메뉴 건너뛰기




Volumn 144, Issue , 2017, Pages 330-339

Toward the identification of viral cap-methyltransferase inhibitors by fluorescence screening assay

Author keywords

Antiviral; Coronavirus; Flavivirus; HTRF; Inhibitor; Methyltransferase

Indexed keywords

ANTIVIRUS AGENT; GUANINE; METHYLTRANSFERASE INHIBITOR; NSP14 PROTEIN; SINEFUNGIN; UNCLASSIFIED DRUG; VIRAL PROTEIN; VIRUS RNA; EXORIBONUCLEASE; METHYLTRANSFERASE; NSP14 PROTEIN, SARS CORONAVIRUS;

EID: 85021847233     PISSN: 01663542     EISSN: 18729096     Source Type: Journal    
DOI: 10.1016/j.antiviral.2017.06.021     Document Type: Article
Times cited : (38)

References (37)
  • 1
    • 85013891656 scopus 로고    scopus 로고
    • Binding of the methyl donor S-Adenosyl-L-Methionine to Middle East respiratory syndrome coronavirus 2’-O- methyltransferase nsp16 promotes recruitment of the allosteric activator nsp10
    • Aouadi, W., Blanjoie, A., Vasseur, J., Canard, B., Decroly, E., Binding of the methyl donor S-Adenosyl-L-Methionine to Middle East respiratory syndrome coronavirus 2’-O- methyltransferase nsp16 promotes recruitment of the allosteric activator nsp10. J. Virol. 91 (2017), 1–18.
    • (2017) J. Virol. , vol.91 , pp. 1-18
    • Aouadi, W.1    Blanjoie, A.2    Vasseur, J.3    Canard, B.4    Decroly, E.5
  • 3
    • 84862203582 scopus 로고    scopus 로고
    • RNA 3 '-end mismatch excision by the severe acute respiratory syndrome coronavirus nonstructural protein nsp10/nsp14 exoribonuclease complex
    • Bouvet, M., Imbert, I., Subissi, L., Gluais, L., Canard, B., Decroly, E., RNA 3 '-end mismatch excision by the severe acute respiratory syndrome coronavirus nonstructural protein nsp10/nsp14 exoribonuclease complex. PNAS 109 (2012), 9372–9377, 10.1073/pnas.1201130109/-/DCSupplemental www.pnas.org/cgi/doi/10.1073/pnas.1201130109.
    • (2012) PNAS , vol.109 , pp. 9372-9377
    • Bouvet, M.1    Imbert, I.2    Subissi, L.3    Gluais, L.4    Canard, B.5    Decroly, E.6
  • 5
    • 84982214178 scopus 로고    scopus 로고
    • Mutagenesis of S-Adenosyl-L-Methionine-Binding residues in coronavirus nsp14 N7-methyltransferase demonstrates differing requirements for genome translation and resistance to innate immunity
    • Case, J.B., Ashbrook, A.W., Dermody, T.S., Denison, M.R., Mutagenesis of S-Adenosyl-L-Methionine-Binding residues in coronavirus nsp14 N7-methyltransferase demonstrates differing requirements for genome translation and resistance to innate immunity. J. Virol. 90 (2016), 7248–7256, 10.1128/JVI.00542-16.
    • (2016) J. Virol. , vol.90 , pp. 7248-7256
    • Case, J.B.1    Ashbrook, A.W.2    Dermody, T.S.3    Denison, M.R.4
  • 6
    • 62549159638 scopus 로고    scopus 로고
    • Functional screen reveals SARS coronavirus nonstructural protein nsp14 as a novel cap N7 methyltransferase
    • Chen, Y., Cai, H., Pan, J., Xiang, N., Tien, P., Ahola, T., Guo, D., Functional screen reveals SARS coronavirus nonstructural protein nsp14 as a novel cap N7 methyltransferase. PNAS 106 (2009), 3484–3489, 10.1073/pnas.0808790106.
    • (2009) PNAS , vol.106 , pp. 3484-3489
    • Chen, Y.1    Cai, H.2    Pan, J.3    Xiang, N.4    Tien, P.5    Ahola, T.6    Guo, D.7
  • 7
    • 80055066817 scopus 로고    scopus 로고
    • Biochemical and structural insights into the mechanisms of SARS coronavirus RNA ribose 2′-O-methylation by nsp16/nsp10 protein complex
    • Chen, Y., Su, C., Ke, M., Jin, X., Xu, L., Zhang, Z., Wu, A., Sun, Y., Yang, Z., Tien, P., Ahola, T., Liang, Y., Liu, X., Guo, D., Biochemical and structural insights into the mechanisms of SARS coronavirus RNA ribose 2′-O-methylation by nsp16/nsp10 protein complex. PLoS Pathog., 7, 2011, e1002294, 10.1371/journal.ppat.1002294.
    • (2011) PLoS Pathog. , vol.7 , pp. e1002294
    • Chen, Y.1    Su, C.2    Ke, M.3    Jin, X.4    Xu, L.5    Zhang, Z.6    Wu, A.7    Sun, Y.8    Yang, Z.9    Tien, P.10    Ahola, T.11    Liang, Y.12    Liu, X.13    Guo, D.14
  • 9
  • 11
    • 83855162132 scopus 로고    scopus 로고
    • Conventional and unconventional mechanisms for capping viral mRNA
    • Decroly, E., Ferron, F., Lescar, J., Canard, B., Conventional and unconventional mechanisms for capping viral mRNA. Nat. Rev. Microbiol. 10 (2012), 51–65, 10.1038/nrmicro2675.
    • (2012) Nat. Rev. Microbiol. , vol.10 , pp. 51-65
    • Decroly, E.1    Ferron, F.2    Lescar, J.3    Canard, B.4
  • 12
    • 77952504334 scopus 로고    scopus 로고
    • HTRF: a technology tailored for drug discovery - a review of theoretical aspects and recent applications
    • Degorce, F., Card, A., Soh, S., Trinquet, E., Knapik, G.P., Xie, B., HTRF: a technology tailored for drug discovery - a review of theoretical aspects and recent applications. Curr. Chem. Genomics 3 (2009), 22–32, 10.2174/1875397300903010022.
    • (2009) Curr. Chem. Genomics , vol.3 , pp. 22-32
    • Degorce, F.1    Card, A.2    Soh, S.3    Trinquet, E.4    Knapik, G.P.5    Xie, B.6
  • 13
    • 84908309281 scopus 로고    scopus 로고
    • IFIT1: a dual sensor and effector molecule that detects non-2’-O methylated viral RNA and inhibits its translation
    • Diamond, M.S., IFIT1: a dual sensor and effector molecule that detects non-2’-O methylated viral RNA and inhibits its translation. Cytokine Growth Factor Rev. 25 (2014), 543–550, 10.1016/j.cytogfr.2014.05.002.
    • (2014) Cytokine Growth Factor Rev. , vol.25 , pp. 543-550
    • Diamond, M.S.1
  • 14
    • 77957764872 scopus 로고    scopus 로고
    • Structural and functional analyses of a conserved hydrophobic pocket of flavivirus methyltransferase
    • Dong, H., Liu, L., Zou, G., Zhao, Y., Li, Z., Lim, S.P., Shi, P.Y., Li, H., Structural and functional analyses of a conserved hydrophobic pocket of flavivirus methyltransferase. J. Biol. Chem. 285 (2010), 32586–32595, 10.1074/jbc.M110.129197.
    • (2010) J. Biol. Chem. , vol.285 , pp. 32586-32595
    • Dong, H.1    Liu, L.2    Zou, G.3    Zhao, Y.4    Li, Z.5    Lim, S.P.6    Shi, P.Y.7    Li, H.8
  • 15
    • 84864912887 scopus 로고    scopus 로고
    • The viral RNA capping machinery as a target for antiviral drugs
    • Ferron, F., Decroly, E., Selisko, B., Canard, B., The viral RNA capping machinery as a target for antiviral drugs. Antivir. Res. 96 (2012), 21–31, 10.1016/j.antiviral.2012.07.007.
    • (2012) Antivir. Res. , vol.96 , pp. 21-31
    • Ferron, F.1    Decroly, E.2    Selisko, B.3    Canard, B.4
  • 16
    • 3142689813 scopus 로고    scopus 로고
    • Human coronavirus 229E nonstructural protein 13: characterization of duplex-unwinding, nucleoside triphosphatase, and RNA 5’-triphosphatase activities
    • Ivanov, K.A., Ziebuhr, J., Human coronavirus 229E nonstructural protein 13: characterization of duplex-unwinding, nucleoside triphosphatase, and RNA 5’-triphosphatase activities. J. Virol. 78 (2004), 7833–7838, 10.1128/JVI.78.14.7833-7838.2004.
    • (2004) J. Virol. , vol.78 , pp. 7833-7838
    • Ivanov, K.A.1    Ziebuhr, J.2
  • 17
    • 11144348687 scopus 로고    scopus 로고
    • Angiotensin-converting enzyme 2: a functional receptor for SARS coronavirus
    • Kuhn, J.H., Li, W., Choe, H., Farzan, M., Angiotensin-converting enzyme 2: a functional receptor for SARS coronavirus. Cell. Mol. Life Sci. 61 (2004), 2738–2743, 10.1007/s00018-004-4242-5.
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 2738-2743
    • Kuhn, J.H.1    Li, W.2    Choe, H.3    Farzan, M.4
  • 20
    • 84938086703 scopus 로고    scopus 로고
    • Structural basis and functional analysis of the SARS coronavirus nsp14-nsp10 complex
    • Ma, Y., Wu, L., Shaw, N., Gao, Y., Wang, J., Sun, Y., Lou, Z., Yan, L., Zhang, R., Rao, Z., Structural basis and functional analysis of the SARS coronavirus nsp14-nsp10 complex. PNAS 112 (2015), 9436–9441, 10.1073/pnas.1508686112.
    • (2015) PNAS , vol.112 , pp. 9436-9441
    • Ma, Y.1    Wu, L.2    Shaw, N.3    Gao, Y.4    Wang, J.5    Sun, Y.6    Lou, Z.7    Yan, L.8    Zhang, R.9    Rao, Z.10
  • 21
    • 84896981937 scopus 로고    scopus 로고
    • Attenuation and restoration of severe acute respiratory syndrome coronavirus mutant lacking 2′-O-methyltransferase activity
    • Menachery, V.D. Jr., B.L.Y., Josset, L., Gralinski, L.E., Scobey, T., Agnihothram, S., Katze, M.G., Baric, R.S., Attenuation and restoration of severe acute respiratory syndrome coronavirus mutant lacking 2′-O-methyltransferase activity. J. Virol. 88 (2014), 4251–4264, 10.1128/JVI.03571-13.
    • (2014) J. Virol. , vol.88 , pp. 4251-4264
    • Menachery, V.D.1    B.L.Y.2    Josset, L.3    Gralinski, L.E.4    Scobey, T.5    Agnihothram, S.6    Katze, M.G.7    Baric, R.S.8
  • 23
    • 33645518839 scopus 로고    scopus 로고
    • Discovery of an RNA virus 3’->5’ exoribonuclease that is critically involved in coronavirus RNA synthesis
    • Minskaia, E., Hertzig, T., Gorbalenya, A.E., Campanacci, V., Cambillau, C., Canard, B., Ziebuhr, J., Discovery of an RNA virus 3’->5’ exoribonuclease that is critically involved in coronavirus RNA synthesis. PNAS 103 (2006), 5108–5113, 10.1073/pnas.0508200103.
    • (2006) PNAS , vol.103 , pp. 5108-5113
    • Minskaia, E.1    Hertzig, T.2    Gorbalenya, A.E.3    Campanacci, V.4    Cambillau, C.5    Canard, B.6    Ziebuhr, J.7
  • 24
    • 53249097514 scopus 로고    scopus 로고
    • Genome-wide analysis of protein-protein interactions and involvement of viral proteins in SARS-CoV replication
    • Pan, J., Peng, X., Gao, Y., Li, Z., Lu, X., Chen, Y., Ishaq, M., Liu, D., DeDiego, M.L., Enjuanes, L., Guo, D., Genome-wide analysis of protein-protein interactions and involvement of viral proteins in SARS-CoV replication. PLoS ONE, 3, 2008, 10.1371/journal.pone.0003299.
    • (2008) PLoS ONE , vol.3
    • Pan, J.1    Peng, X.2    Gao, Y.3    Li, Z.4    Lu, X.5    Chen, Y.6    Ishaq, M.7    Liu, D.8    DeDiego, M.L.9    Enjuanes, L.10    Guo, D.11
  • 25
    • 34047219728 scopus 로고    scopus 로고
    • High-yield production of short GpppA- and 7MeGpppA-capped RNAs and HPLC-monitoring of methyltransfer reactions at the guanine-N7 and adenosine-2’O positions
    • Peyrane, F., Selisko, B., Decroly, E., Vasseur, J.J., Benarroch, D., Canard, B., Alvarez, K., High-yield production of short GpppA- and 7MeGpppA-capped RNAs and HPLC-monitoring of methyltransfer reactions at the guanine-N7 and adenosine-2’O positions. Nucleic Acids Res., 35, 2007, 10.1093/nar/gkl1119.
    • (2007) Nucleic Acids Res. , vol.35
    • Peyrane, F.1    Selisko, B.2    Decroly, E.3    Vasseur, J.J.4    Benarroch, D.5    Canard, B.6    Alvarez, K.7
  • 29
    • 84994851357 scopus 로고    scopus 로고
    • Chapter three – the nonstructural proteins directing coronavirus RNA synthesis and processing
    • Snijder, E.J., Decroly, E., Ziebuhr, J., Chapter three – the nonstructural proteins directing coronavirus RNA synthesis and processing. Advances in Virus Research, 2016, 59–126, 10.1016/bs.aivir.2016.08.008.
    • (2016) Advances in Virus Research , pp. 59-126
    • Snijder, E.J.1    Decroly, E.2    Ziebuhr, J.3
  • 30
    • 84896721871 scopus 로고    scopus 로고
    • Yeast-based assays for the high-throughput screening of inhibitors of coronavirus RNA cap guanine-N7-methyltransferase
    • Sun, Y., Wang, Z., Tao, J., Wang, Y., Wu, A., Yang, Z., Wang, K., Shi, L., Chen, Y., Guo, D., Yeast-based assays for the high-throughput screening of inhibitors of coronavirus RNA cap guanine-N7-methyltransferase. Antivir. Res. 104 (2014), 156–164, 10.1016/j.antiviral.2014.02.002.
    • (2014) Antivir. Res. , vol.104 , pp. 156-164
    • Sun, Y.1    Wang, Z.2    Tao, J.3    Wang, Y.4    Wu, A.5    Yang, Z.6    Wang, K.7    Shi, L.8    Chen, Y.9    Guo, D.10
  • 32
    • 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
  • 34
    • 84872604349 scopus 로고    scopus 로고
    • Structural basis for dsRNA recognition, filament formation, and antiviral signal activation by MDA5
    • Wu, B., Peisley, A., Richards, C., Yao, H., Zeng, X., Lin, C., Chu, F., Walz, T., Hur, S., Structural basis for dsRNA recognition, filament formation, and antiviral signal activation by MDA5. Cell 152 (2013), 276–289, 10.1016/j.cell.2012.11.048.
    • (2013) Cell , vol.152 , pp. 276-289
    • Wu, B.1    Peisley, A.2    Richards, C.3    Yao, H.4    Zeng, X.5    Lin, C.6    Chu, F.7    Walz, T.8    Hur, S.9
  • 35
    • 84906972010 scopus 로고    scopus 로고
    • Rational design of human metapneumovirus live attenuated vaccine candidates by inhibiting viral mRNA cap methyltransferase
    • Zhang, Y., Wei, Y., Zhang, X., Cai, H., Niewiesk, S., Li, J., Rational design of human metapneumovirus live attenuated vaccine candidates by inhibiting viral mRNA cap methyltransferase. J. Virol. 88 (2014), 11411–11429, 10.1128/jvi.00876-14.
    • (2014) J. Virol. , vol.88 , pp. 11411-11429
    • Zhang, Y.1    Wei, Y.2    Zhang, X.3    Cai, H.4    Niewiesk, S.5    Li, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.