
    • 67749095196 scopus 로고    scopus 로고
    • Vpu directs the degradation of the human immunodeficiency virus restriction factor BST-2/Tetherin via a {beta}TrCP-dependent mechanism
    • Douglas, J. L., K. Viswanathan, M. N. McCarroll, J. K. Gustin, K. Früh, and A. V. Moses, 2009: Vpu directs the degradation of the human immunodeficiency virus restriction factor BST-2/Tetherin via a {beta}TrCP-dependent mechanism. J. Virol. 83, 7931-7947.
    • (2009) J. Virol. , vol.83 , pp. 7931-7947
    • Douglas, J.L.1    Viswanathan, K.2    McCarroll, M.N.3    Gustin, J.K.4    Früh, K.5    Moses, A.V.6
  • 21
    • 77954055324 scopus 로고    scopus 로고
    • Antagonism of tetherin restriction of HIV-1 release by Vpu involves binding and sequestration of the restriction factor in a perinuclear compartment
    • Dubé, M., B. B. Roy, P. Guiot-Guillain, J. Binette, J. Mercier, A. Chiasson, and E. A. Cohen, 2010: Antagonism of tetherin restriction of HIV-1 release by Vpu involves binding and sequestration of the restriction factor in a perinuclear compartment. PLoS Pathog. 6, e1000856.
    • (2010) PLoS Pathog. , vol.6
    • Dubé, M.1    Roy, B.B.2    Guiot-Guillain, P.3    Binette, J.4    Mercier, J.5    Chiasson, A.6    Cohen, E.A.7
  • 25
    • 79952390996 scopus 로고    scopus 로고
    • Ebolavirus proteins suppress the effects of small interfering RNA by direct interaction with the mammalian RNA interference pathway
    • Fabozzi, G., C. S. Nabel, M. A. Dolan, and N. J. Sullivan, 2011: Ebolavirus proteins suppress the effects of small interfering RNA by direct interaction with the mammalian RNA interference pathway. J. Virol. 85, 2512-2523.
    • (2011) J. Virol. , vol.85 , pp. 2512-2523
    • Fabozzi, G.1    Nabel, C.S.2    Dolan, M.A.3    Sullivan, N.J.4
  • 26
    • 33845728488 scopus 로고    scopus 로고
    • The VP35 protein of Ebola virus inhibits the antiviral effect mediated by double-stranded RNA-dependent protein kinase PKR
    • Feng, Z., M. Cerveny, Z. Yan, and B. He, 2007: The VP35 protein of Ebola virus inhibits the antiviral effect mediated by double-stranded RNA-dependent protein kinase PKR. J. Virol. 81, 182-192.
    • (2007) J. Virol. , vol.81 , pp. 182-192
    • Feng, Z.1    Cerveny, M.2    Yan, Z.3    He, B.4
  • 27
    • 34347225099 scopus 로고    scopus 로고
    • The dsRNA protein kinase PKR: virus and cell control
    • García, M. A., E. F. Meurs, and M. Esteban, 2007: The dsRNA protein kinase PKR: virus and cell control. Biochimie 89, 799-811.
    • (2007) Biochimie , vol.89 , pp. 799-811
    • García, M.A.1    Meurs, E.F.2    Esteban, M.3
  • 28
    • 33646555810 scopus 로고    scopus 로고
    • Type 1 interferons and the virus-host relationship: a lesson in detente
    • García-Sastre, A., and C. A. Biron, 2006: Type 1 interferons and the virus-host relationship: a lesson in detente. Science 312, 879-882.
    • (2006) Science , vol.312 , pp. 879-882
    • García-Sastre, A.1    Biron, C.A.2
  • 29
    • 70349232639 scopus 로고    scopus 로고
    • Tipping the balance: antagonism of PKR kinase and ADAR1 deaminase functions by virus gene products
    • George, C. X., Z. Li, K. M. Okonski, A. M. Toth, Y. Wang, and C. E. Samuel, 2009: Tipping the balance: antagonism of PKR kinase and ADAR1 deaminase functions by virus gene products. J. Interferon Cytokine Res. 29, 477-487.
    • (2009) J. Interferon Cytokine Res. , vol.29 , pp. 477-487
    • George, C.X.1    Li, Z.2    Okonski, K.M.3    Toth, A.M.4    Wang, Y.5    Samuel, C.E.6
  • 31
    • 77950495072 scopus 로고    scopus 로고
    • Antagonism of CD317 restriction of human immunodeficiency virus type 1 (HIV-1) particle release and depletion of CD317 are separable activities of HIV-1 Vpu
    • Goffinet, C., S. Homann, I. Ambiel, N. Tibroni, D. Rupp, O. T. Keppler, and O. T. Fackler, 2010: Antagonism of CD317 restriction of human immunodeficiency virus type 1 (HIV-1) particle release and depletion of CD317 are separable activities of HIV-1 Vpu. J. Virol. 84, 4089-4094.
    • (2010) J. Virol. , vol.84 , pp. 4089-4094
    • Goffinet, C.1    Homann, S.2    Ambiel, I.3    Tibroni, N.4    Rupp, D.5    Keppler, O.T.6    Fackler, O.T.7
  • 35
    • 34347268783 scopus 로고    scopus 로고
    • Interferon-induced Mx proteins in antiviral host defense
    • Haller, O., P. Staeheli, and G. Kochs, 2007: Interferon-induced Mx proteins in antiviral host defense. Biochimie 89, 812-818.
    • (2007) Biochimie , vol.89 , pp. 812-818
    • Haller, O.1    Staeheli, P.2    Kochs, G.3
  • 36
    • 77649251047 scopus 로고    scopus 로고
    • Immunoelectron microscopic evidence for Tetherin/BST2 as the physical bridge between HIV-1 virions and the plasma membrane
    • Hammonds, J., J. J. Wang, H. Yi, and P. Spearman, 2010: Immunoelectron microscopic evidence for Tetherin/BST2 as the physical bridge between HIV-1 virions and the plasma membrane. PLoS Pathog. 6, e1000749.
    • (2010) PLoS Pathog. , vol.6
    • Hammonds, J.1    Wang, J.J.2    Yi, H.3    Spearman, P.4
  • 37
    • 0037303217 scopus 로고    scopus 로고
    • Biochemical and functional characterization of the Ebola virus VP24 protein: implications for a role in virus assembly and budding
    • Han, Z., H. Boshra, J. O. Sunyer, S. H. Zwiers, J. Paragas, and R. N. Harty, 2003: Biochemical and functional characterization of the Ebola virus VP24 protein: implications for a role in virus assembly and budding. J. Virol. 77, 1793-1800.
    • (2003) J. Virol. , vol.77 , pp. 1793-1800
    • Han, Z.1    Boshra, H.2    Sunyer, J.O.3    Zwiers, S.H.4    Paragas, J.5    Harty, R.N.6
  • 38
    • 29144487064 scopus 로고    scopus 로고
    • Filovirus assembly and budding
    • Hartlieb, B., and W. Weissenhorn, 2006: Filovirus assembly and budding. Virology 344, 64-70.
    • (2006) Virology , vol.344 , pp. 64-70
    • Hartlieb, B.1    Weissenhorn, W.2
  • 39
    • 5344258197 scopus 로고    scopus 로고
    • A C-terminal basic amino acid motif of Zaire ebolavirus VP35 is essential for type I interferon antagonism and displays high identity with the RNA-binding domain of another interferon antagonist, the NS1 protein of influenza A virus
    • Hartman, A. L., J. S. Towner, and S. T. Nichol, 2004: A C-terminal basic amino acid motif of Zaire ebolavirus VP35 is essential for type I interferon antagonism and displays high identity with the RNA-binding domain of another interferon antagonist, the NS1 protein of influenza A virus. Virology 328, 177-184.
    • (2004) Virology , vol.328 , pp. 177-184
    • Hartman, A.L.1    Towner, J.S.2    Nichol, S.T.3
  • 40
    • 33745276555 scopus 로고    scopus 로고
    • Reverse genetic generation of recombinant Zaire Ebola viruses containing disrupted IRF-3 inhibitory domains results in attenuated virus growth in vitro and higher levels of IRF-3 activation without inhibiting viral transcription or replication
    • Hartman, A. L., J. E. Dover, J. S. Towner, and S. T. Nichol, 2006: Reverse genetic generation of recombinant Zaire Ebola viruses containing disrupted IRF-3 inhibitory domains results in attenuated virus growth in vitro and higher levels of IRF-3 activation without inhibiting viral transcription or replication. J. Virol. 80, 6430-6440.
    • (2006) J. Virol. , vol.80 , pp. 6430-6440
    • Hartman, A.L.1    Dover, J.E.2    Towner, J.S.3    Nichol, S.T.4
  • 41
    • 40149109042 scopus 로고    scopus 로고
    • Inhibition of IRF-3 activation by VP35 is critical for the high level of virulence of Ebola virus
    • Hartman, A. L., B. H. Bird, J. S. Towner, Z. A. Antoniadou, S. R. Zaki, and S. T. Nichol, 2008a: Inhibition of IRF-3 activation by VP35 is critical for the high level of virulence of Ebola virus. J. Virol. 82, 2699-2704.
    • (2008) J. Virol. , vol.82 , pp. 2699-2704
    • Hartman, A.L.1    Bird, B.H.2    Towner, J.S.3    Antoniadou, Z.A.4    Zaki, S.R.5    Nichol, S.T.6
  • 42
    • 43949091157 scopus 로고    scopus 로고
    • Whole-genome expression profiling reveals that inhibition of host innate immune response pathways by Ebola virus can be reversed by a single amino acid change in the VP35 protein
    • Hartman, A. L., L. Ling, S. T. Nichol, and M. L. Hibberd, 2008b: Whole-genome expression profiling reveals that inhibition of host innate immune response pathways by Ebola virus can be reversed by a single amino acid change in the VP35 protein. J. Virol. 82, 5348-5358.
    • (2008) J. Virol. , vol.82 , pp. 5348-5358
    • Hartman, A.L.1    Ling, L.2    Nichol, S.T.3    Hibberd, M.L.4
  • 47
    • 0036670360 scopus 로고    scopus 로고
    • The assembly of Ebola virus nucleocapsid requires virion-associated proteins 35 and 24 and posttranslational modification of nucleoprotein
    • Huang, Y., L. Xu, Y. Sun, and G. J. Nabel, 2002: The assembly of Ebola virus nucleocapsid requires virion-associated proteins 35 and 24 and posttranslational modification of nucleoprotein. Mol. Cell 10, 307-316.
    • (2002) Mol. Cell , vol.10 , pp. 307-316
    • Huang, Y.1    Xu, L.2    Sun, Y.3    Nabel, G.J.4
  • 51
    • 76249118239 scopus 로고    scopus 로고
    • The VP35 protein of Ebola virus impairs dendritic cell maturation induced by virus and lipopolysaccharide
    • Jin, H., Z. Yan, B. S. Prabhakar, Z. Feng, Y. Ma, D. Verpooten, B. Ganesh, and B. He, 2010: The VP35 protein of Ebola virus impairs dendritic cell maturation induced by virus and lipopolysaccharide. J. Gen. Virol. 91, 352-361.
    • (2010) J. Gen. Virol. , vol.91 , pp. 352-361
    • Jin, H.1    Yan, Z.2    Prabhakar, B.S.3    Feng, Z.4    Ma, Y.5    Verpooten, D.6    Ganesh, B.7    He, B.8
  • 53
    • 62449106199 scopus 로고    scopus 로고
    • Tetherin-mediated restriction of filovirus budding is antagonized by the Ebola glycoprotein
    • Kaletsky, R. L., J. R. Francica, C. Agrawal-Gamse, and P. Bates, 2009: Tetherin-mediated restriction of filovirus budding is antagonized by the Ebola glycoprotein. Proc. Natl. Acad. Sci. U.S.A. 106, 2886-2891.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 2886-2891
    • Kaletsky, R.L.1    Francica, J.R.2    Agrawal-Gamse, C.3    Bates, P.4
  • 54
    • 20544448655 scopus 로고    scopus 로고
    • How Ebola virus infects cells
    • Kawaoka, Y., 2005: How Ebola virus infects cells. N. Engl. J. Med. 352, 2645-2646.
    • (2005) N. Engl. J. Med. , vol.352 , pp. 2645-2646
    • Kawaoka, Y.1
  • 58
    • 50649111431 scopus 로고    scopus 로고
    • Filoviruses. A compendium of 40years of epidemiological, clinical, and laboratory studies
    • Kuhn, J. H., 2008: Filoviruses. A compendium of 40years of epidemiological, clinical, and laboratory studies. Arch. Virol. Suppl. 20, 13-360.
    • (2008) Arch. Virol. Suppl. , vol.20 , pp. 13-360
    • Kuhn, J.H.1
  • 59
    • 0141494290 scopus 로고    scopus 로고
    • Bst-2/HM1.24 is a raft-associated apical membrane protein with an unusual topology
    • Kupzig, S., V. Korolchuk, R. Rollason, A. Sugden, A. Wilde, and G. Banting, 2003: Bst-2/HM1.24 is a raft-associated apical membrane protein with an unusual topology. Traffic 4, 694-709.
    • (2003) Traffic , vol.4 , pp. 694-709
    • Kupzig, S.1    Korolchuk, V.2    Rollason, R.3    Sugden, A.4    Wilde, A.5    Banting, G.6
  • 60
    • 70350266393 scopus 로고    scopus 로고
    • Antagonism to and intracellular sequestration of human tetherin by the human immunodeficiency virus type 2 envelope glycoprotein
    • Le Tortorec, A., and S. J. Neil, 2009: Antagonism to and intracellular sequestration of human tetherin by the human immunodeficiency virus type 2 envelope glycoprotein. J. Virol. 83, 11966-11978.
    • (2009) J. Virol. , vol.83 , pp. 11966-11978
    • Le Tortorec, A.1    Neil, S.J.2
  • 61
    • 67649807456 scopus 로고    scopus 로고
    • Fold prediction of VP24 protein of Ebola and Marburg viruses using de novo fragment assembly
    • Lee, M. S., F. J. Lebeda, and M. A. Olson, 2009: Fold prediction of VP24 protein of Ebola and Marburg viruses using de novo fragment assembly. J. Struct. Biol. 167, 136-144.
    • (2009) J. Struct. Biol. , vol.167 , pp. 136-144
    • Lee, M.S.1    Lebeda, F.J.2    Olson, M.A.3
  • 65
    • 3142710288 scopus 로고    scopus 로고
    • Contribution of Ebola virus glycoprotein, nucleoprotein, and VP24 to budding of VP40 virus-like particles
    • Licata, J. M., R. F. Johnson, Z. Han, and R. N. Harty, 2004: Contribution of Ebola virus glycoprotein, nucleoprotein, and VP24 to budding of VP40 virus-like particles. J. Virol. 78, 7344-7351.
    • (2004) J. Virol. , vol.78 , pp. 7344-7351
    • Licata, J.M.1    Johnson, R.F.2    Han, Z.3    Harty, R.N.4
  • 66
    • 79951671973 scopus 로고    scopus 로고
    • New developments in the induction and antiviral effectors of type I interferon
    • Liu, S. Y., D. J. Sanchez, and G. Cheng, 2011: New developments in the induction and antiviral effectors of type I interferon. Curr. Opin. Immunol. 23, 57-64.
    • (2011) Curr. Opin. Immunol. , vol.23 , pp. 57-64
    • Liu, S.Y.1    Sanchez, D.J.2    Cheng, G.3
  • 67
    • 77953736161 scopus 로고    scopus 로고
    • Ebola virus glycoprotein counteracts BST-2/Tetherin restriction in a sequence-independent manner that does not require tetherin surface removal
    • Lopez, L. A., S. J. Yang, H. Hauser, C. M. Exline, K. G. Haworth, J. Oldenburg, and P. M. Cannon, 2010: Ebola virus glycoprotein counteracts BST-2/Tetherin restriction in a sequence-independent manner that does not require tetherin surface removal. J. Virol. 84, 7243-7255.
    • (2010) J. Virol. , vol.84 , pp. 7243-7255
    • Lopez, L.A.1    Yang, S.J.2    Hauser, H.3    Exline, C.M.4    Haworth, K.G.5    Oldenburg, J.6    Cannon, P.M.7
  • 68
    • 79551715390 scopus 로고    scopus 로고
    • The IFITM proteins inhibit HIV-1 infection
    • Lu, J., Q. Pan, L. Rong, W. He, S. L. Liu, and C. Liang, 2011: The IFITM proteins inhibit HIV-1 infection. J. Virol. 85, 2126-2137.
    • (2011) J. Virol. , vol.85 , pp. 2126-2137
    • Lu, J.1    Pan, Q.2    Rong, L.3    He, W.4    Liu, S.L.5    Liang, C.6
  • 69
    • 0043166564 scopus 로고    scopus 로고
    • Protection from lethal infection is determined by innate immune responses in a mouse model of Ebola virus infection
    • Mahanty, S., M. Gupta, J. Paragas, M. Bray, R. Ahmed, and P. E. Rollin, 2003: Protection from lethal infection is determined by innate immune responses in a mouse model of Ebola virus infection. Virology 312, 415-424.
    • (2003) Virology , vol.312 , pp. 415-424
    • Mahanty, S.1    Gupta, M.2    Paragas, J.3    Bray, M.4    Ahmed, R.5    Rollin, P.E.6
  • 70
    • 70349663496 scopus 로고    scopus 로고
    • HIV-1 Vpu neutralizes the antiviral factor Tetherin/BST-2 by binding it and directing its beta-TrCP2-dependent degradation
    • Mangeat, B., G. Gers-Huber, M. Lehmann, M. Zufferey, J. Luban, and V. Piguet, 2009: HIV-1 Vpu neutralizes the antiviral factor Tetherin/BST-2 by binding it and directing its beta-TrCP2-dependent degradation. PLoS Pathog. 5, e1000574.
    • (2009) PLoS Pathog. , vol.5
    • Mangeat, B.1    Gers-Huber, G.2    Lehmann, M.3    Zufferey, M.4    Luban, J.5    Piguet, V.6
  • 71
    • 70349267563 scopus 로고    scopus 로고
    • Molecular mechanism of BST2/tetherin downregulation by K5/MIR2 of Kaposi's sarcoma-associated herpesvirus
    • Mansouri, M., K. Viswanathan, J. L. Douglas, J. Hines, J. Gustin, A. V. Moses, and K. Früh, 2009: Molecular mechanism of BST2/tetherin downregulation by K5/MIR2 of Kaposi's sarcoma-associated herpesvirus. J. Virol. 83, 9672-9681.
    • (2009) J. Virol. , vol.83 , pp. 9672-9681
    • Mansouri, M.1    Viswanathan, K.2    Douglas, J.L.3    Hines, J.4    Gustin, J.5    Moses, A.V.6    Früh, K.7
  • 72
    • 73849109409 scopus 로고    scopus 로고
    • Ebolavirus VP24 binding to karyopherins is required for inhibition of interferon signaling
    • Mateo, M., S. P. Reid, L. W. Leung, C. F. Basler, and V. E. Volchkov, 2010: Ebolavirus VP24 binding to karyopherins is required for inhibition of interferon signaling. J. Virol. 84, 1169-1175.
    • (2010) J. Virol. , vol.84 , pp. 1169-1175
    • Mateo, M.1    Reid, S.P.2    Leung, L.W.3    Basler, C.F.4    Volchkov, V.E.5
  • 76
    • 0142159487 scopus 로고    scopus 로고
    • Comparison of the transcription and replication strategies of marburg virus and Ebola virus by using artificial replication systems
    • Mühlberger, E., M. Weik, V. E. Volchkov, H. D. Klenk, and S. Becker, 1999: Comparison of the transcription and replication strategies of marburg virus and Ebola virus by using artificial replication systems. J. Virol. 73, 2333-2342.
    • (1999) J. Virol. , vol.73 , pp. 2333-2342
    • Mühlberger, E.1    Weik, M.2    Volchkov, V.E.3    Klenk, H.D.4    Becker, S.5
  • 77
    • 38549095979 scopus 로고    scopus 로고
    • Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu
    • Neil, S. J., T. Zang, and P. D. Bieniasz, 2008: Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu. Nature, 451, 425-430.
    • (2008) Nature , vol.451 , pp. 425-430
    • Neil, S.J.1    Zang, T.2    Bieniasz, P.D.3
  • 78
    • 84876448867 scopus 로고    scopus 로고
    • NIAID, NIAID category A, B, and C priority pathogens. Available at: (accessed on 10 August 2011).
    • NIAID, 2011: NIAID category A, B, and C priority pathogens. Available at: http://www.niaid.nih.gov/topics/biodefenserelated/biodefense/research/pages/cata.aspx (accessed on 10 August 2011).
    • (2011)
  • 79
    • 0035923525 scopus 로고    scopus 로고
    • Plasma membrane rafts play a critical role in HIV-1 assembly and release
    • Ono, A., and E. O. Freed, 2001: Plasma membrane rafts play a critical role in HIV-1 assembly and release. Proc. Natl. Acad. Sci. U.S.A. 98, 13925-13930.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 13925-13930
    • Ono, A.1    Freed, E.O.2
  • 80
    • 77954043624 scopus 로고    scopus 로고
    • The RING-CH ligase K5 antagonizes restriction of KSHV and HIV-1 particle release by mediating ubiquitin-dependent endosomal degradation of tetherin
    • Pardieu, C., R. Vigan, S. J. Wilson, A. Calvi, T. Zang, P. Bieniasz, P. Kellam, G. J. Towers, and S. J. Neil, 2010: The RING-CH ligase K5 antagonizes restriction of KSHV and HIV-1 particle release by mediating ubiquitin-dependent endosomal degradation of tetherin. PLoS Pathog. 6, e1000843.
    • (2010) PLoS Pathog. , vol.6
    • Pardieu, C.1    Vigan, R.2    Wilson, S.J.3    Calvi, A.4    Zang, T.5    Bieniasz, P.6    Kellam, P.7    Towers, G.J.8    Neil, S.J.9
  • 82
    • 63149113399 scopus 로고    scopus 로고
    • Ebola virus protein VP35 impairs the function of interferon regulatory factor-activating kinases IKKepsilon and TBK-1
    • Prins, K. C., W. B. Cárdenas, and C. F. Basler, 2009: Ebola virus protein VP35 impairs the function of interferon regulatory factor-activating kinases IKKepsilon and TBK-1. J. Virol. 83, 3069-3077.
    • (2009) J. Virol. , vol.83 , pp. 3069-3077
    • Prins, K.C.1    Cárdenas, W.B.2    Basler, C.F.3
  • 83
    • 77957189097 scopus 로고    scopus 로고
    • Basic residues within the ebolavirus VP35 protein are required for its viral polymerase cofactor function
    • Prins, K. C., J. M. Binning, R. S. Shabman, D. W. Leung, G. K. Amarasinghe, and C. F. Basler, 2010a: Basic residues within the ebolavirus VP35 protein are required for its viral polymerase cofactor function. J. Virol. 84, 10581-10591.
    • (2010) J. Virol. , vol.84 , pp. 10581-10591
    • Prins, K.C.1    Binning, J.M.2    Shabman, R.S.3    Leung, D.W.4    Amarasinghe, G.K.5    Basler, C.F.6
  • 86
    • 26244437083 scopus 로고    scopus 로고
    • Homo-oligomerization facilitates the interferon-antagonist activity of the ebolavirus VP35 protein
    • Reid, S. P., W. B. Cárdenas, and C. F. Basler, 2005: Homo-oligomerization facilitates the interferon-antagonist activity of the ebolavirus VP35 protein. Virology, 341, 179-189.
    • (2005) Virology , vol.341 , pp. 179-189
    • Reid, S.P.1    Cárdenas, W.B.2    Basler, C.F.3
  • 88
    • 37149040796 scopus 로고    scopus 로고
    • Ebola virus VP24 proteins inhibit the interaction of NPI-1 subfamily karyopherin alpha proteins with activated STAT1
    • Reid, S. P., C. Valmas, O. Martinez, F. M. Sanchez, and C. F. Basler, 2007: Ebola virus VP24 proteins inhibit the interaction of NPI-1 subfamily karyopherin alpha proteins with activated STAT1. J. Virol. 81, 13469-13477.
    • (2007) J. Virol. , vol.81 , pp. 13469-13477
    • Reid, S.P.1    Valmas, C.2    Martinez, O.3    Sanchez, F.M.4    Basler, C.F.5
  • 89
    • 46249115827 scopus 로고    scopus 로고
    • Interferon-inducible antiviral effectors
    • Sadler, A. J., and B. R. Williams, 2008: Interferon-inducible antiviral effectors. Nat. Rev. Immunol. 8, 559-568.
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 559-568
    • Sadler, A.J.1    Williams, B.R.2
  • 90
    • 60049094369 scopus 로고    scopus 로고
    • Inhibition of Lassa and Marburg virus production by tetherin
    • Sakuma, T., T. Noda, S. Urata, Y. Kawaoka, and J. Yasuda, 2009: Inhibition of Lassa and Marburg virus production by tetherin. J. Virol. 83, 2382-2385.
    • (2009) J. Virol. , vol.83 , pp. 2382-2385
    • Sakuma, T.1    Noda, T.2    Urata, S.3    Kawaoka, Y.4    Yasuda, J.5
  • 91
    • 0029976177 scopus 로고    scopus 로고
    • The virion glycoproteins of Ebola viruses are encoded in two reading frames and are expressed through transcriptional editing
    • Sanchez, A., S. G. Trappier, B. W. Mahy, C. J. Peters, and S. T. Nichol, 1996: The virion glycoproteins of Ebola viruses are encoded in two reading frames and are expressed through transcriptional editing. Proc. Natl. Acad. Sci. U.S.A. 93, 3602-3607.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 3602-3607
    • Sanchez, A.1    Trappier, S.G.2    Mahy, B.W.3    Peters, C.J.4    Nichol, S.T.5
  • 93
    • 34547108380 scopus 로고    scopus 로고
    • JAK-STAT signaling: from interferons to cytokines
    • Schindler, C., D. E. Levy, and T. Decker, 2007: JAK-STAT signaling: from interferons to cytokines. J. Biol. Chem. 282, 20059-20063.
    • (2007) J. Biol. Chem. , vol.282 , pp. 20059-20063
    • Schindler, C.1    Levy, D.E.2    Decker, T.3
  • 94
    • 79955542915 scopus 로고    scopus 로고
    • A diverse range of gene products are effectors of the type I interferon antiviral response
    • Schoggins, J. W., S. J. Wilson, M. Panis, M. Y. Murphy, C. T. Jones, P. Bieniasz, and C. M. Rice, 2011: A diverse range of gene products are effectors of the type I interferon antiviral response. Nature 472, 481-485.
    • (2011) Nature , vol.472 , pp. 481-485
    • Schoggins, J.W.1    Wilson, S.J.2    Panis, M.3    Murphy, M.Y.4    Jones, C.T.5    Bieniasz, P.6    Rice, C.M.7
  • 95
    • 69249205651 scopus 로고    scopus 로고
    • Ebola virus VP35 antagonizes PKR activity through its C-terminal interferon inhibitory domain
    • Schumann, M., T. Gantke, and E. Muhlberger, 2009: Ebola virus VP35 antagonizes PKR activity through its C-terminal interferon inhibitory domain. J. Virol. 83, 8993-8997.
    • (2009) J. Virol. , vol.83 , pp. 8993-8997
    • Schumann, M.1    Gantke, T.2    Muhlberger, E.3
  • 96
    • 0030670639 scopus 로고    scopus 로고
    • Extracellular signal-dependent nuclear import of Stat1 is mediated by nuclear pore-targeting complex formation with NPI-1, but not Rch1
    • Sekimoto, T., N. Imamoto, K. Nakajima, T. Hirano, and Y. Yoneda, 1997: Extracellular signal-dependent nuclear import of Stat1 is mediated by nuclear pore-targeting complex formation with NPI-1, but not Rch1. EMBO J. 16, 7067-7077.
    • (1997) EMBO J. , vol.16 , pp. 7067-7077
    • Sekimoto, T.1    Imamoto, N.2    Nakajima, K.3    Hirano, T.4    Yoneda, Y.5
  • 97
    • 78651500759 scopus 로고    scopus 로고
    • The small interferon-induced transmembrane genes and proteins
    • Siegrist, F., M. Ebeling, and U. Certa, 2011: The small interferon-induced transmembrane genes and proteins. J. Interferon Cytokine Res. 31, 183-197.
    • (2011) J. Interferon Cytokine Res. , vol.31 , pp. 183-197
    • Siegrist, F.1    Ebeling, M.2    Certa, U.3
  • 102
  • 103
    • 0029589329 scopus 로고
    • GP mRNA of Ebola virus is edited by the Ebola virus polymerase and by T7 and vaccinia virus polymerases
    • Volchkov, V. E., S. Becker, V. A. Volchkova, V. A. Ternovoj, A. N. Kotov, S. V. Netesov, and H. D. Klenk, 1995: GP mRNA of Ebola virus is edited by the Ebola virus polymerase and by T7 and vaccinia virus polymerases. Virology 214, 421-430.
    • (1995) Virology , vol.214 , pp. 421-430
    • Volchkov, V.E.1    Becker, S.2    Volchkova, V.A.3    Ternovoj, V.A.4    Kotov, A.N.5    Netesov, S.V.6    Klenk, H.D.7
  • 105
    • 0033527892 scopus 로고    scopus 로고
    • Delta-peptide is the carboxy-terminal cleavage fragment of the nonstructural small glycoprotein sGP of Ebola virus
    • Volchkova, V. A., H. D. Klenk, and V. E. Volchkov, 1999: Delta-peptide is the carboxy-terminal cleavage fragment of the nonstructural small glycoprotein sGP of Ebola virus. Virology 265, 164-171.
    • (1999) Virology , vol.265 , pp. 164-171
    • Volchkova, V.A.1    Klenk, H.D.2    Volchkov, V.E.3
  • 107
    • 80054992566 scopus 로고    scopus 로고
    • Influenza virus is not restricted by tetherin whereas influenza VLP production is restricted by tetherin
    • 1)
    • Watanabe, R., G. P. Leser, and R. A. Lamb, 2011: Influenza virus is not restricted by tetherin whereas influenza VLP production is restricted by tetherin. Virology 417(1), 50-56.
    • (2011) Virology , vol.417 , pp. 50-56
    • Watanabe, R.1    Leser, G.P.2    Lamb, R.A.3
  • 108
    • 78649404289 scopus 로고    scopus 로고
    • Interferon-induced cell membrane proteins, IFITM3 and tetherin, inhibit vesicular stomatitis virus infection via distinct mechanisms
    • Weidner, J. M., D. Jiang, X. B. Pan, J. Chang, T. M. Block, and J. T. Guo, 2010: Interferon-induced cell membrane proteins, IFITM3 and tetherin, inhibit vesicular stomatitis virus infection via distinct mechanisms. J. Virol. 84, 12646-12657.
    • (2010) J. Virol. , vol.84 , pp. 12646-12657
    • Weidner, J.M.1    Jiang, D.2    Pan, X.B.3    Chang, J.4    Block, T.M.5    Guo, J.T.6
  • 109
    • 0031954296 scopus 로고    scopus 로고
    • Characterization of Ebola virus entry by using pseudotyped viruses: identification of receptor-deficient cell lines
    • Wool-Lewis, R. J., and P. Bates, 1998: Characterization of Ebola virus entry by using pseudotyped viruses: identification of receptor-deficient cell lines. J. Virol. 72, 3155-3160.
    • (1998) J. Virol. , vol.72 , pp. 3155-3160
    • Wool-Lewis, R.J.1    Bates, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.