메뉴 건너뛰기




Volumn 90, Issue 13, 2016, Pages 6140-6147

NSs virulence factor of Rift Valley fever virus engages the F-box proteins FBXW11 and β-TRCP1 to degrade the antiviral protein kinase PKR

Author keywords

[No Author keywords available]

Indexed keywords

BETA TRANSDUCIN REPEAT CONTAINING PROTEIN; F BOX PROTEIN; FBXW11 PROTEIN; INITIATION FACTOR 2ALPHA; PROTEIN KINASE R; SKP1 PROTEIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; VIRULENCE FACTOR; CULLIN; CULLIN 1; FBXW11 PROTEIN, HUMAN; S PHASE KINASE ASSOCIATED PROTEIN; SKP1 PROTEIN, HUMAN; SMALL INTERFERING RNA; UBIQUITIN PROTEIN LIGASE; VIRAL PROTEIN;

EID: 84975298037     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00016-16     Document Type: Article
Times cited : (47)

References (37)
  • 1
    • 84943453553 scopus 로고    scopus 로고
    • Rift Valley fever virus: a review of diagnosis and vaccination, and implications for emergence in Europe
    • Mansfield KL, Banyard AC, McElhinney L, Johnson N, Horton DL, Hernandez-Triana LM, Fooks AR. 2015. Rift Valley fever virus: a review of diagnosis and vaccination, and implications for emergence in Europe. Vaccine 33:5520-5531. http://dx.doi.org/10.1016/j.vaccine.2015.08.020.
    • (2015) Vaccine , vol.33 , pp. 5520-5531
    • Mansfield, K.L.1    Banyard, A.C.2    McElhinney, L.3    Johnson, N.4    Horton, D.L.5    Hernandez-Triana, L.M.6    Fooks, A.R.7
  • 2
    • 84941996205 scopus 로고    scopus 로고
    • Interplay between the virus and host in Rift Valley fever pathogenesis
    • Terasaki K, Makino S. 2015. Interplay between the virus and host in Rift Valley fever pathogenesis. J Innate Immun 7:450-458. http://dx.doi.org/10.1159/000373924.
    • (2015) J Innate Immun , vol.7 , pp. 450-458
    • Terasaki, K.1    Makino, S.2
  • 3
  • 5
    • 84880511791 scopus 로고    scopus 로고
    • Relevance of Rift Valley fever to public health in the European Union
    • Chevalier V. 2013. Relevance of Rift Valley fever to public health in the European Union. Clin Microbiol Infect 19:705-708. http://dx.doi.org/10.1111/1469-0691.12163.
    • (2013) Clin Microbiol Infect , vol.19 , pp. 705-708
    • Chevalier, V.1
  • 6
    • 84897147048 scopus 로고    scopus 로고
    • The risk of Rift Valley fever virus introduction and establishment in the United States and European Union
    • Rolin AI, Berrang-Ford L, Kulkarni MA. 2013. The risk of Rift Valley fever virus introduction and establishment in the United States and European Union. Emerg Microbes Infect 2:e81. http://dx.doi.org/10.1038/emi.2013.81.
    • (2013) Emerg Microbes Infect , vol.2
    • Rolin, A.I.1    Berrang-Ford, L.2    Kulkarni, M.A.3
  • 7
    • 84857712949 scopus 로고    scopus 로고
    • Induction of DNA damage signaling upon Rift Valley fever virus infection results in cell cycle arrest and increased viral replication
    • Baer A, Austin D, Narayanan A, Popova T, Kainulainen M, Bailey C, Kashanchi F, Weber F, Kehn-Hall K. 2012. Induction of DNA damage signaling upon Rift Valley fever virus infection results in cell cycle arrest and increased viral replication. J Biol Chem 287:7399-7410. http://dx.doi.org/10.1074/jbc.M111.296608.
    • (2012) J Biol Chem , vol.287 , pp. 7399-7410
    • Baer, A.1    Austin, D.2    Narayanan, A.3    Popova, T.4    Kainulainen, M.5    Bailey, C.6    Kashanchi, F.7    Weber, F.8    Kehn-Hall, K.9
  • 8
    • 33847062553 scopus 로고    scopus 로고
    • The NSm proteins of Rift Valley fever virus are dispensable for maturation, replication and infection
    • Gerrard SR, Bird BH, Albarino CG, Nichol ST. 2007. The NSm proteins of Rift Valley fever virus are dispensable for maturation, replication and infection. Virology 359:459-465. http://dx.doi.org/10.1016/j.virol.2006.09.035.
    • (2007) Virology , vol.359 , pp. 459-465
    • Gerrard, S.R.1    Bird, B.H.2    Albarino, C.G.3    Nichol, S.T.4
  • 9
    • 66149086445 scopus 로고    scopus 로고
    • NSs protein of Rift Valley fever virus induces the specific degradation of the double-stranded RNAdependent protein kinase
    • Habjan M, Pichlmair A, Elliott RM, Overby AK, Glatter T, Gstaiger M, Superti-Furga G, Unger H, Weber F. 2009. NSs protein of Rift Valley fever virus induces the specific degradation of the double-stranded RNAdependent protein kinase. J Virol 83:4365-4375. http://dx.doi.org/10.1128/JVI.02148-08.
    • (2009) J Virol , vol.83 , pp. 4365-4375
    • Habjan, M.1    Pichlmair, A.2    Elliott, R.M.3    Overby, A.K.4    Glatter, T.5    Gstaiger, M.6    Superti-Furga, G.7    Unger, H.8    Weber, F.9
  • 10
    • 61449213995 scopus 로고    scopus 로고
    • Rift Valley fever virus NSs protein promotes post-transcriptional downregulation of protein kinase PKR and inhibits eIF2alpha phosphorylation
    • Ikegami T, Narayanan K, Won S, Kamitani W, Peters CJ, Makino S. 2009. Rift Valley fever virus NSs protein promotes post-transcriptional downregulation of protein kinase PKR and inhibits eIF2alpha phosphorylation. PLoS Pathog 5:e1000287. http://dx.doi.org/10.1371/journal.ppat.1000287.
    • (2009) PLoS Pathog , vol.5
    • Ikegami, T.1    Narayanan, K.2    Won, S.3    Kamitani, W.4    Peters, C.J.5    Makino, S.6
  • 11
    • 84895753857 scopus 로고    scopus 로고
    • Deletion of the NSm virulence gene of Rift Valley fever virus inhibits virus replication in and dissemination from the midgut of Aedes aegypti mosquitoes
    • Kading RC, Crabtree MB, Bird BH, Nichol ST, Erickson BR, Horiuchi K, Biggerstaff BJ, Miller BR. 2014. Deletion of the NSm virulence gene of Rift Valley fever virus inhibits virus replication in and dissemination from the midgut of Aedes aegypti mosquitoes. PLoS Negl Trop Dis 8:e2670. http://dx.doi.org/10.1371/journal.pntd.0002670.
    • (2014) PLoS Negl Trop Dis , vol.8
    • Kading, R.C.1    Crabtree, M.B.2    Bird, B.H.3    Nichol, S.T.4    Erickson, B.R.5    Horiuchi, K.6    Biggerstaff, B.J.7    Miller, B.R.8
  • 12
    • 37049008494 scopus 로고    scopus 로고
    • NSm protein of Rift Valley fever virus suppresses virus-induced apoptosis
    • Won S, Ikegami T, Peters CJ, Makino S. 2007. NSm protein of Rift Valley fever virus suppresses virus-induced apoptosis. J Virol 81:13335-13345. http://dx.doi.org/10.1128/JVI.01238-07.
    • (2007) J Virol , vol.81 , pp. 13335-13345
    • Won, S.1    Ikegami, T.2    Peters, C.J.3    Makino, S.4
  • 13
    • 84896987305 scopus 로고    scopus 로고
    • Interferon-stimulated genes: a complex web of host defenses
    • Schneider WM, Chevillotte MD, Rice CM. 2014. Interferon-stimulated genes: a complex web of host defenses. Annu Rev Immunol 32:513-545. http://dx.doi.org/10.1146/annurev-immunol-032713-120231.
    • (2014) Annu Rev Immunol , vol.32 , pp. 513-545
    • Schneider, W.M.1    Chevillotte, M.D.2    Rice, C.M.3
  • 14
    • 46249115827 scopus 로고    scopus 로고
    • Interferon-inducible antiviral effectors
    • Sadler AJ, Williams BR. 2008. Interferon-inducible antiviral effectors. Nat Rev Immunol 8:559-568. http://dx.doi.org/10.1038/nri2314.
    • (2008) Nat Rev Immunol , vol.8 , pp. 559-568
    • Sadler, A.J.1    Williams, B.R.2
  • 15
    • 84902191775 scopus 로고    scopus 로고
    • Protein kinase R and the inflammasome
    • Yim HC, Williams BR. 2014. Protein kinase R and the inflammasome. J Interferon Cytokine Res 34:447-454. http://dx.doi.org/10.1089/jir.2014.0008.
    • (2014) J Interferon Cytokine Res , vol.34 , pp. 447-454
    • Yim, H.C.1    Williams, B.R.2
  • 16
    • 0034767753 scopus 로고    scopus 로고
    • Antiviral actions of interferons
    • Samuel CE. 2001. Antiviral actions of interferons. Clin Microbiol Rev 14:778-809. http://dx.doi.org/10.1128/CMR.14.4.778-809.2001.
    • (2001) Clin Microbiol Rev , vol.14 , pp. 778-809
    • Samuel, C.E.1
  • 17
    • 0035152344 scopus 로고    scopus 로고
    • Genetic evidence for an interferon-antagonistic function of Rift Valley fever virus nonstructural protein NSs
    • Bouloy M, Janzen C, Vialat P, Khun H, Pavlovic J, Huerre M, Haller O. 2001. Genetic evidence for an interferon-antagonistic function of Rift Valley fever virus nonstructural protein NSs. J Virol 75:1371-1377. http://dx.doi.org/10.1128/JVI.75.3.1371-1377.2001.
    • (2001) J Virol , vol.75 , pp. 1371-1377
    • Bouloy, M.1    Janzen, C.2    Vialat, P.3    Khun, H.4    Pavlovic, J.5    Huerre, M.6    Haller, O.7
  • 18
    • 4444374579 scopus 로고    scopus 로고
    • NSs protein of Rift Valley fever virus blocks interferon production by inhibiting host gene transcription
    • Billecocq A, Spiegel M, Vialat P, Kohl A, Weber F, Bouloy M, Haller O. 2004. NSs protein of Rift Valley fever virus blocks interferon production by inhibiting host gene transcription. J Virol 78:9798-9806. http://dx.doi.org/10.1128/JVI.78.18.9798-9806.2004.
    • (2004) J Virol , vol.78 , pp. 9798-9806
    • Billecocq, A.1    Spiegel, M.2    Vialat, P.3    Kohl, A.4    Weber, F.5    Bouloy, M.6    Haller, O.7
  • 20
    • 84929179468 scopus 로고    scopus 로고
    • A ωXaV motif in the Rift Valley fever virus NSs protein is essential for degrading p62, forming nuclear filaments and virulence
    • Cyr N, de la Fuente C, Lecoq L, Guendel I, Chabot PR, Kehn-Hall K, Omichinski JG. 2015. A ωXaV motif in the Rift Valley fever virus NSs protein is essential for degrading p62, forming nuclear filaments and virulence. Proc Natl Acad Sci U S A 112:6021-6026. http://dx.doi.org/10.1073/pnas.1503688112.
    • (2015) Proc Natl Acad Sci U S A , vol.112 , pp. 6021-6026
    • Cyr, N.1    de la Fuente, C.2    Lecoq, L.3    Guendel, I.4    Chabot, P.R.5    Kehn-Hall, K.6    Omichinski, J.G.7
  • 21
    • 1342264311 scopus 로고    scopus 로고
    • TFIIH transcription factor, a target for the Rift Valley hemorrhagic fever virus
    • Le May N, Dubaele S, De Santis LP, Billecocq A, Bouloy M, Egly JM. 2004. TFIIH transcription factor, a target for the Rift Valley hemorrhagic fever virus. Cell 116:541-550. http://dx.doi.org/10.1016/S0092-8674(04)00132-1.
    • (2004) Cell , vol.116 , pp. 541-550
    • Le May, N.1    Dubaele, S.2    De Santis, L.P.3    Billecocq, A.4    Bouloy, M.5    Egly, J.M.6
  • 22
    • 84894536027 scopus 로고    scopus 로고
    • Virulence factor NSs of Rift Valley fever virus recruits the F-box protein FBXO3 to degrade subunit p62 of general transcription factor TFIIH
    • Kainulainen M, Habjan M, Hubel P, Busch L, Lau S, Colinge J, Superti-Furga G, Pichlmair A, Weber F. 2014. Virulence factor NSs of Rift Valley fever virus recruits the F-box protein FBXO3 to degrade subunit p62 of general transcription factor TFIIH. J Virol 88:3464-3473. http://dx.doi.org/10.1128/JVI.02914-13.
    • (2014) J Virol , vol.88 , pp. 3464-3473
    • Kainulainen, M.1    Habjan, M.2    Hubel, P.3    Busch, L.4    Lau, S.5    Colinge, J.6    Superti-Furga, G.7    Pichlmair, A.8    Weber, F.9
  • 23
    • 80052073169 scopus 로고    scopus 로고
    • NSs protein of Rift Valley fever virus promotes posttranslational downregulation of the TFIIH subunit p62
    • Kalveram B, Lihoradova O, Ikegami T. 2011. NSs protein of Rift Valley fever virus promotes posttranslational downregulation of the TFIIH subunit p62. J Virol 85:6234-6243. http://dx.doi.org/10.1128/JVI.02255-10.
    • (2011) J Virol , vol.85 , pp. 6234-6243
    • Kalveram, B.1    Lihoradova, O.2    Ikegami, T.3
  • 25
    • 79952792593 scopus 로고    scopus 로고
    • Interferon antagonist NSs of La Crosse virus triggers a DNA damage response-like degradation of transcribing RNA polymerase II
    • Verbruggen P, Ruf M, Blakqori G, Overby AK, Heidemann M, Eick D, Weber F. 2011. Interferon antagonist NSs of La Crosse virus triggers a DNA damage response-like degradation of transcribing RNA polymerase II. J Biol Chem 286:3681-3692. http://dx.doi.org/10.1074/jbc.M110.154799.
    • (2011) J Biol Chem , vol.286 , pp. 3681-3692
    • Verbruggen, P.1    Ruf, M.2    Blakqori, G.3    Overby, A.K.4    Heidemann, M.5    Eick, D.6    Weber, F.7
  • 26
    • 0345064267 scopus 로고
    • Monoclonal antibodies to an interferon-induced Mr 68, 000 protein and their use for the detection of double-stranded RNA-dependent protein kinase in human cells
    • Laurent AG, Krust B, Galabru J, Svab J, Hovanessian AG. 1985. Monoclonal antibodies to an interferon-induced Mr 68, 000 protein and their use for the detection of double-stranded RNA-dependent protein kinase in human cells. Proc Natl Acad Sci U S A 82:4341-4345. http://dx.doi.org/10.1073/pnas.82.13.4341.
    • (1985) Proc Natl Acad Sci U S A , vol.82 , pp. 4341-4345
    • Laurent, A.G.1    Krust, B.2    Galabru, J.3    Svab, J.4    Hovanessian, A.G.5
  • 27
    • 63949084607 scopus 로고    scopus 로고
    • SUnSET, a nonradioactive method to monitor protein synthesis
    • Schmidt EK, Clavarino G, Ceppi M, Pierre P. 2009. SUnSET, a nonradioactive method to monitor protein synthesis. Nat Methods 6:275-277. http://dx.doi.org/10.1038/nmeth.1314.
    • (2009) Nat Methods , vol.6 , pp. 275-277
    • Schmidt, E.K.1    Clavarino, G.2    Ceppi, M.3    Pierre, P.4
  • 28
    • 84943635310 scopus 로고    scopus 로고
    • Synthesis of an arrayed sgRNA library targeting the human genome
    • Schmidt T, Schmid-Burgk JL, Hornung V. 2015. Synthesis of an arrayed sgRNA library targeting the human genome. Sci Rep 5:14987. http://dx.doi.org/10.1038/srep14987.
    • (2015) Sci Rep , vol.5 , pp. 14987
    • Schmidt, T.1    Schmid-Burgk, J.L.2    Hornung, V.3
  • 29
    • 84907214220 scopus 로고    scopus 로고
    • OutKnocker: a web tool for rapid and simple genotyping of designer nuclease edited cell lines
    • Schmid-Burgk JL, Schmidt T, Gaidt MM, Pelka K, Latz E, Ebert TS, Hornung V. 2014. OutKnocker: a web tool for rapid and simple genotyping of designer nuclease edited cell lines. Genome Res 24:1719-1723. http://dx.doi.org/10.1101/gr.176701.114.
    • (2014) Genome Res , vol.24 , pp. 1719-1723
    • Schmid-Burgk, J.L.1    Schmidt, T.2    Gaidt, M.M.3    Pelka, K.4    Latz, E.5    Ebert, T.S.6    Hornung, V.7
  • 30
    • 84878260314 scopus 로고    scopus 로고
    • Mechanisms and function of substrate recruitment by F-box proteins
    • Skaar JR, Pagan JK, Pagano M. 2013. Mechanisms and function of substrate recruitment by F-box proteins. Nat Rev Mol Cell Biol 14:369-381. http://dx.doi.org/10.1038/nrm3582.
    • (2013) Nat Rev Mol Cell Biol , vol.14 , pp. 369-381
    • Skaar, J.R.1    Pagan, J.K.2    Pagano, M.3
  • 31
    • 34547128096 scopus 로고    scopus 로고
    • Protein kinase PKR plays a stimulus-and virus-dependent role in apoptotic death and virus multiplication in human cells
    • Zhang P, Samuel CE. 2007. Protein kinase PKR plays a stimulus-and virus-dependent role in apoptotic death and virus multiplication in human cells. J Virol 81:8192-8200. http://dx.doi.org/10.1128/JVI.00426-07.
    • (2007) J Virol , vol.81 , pp. 8192-8200
    • Zhang, P.1    Samuel, C.E.2
  • 32
    • 66449110553 scopus 로고    scopus 로고
    • SnapShot: F box proteins I
    • 1160-1160.e1161
    • Skaar JR, Pagan JK, Pagano M. 2009. SnapShot: F box proteins I. Cell 137:1160-1160.e1161. http://dx.doi.org/10.1016/j.cell.2009.05.039.
    • (2009) Cell , vol.137
    • Skaar, J.R.1    Pagan, J.K.2    Pagano, M.3
  • 33
    • 67549093540 scopus 로고    scopus 로고
    • SnapShot: F box proteins II
    • 1358-1358.e1351
    • Skaar JR, D'Angiolella V, Pagan JK, Pagano M. 2009. SnapShot: F box proteins II. Cell 137:1358-1358.e1351. http://dx.doi.org/10.1016/j.cell.2009.05.040.
    • (2009) Cell , vol.137
    • Skaar, J.R.1    D'Angiolella, V.2    Pagan, J.K.3    Pagano, M.4
  • 34
    • 84959506581 scopus 로고    scopus 로고
    • Protein kinase R degradation is essential for Rift Valley fever virus infection and is regulated by SKP1-CUL1-F-box (SCF)FBXW11-NSs E3 ligase
    • Mudhasani R, Tran JP, Retterer C, Kota KP, Whitehouse CA, Bavari S. 2016. Protein kinase R degradation is essential for Rift Valley fever virus infection and is regulated by SKP1-CUL1-F-box (SCF)FBXW11-NSs E3 ligase. PLoS Pathog 12:e1005437. http://dx.doi.org/10.1371/journal.ppat.1005437.
    • (2016) PLoS Pathog , vol.12
    • Mudhasani, R.1    Tran, J.P.2    Retterer, C.3    Kota, K.P.4    Whitehouse, C.A.5    Bavari, S.6
  • 36
    • 84905666717 scopus 로고    scopus 로고
    • A high-content RNAi screen identifies ubiquitin modifiers that regulate TNF-dependent nuclear accumulation of NF-κB
    • Fraser B, Maranchuk RA, Foley E. 2014. A high-content RNAi screen identifies ubiquitin modifiers that regulate TNF-dependent nuclear accumulation of NF-κB. Front Immunol 5:322. http://dx.doi.org/10.3389/fimmu.2014.00322.
    • (2014) Front Immunol , vol.5 , pp. 322
    • Fraser, B.1    Maranchuk, R.A.2    Foley, E.3
  • 37
    • 0034723296 scopus 로고    scopus 로고
    • Homodimer of two F-box proteins α-TrCP1 or α-TrCP2 binds to IkappaBalpha for signal-dependent ubiquitination
    • Suzuki H, Chiba T, Suzuki T, Fujita T, Ikenoue T, Omata M, Furuichi K, Shikama H, Tanaka K. 2000. Homodimer of two F-box proteins α-TrCP1 or α-TrCP2 binds to IkappaBalpha for signal-dependent ubiquitination. J Biol Chem 275:2877-2884. http://dx.doi.org/10.1074/jbc.275.4.2877.
    • (2000) J Biol Chem , vol.275 , pp. 2877-2884
    • Suzuki, H.1    Chiba, T.2    Suzuki, T.3    Fujita, T.4    Ikenoue, T.5    Omata, M.6    Furuichi, K.7    Shikama, H.8    Tanaka, K.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.