메뉴 건너뛰기




Volumn 87, Issue 8, 2013, Pages 4609-4622

Membrane topology and function of dengue virus NS2A protein

Author keywords

[No Author keywords available]

Indexed keywords

NONSTRUCTURAL PROTEIN 2; NONSTRUCTURAL PROTEIN 2A; UNCLASSIFIED DRUG;

EID: 84875777404     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02424-12     Document Type: Article
Times cited : (163)

References (44)
  • 2
    • 0018770470 scopus 로고
    • Methylation status of intracellular dengue type 2 40 S RNA
    • Cleaves GR, Dubin DT. 1979. Methylation status of intracellular dengue type 2 40 S RNA. Virology 96:159-165.
    • (1979) Virology , vol.96 , pp. 159-165
    • Cleaves, G.R.1    Dubin, D.T.2
  • 3
    • 0032486487 scopus 로고    scopus 로고
    • Subcellular localization and some biochemical properties of the flavivirus Kunjin nonstructural proteins NS2A and NS4A
    • Mackenzie JM, Khromykh AA, Jones MK, Westaway EG. 1998. Subcellular localization and some biochemical properties of the flavivirus Kunjin nonstructural proteins NS2A and NS4A. Virology 245:203-215.
    • (1998) Virology , vol.245 , pp. 203-215
    • Mackenzie, J.M.1    Khromykh, A.A.2    Jones, M.K.3    Westaway, E.G.4
  • 4
    • 0030774240 scopus 로고    scopus 로고
    • Trans-complementation of yellow fever virus NS1 reveals a role in early RNA replication
    • Lindenbach BD, Rice CM. 1997. Trans-complementation of yellow fever virus NS1 reveals a role in early RNA replication. J. Virol. 71:9608-9617.
    • (1997) J. Virol. , vol.71 , pp. 9608-9617
    • Lindenbach, B.D.1    Rice, C.M.2
  • 5
    • 33645798035 scopus 로고    scopus 로고
    • Vascular leakage in severe dengue virus infections: a potential role for the nonstructural viral protein NS1 and complement
    • Avirutnan P, Punyadee N, Noisakran S, Komoltri C, Thiemmeca S, et al. 2006. Vascular leakage in severe dengue virus infections: a potential role for the nonstructural viral protein NS1 and complement. J. Infect. Dis. 193:1078-1088.
    • (2006) J. Infect. Dis. , vol.193 , pp. 1078-1088
    • Avirutnan, P.1    Punyadee, N.2    Noisakran, S.3    Komoltri, C.4    Thiemmeca, S.5
  • 6
    • 0027446550 scopus 로고
    • RNA-stimulated NTPase activity associated with yellow fever virus NS3 protein expressed in bacteria
    • Warrener P, Tamura JK, Collett MS. 1993. RNA-stimulated NTPase activity associated with yellow fever virus NS3 protein expressed in bacteria. J. Virol. 67:989-996.
    • (1993) J. Virol. , vol.67 , pp. 989-996
    • Warrener, P.1    Tamura, J.K.2    Collett, M.S.3
  • 7
    • 0025865788 scopus 로고
    • In vitro synthesis of West Nile virus proteins indicates that the amino-terminal segment of the NS3 protein contains the active centre of the protease which cleaves the viral polyprotein after multiple basic amino acids
    • Wengler G, Czaya G, Farber PM, Hegemann JH. 1991. In vitro synthesis of West Nile virus proteins indicates that the amino-terminal segment of the NS3 protein contains the active centre of the protease which cleaves the viral polyprotein after multiple basic amino acids. J. Gen. Virol. 72: 851-858.
    • (1991) J. Gen. Virol. , vol.72 , pp. 851-858
    • Wengler, G.1    Czaya, G.2    Farber, P.M.3    Hegemann, J.H.4
  • 8
    • 0036232747 scopus 로고    scopus 로고
    • Mutations in the yellow fever virus nonstructural protein NS2A selectively block production of infectious particles
    • Kummerer BM, Rice CM. 2002. Mutations in the yellow fever virus nonstructural protein NS2A selectively block production of infectious particles. J. Virol. 76:4773-4784.
    • (2002) J. Virol. , vol.76 , pp. 4773-4784
    • Kummerer, B.M.1    Rice, C.M.2
  • 9
    • 41149101538 scopus 로고    scopus 로고
    • Yellow fever virus NS3 plays an essential role in virus assembly independent of its known enzymatic functions
    • Patkar CG, Kuhn RJ. 2008. Yellow fever virus NS3 plays an essential role in virus assembly independent of its known enzymatic functions. J. Virol. 82:3342-3352.
    • (2008) J. Virol. , vol.82 , pp. 3342-3352
    • Patkar, C.G.1    Kuhn, R.J.2
  • 11
    • 0037013858 scopus 로고    scopus 로고
    • An RNA cap (nucleoside-2'-O-)-methyltransferase in the flavivirus RNA polymerase NS5: crystal structure and functional characterization
    • Egloff MP, Benarroch D, Selisko B, Romette JL, Canard B. 2002. An RNA cap (nucleoside-2'-O-)-methyltransferase in the flavivirus RNA polymerase NS5: crystal structure and functional characterization. EMBO J. 21:2757-2768.
    • (2002) EMBO J. , vol.21 , pp. 2757-2768
    • Egloff, M.P.1    Benarroch, D.2    Selisko, B.3    Romette, J.L.4    Canard, B.5
  • 12
    • 33748669852 scopus 로고    scopus 로고
    • West Nile virus 5'-cap structure is formed by sequential guanine N-7 and ribose 2'-O methylations by nonstructural protein 5
    • Ray D, Shah A, Tilgner M, Guo Y, Zhao Y, Dong H, Deas TS, Zhou Y, Li H, Shi PY. 2006. West Nile virus 5'-cap structure is formed by sequential guanine N-7 and ribose 2'-O methylations by nonstructural protein 5. J. Virol. 80:8362-8370.
    • (2006) J. Virol. , vol.80 , pp. 8362-8370
    • Ray, D.1    Shah, A.2    Tilgner, M.3    Guo, Y.4    Zhao, Y.5    Dong, H.6    Deas, T.S.7    Zhou, Y.8    Li, H.9    Shi, P.Y.10
  • 13
    • 73249127604 scopus 로고    scopus 로고
    • The flavivirus NS5 protein is a true RNA guanylyltransferase that catalyzes a two-step reaction to form theRNAcap structure
    • Issur M, Geiss BJ, Bougie I, Picard-Jean F, Despins S, Mayette J, Hobdey SE, Bisaillon M. 2009. The flavivirus NS5 protein is a true RNA guanylyltransferase that catalyzes a two-step reaction to form theRNAcap structure. RNA 15:2340-2350.
    • (2009) RNA , vol.15 , pp. 2340-2350
    • Issur, M.1    Geiss, B.J.2    Bougie, I.3    Picard-Jean, F.4    Despins, S.5    Mayette, J.6    Hobdey, S.E.7    Bisaillon, M.8
  • 14
    • 0035955628 scopus 로고    scopus 로고
    • De novo synthesis of RNA by the dengue virus RNA-dependent RNA polymerase exhibits temperature dependence at the initiation but not elongation phase
    • Ackermann M, Padmanabhan R. 2001. De novo synthesis of RNA by the dengue virus RNA-dependent RNA polymerase exhibits temperature dependence at the initiation but not elongation phase. J. Biol. Chem. 276: 39926-39937.
    • (2001) J. Biol. Chem. , vol.276 , pp. 39926-39937
    • Ackermann, M.1    Padmanabhan, R.2
  • 15
  • 18
    • 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, Buhler S, Bartenschlager R. 2007. The non-structural protein 4A of dengue virus is an integral membrane protein inducing membrane alterations in a 2K-regulated manner. J. Biol. Chem. 282:8873-8882.
    • (2007) J. Biol. Chem. , vol.282 , pp. 8873-8882
    • Miller, S.1    Kastner, S.2    Krijnse-Locker, J.3    Buhler, S.4    Bartenschlager, R.5
  • 19
    • 33646851580 scopus 로고    scopus 로고
    • Subcellular localization and membrane topology of the Dengue virus type 2 non-structural protein 4B
    • Miller S, Sparacio S, Bartenschlager R. 2006. Subcellular localization and membrane topology of the Dengue virus type 2 non-structural protein 4B. J. Biol. Chem. 281:8854-8863.
    • (2006) J. Biol. Chem. , vol.281 , pp. 8854-8863
    • Miller, S.1    Sparacio, S.2    Bartenschlager, R.3
  • 22
    • 0024590191 scopus 로고
    • Yellow fever virus proteins NS2A, NS2B, and NS4B: identification and partial N-terminal amino acid sequence analysis
    • Chambers TJ, McCourt DW, Rice CM. 1989. Yellow fever virus proteins NS2A, NS2B, and NS4B: identification and partial N-terminal amino acid sequence analysis. Virology 169:100-109.
    • (1989) Virology , vol.169 , pp. 100-109
    • Chambers, T.J.1    McCourt, D.W.2    Rice, C.M.3
  • 23
    • 0028849770 scopus 로고
    • Evidence that flavivirus NS1-NS2A cleavage is mediated by a membrane-bound host protease in the endoplasmic reticulum
    • Falgout B, Markoff L. 1995. Evidence that flavivirus NS1-NS2A cleavage is mediated by a membrane-bound host protease in the endoplasmic reticulum. J. Virol. 69:7232-7243.
    • (1995) J. Virol. , vol.69 , pp. 7232-7243
    • Falgout, B.1    Markoff, L.2
  • 25
    • 7644234588 scopus 로고    scopus 로고
    • Analysis of adaptive mutations in Kunjin virus replicon RNA reveals a novel role for the flavivirus nonstructural protein NS2A in inhibition of beta interferon promoter-driven transcription
    • Liu WJ, Chen HB, Wang XJ, Huang H, Khromykh AA. 2004. Analysis of adaptive mutations in Kunjin virus replicon RNA reveals a novel role for the flavivirus nonstructural protein NS2A in inhibition of beta interferon promoter-driven transcription. J. Virol. 78:12225-12235.
    • (2004) J. Virol. , vol.78 , pp. 12225-12235
    • Liu, W.J.1    Chen, H.B.2    Wang, X.J.3    Huang, H.4    Khromykh, A.A.5
  • 26
    • 33144482922 scopus 로고    scopus 로고
    • A single amino acid substitution in the West Nile virus nonstructural protein NS2A disables its ability to inhibit alpha/beta interferon induction and attenuates virus virulence in mice
    • Liu WJ, Wang XJ, Clark DC, Lobigs M, Hall RA, Khromykh AA. 2006. A single amino acid substitution in the West Nile virus nonstructural protein NS2A disables its ability to inhibit alpha/beta interferon induction and attenuates virus virulence in mice. J. Virol. 80:2396-2404.
    • (2006) J. Virol. , vol.80 , pp. 2396-2404
    • Liu, W.J.1    Wang, X.J.2    Clark, D.C.3    Lobigs, M.4    Hall, R.A.5    Khromykh, A.A.6
  • 27
    • 84869015272 scopus 로고    scopus 로고
    • Blocking double-stranded RNA-activated protein kinase PKR by Japanese encephalitis virus nonstructural protein 2A
    • Tu YC, Yu CY, Liang JJ, Lin E, Liao CL, Lin YL. 2012. Blocking double-stranded RNA-activated protein kinase PKR by Japanese encephalitis virus nonstructural protein 2A. J. Virol. 86:10347-10358.
    • (2012) J. Virol. , vol.86 , pp. 10347-10358
    • Tu, Y.C.1    Yu, C.Y.2    Liang, J.J.3    Lin, E.4    Liao, C.L.5    Lin, Y.L.6
  • 31
    • 79957470943 scopus 로고    scopus 로고
    • Development and characterization of a stable luciferase dengue virus for high-throughput screening
    • Zou G, Xu HY, Qing M, Wang QY, Shi PY. 2011. Development and characterization of a stable luciferase dengue virus for high-throughput screening. Antiviral Res. 91:11-19.
    • (2011) Antiviral Res. , vol.91 , pp. 11-19
    • Zou, G.1    Xu, H.Y.2    Qing, M.3    Wang, Q.Y.4    Shi, P.Y.5
  • 32
    • 0031930410 scopus 로고    scopus 로고
    • Identification of a major determinant of mouse neurovirulence of dengue virus type 2 using stably cloned genomic-length cDNA
    • Gualano RC, Pryor MJ, Cauchi MR, Wright PJ, Davidson AD. 1998. Identification of a major determinant of mouse neurovirulence of dengue virus type 2 using stably cloned genomic-length cDNA. J. Gen. Virol. 79:437-446.
    • (1998) J. Gen. Virol. , vol.79 , pp. 437-446
    • Gualano, R.C.1    Pryor, M.J.2    Cauchi, M.R.3    Wright, P.J.4    Davidson, A.D.5
  • 33
    • 34250663574 scopus 로고    scopus 로고
    • The fluorescence protease protection (FPP) assay to determine protein localization and membrane topology
    • Lorenz H, Hailey DW, Wunder C, Lippincott-Schwartz J. 2006. The fluorescence protease protection (FPP) assay to determine protein localization and membrane topology. Nat. Protoc. 1:276-279.
    • (2006) Nat. Protoc. , vol.1 , pp. 276-279
    • Lorenz, H.1    Hailey, D.W.2    Wunder, C.3    Lippincott-Schwartz, J.4
  • 34
    • 79953207656 scopus 로고    scopus 로고
    • Membrane topology of NAADP-sensitive two-pore channels and their regulation by N-linked glycosylation
    • Hooper R, Churamani D, Brailoiu E, Taylor CW, Patel S. 2011. Membrane topology of NAADP-sensitive two-pore channels and their regulation by N-linked glycosylation. J. Biol. Chem. 286:9141-9149.
    • (2011) J. Biol. Chem. , vol.286 , pp. 9141-9149
    • Hooper, R.1    Churamani, D.2    Brailoiu, E.3    Taylor, C.W.4    Patel, S.5
  • 36
    • 84865305540 scopus 로고    scopus 로고
    • A novel coding-region RNA element modulates infectious dengue virus particle production in both mammalian and mosquito cells and regulates viral replication in Aedes aegypti mosquitoes
    • Groat-Carmona AM, Orozco S, Friebe P, Payne A, Kramer L, Harris E. 2012. A novel coding-region RNA element modulates infectious dengue virus particle production in both mammalian and mosquito cells and regulates viral replication in Aedes aegypti mosquitoes. Virology 432:511-526.
    • (2012) Virology , vol.432 , pp. 511-526
    • Groat-Carmona, A.M.1    Orozco, S.2    Friebe, P.3    Payne, A.4    Kramer, L.5    Harris, E.6
  • 37
    • 79958200530 scopus 로고    scopus 로고
    • Solution structure of a human minimembrane protein Ost4, a subunit of the oligosaccharyltransferase complex
    • Gayen S, Kang C. 2011. Solution structure of a human minimembrane protein Ost4, a subunit of the oligosaccharyltransferase complex. Biochem. Biophys. Res. Commun. 409:572-576.
    • (2011) Biochem. Biophys. Res. Commun. , vol.409 , pp. 572-576
    • Gayen, S.1    Kang, C.2
  • 38
    • 0003919736 scopus 로고
    • NMRof proteins and nucleic acids
    • Wiley, New York, NY
    • Wuthrich K. 1986.NMRof proteins and nucleic acids. Wiley, New York, NY.
    • (1986)
    • Wuthrich, K.1
  • 39
    • 4644340524 scopus 로고    scopus 로고
    • Automated NMR structure calculation with CYANA
    • Guntert P. 2004. Automated NMR structure calculation with CYANA. Methods Mol. Biol. 278:353-378.
    • (2004) Methods Mol. Biol. , vol.278 , pp. 353-378
    • Guntert, P.1
  • 40
    • 79954633991 scopus 로고    scopus 로고
    • N-linked glycosylation of dengue virus NS1 protein modulates secretion, cell-surface expression, hexamer stability, and interactions with human complement
    • Somnuke P, Hauhart RE, Atkinson JP, Diamond MS, Avirutnan P. 2011. N-linked glycosylation of dengue virus NS1 protein modulates secretion, cell-surface expression, hexamer stability, and interactions with human complement. Virology 413:253-264.
    • (2011) Virology , vol.413 , pp. 253-264
    • Somnuke, P.1    Hauhart, R.E.2    Atkinson, J.P.3    Diamond, M.S.4    Avirutnan, P.5
  • 41
    • 0025171037 scopus 로고
    • Cleavage of dengue virus NS1-NS2A requires an octapeptide sequence at the C terminus of NS1
    • Hori H, Lai CJ. 1990. Cleavage of dengue virus NS1-NS2A requires an octapeptide sequence at the C terminus of NS1. J. Virol. 64:4573-4577.
    • (1990) J. Virol. , vol.64 , pp. 4573-4577
    • Hori, H.1    Lai, C.J.2
  • 42
    • 79960977911 scopus 로고    scopus 로고
    • Solution NMR study of integral membrane proteins
    • Kang C, Li Q. 2011. Solution NMR study of integral membrane proteins. Curr. Opin. Chem. Biol. 15:560-569.
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 560-569
    • Kang, C.1    Li, Q.2
  • 43
    • 32944464105 scopus 로고    scopus 로고
    • An evaluation of chemical shift indexbased secondary structure determination in proteins: influence of random coil chemical shifts
    • Mielke SP, Krishnan VV. 2004. An evaluation of chemical shift indexbased secondary structure determination in proteins: influence of random coil chemical shifts. J. Biomol. NMR 30:143-153.
    • (2004) J. Biomol. NMR , vol.30 , pp. 143-153
    • Mielke, S.P.1    Krishnan, V.V.2
  • 44
    • 0028206422 scopus 로고
    • Mutagenesis of the yellow fever virus NS2A/2B cleavage site: effects on proteolytic processing, viral replication, and evidence for alternative processing of the NS2A protein
    • Nestorowicz A, Chambers TJ, Rice CM. 1994. Mutagenesis of the yellow fever virus NS2A/2B cleavage site: effects on proteolytic processing, viral replication, and evidence for alternative processing of the NS2A protein. Virology 199:114-123.
    • (1994) Virology , vol.199 , pp. 114-123
    • Nestorowicz, A.1    Chambers, T.J.2    Rice, C.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.