메뉴 건너뛰기




Volumn 90, Issue 16, 2016, Pages 7248-7256

Mutagenesis of S-adenosyl-L-methionine-binding residues in coronavirus nsp14 N7-methyltransferase demonstrates differing requirements for genome translation and resistance to innate immunity

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; BETA INTERFERON; METHYLTRANSFERASE; MUTAGENIC AGENT; N7 METHYLTRANSFERASE; NSP14 PROTEIN; S ADENOSYLMETHIONINE; UNCLASSIFIED DRUG; VIRUS PROTEIN; ANTIVIRUS AGENT; NONSTRUCTURAL PROTEIN, CORONAVIRUS; VIRAL PROTEIN; VIRUS RNA;

EID: 84982214178     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00542-16     Document Type: Article
Times cited : (52)

References (40)
  • 1
    • 0017224213 scopus 로고
    • Capping of eucaryotic mRNAs
    • Shatkin AJ. 1976. Capping of eucaryotic mRNAs. Cell 9:645-653. http: //dx.doi.org/10.1016/0092-8674(76)90128-8.
    • (1976) Cell , vol.9 , pp. 645-653
    • Shatkin, A.J.1
  • 2
    • 0018620777 scopus 로고
    • Transcription units formRNAproduction in eukaryotic cells and their DNA viruses
    • Darnell JE. 1979. Transcription units formRNAproduction in eukaryotic cells and their DNA viruses. Prog Nucleic Acid Res Mol Biol 22:327-353. http://dx.doi.org/10.1016/S0079-6603(08)60803-X.
    • (1979) Prog Nucleic Acid Res Mol Biol , vol.22 , pp. 327-353
    • Darnell, J.E.1
  • 3
    • 0034567861 scopus 로고    scopus 로고
    • Viral and cellular mRNA capping: past and prospects
    • Furuichi Y, Shatkin AJ. 2000. Viral and cellular mRNA capping: past and prospects. Adv Virus Res 55:135-184. http://dx.doi.org/10.1016/S0065 -3527(00)55003-9.
    • (2000) Adv Virus Res , vol.55 , pp. 135-184
    • Furuichi, Y.1    Shatkin, A.J.2
  • 4
    • 0030728936 scopus 로고    scopus 로고
    • Cocrystal structure of the messenger RNA 5= cap-binding protein (eIF4E) bound to 7-methyl-GDP
    • Marcotrigiano J, Gingras A-C, Sonenberg N, Burley SK. 1997. Cocrystal structure of the messenger RNA 5= cap-binding protein (eIF4E) bound to 7-methyl-GDP. Cell 89:951-961. http://dx.doi.org/10.1016 /S0092-8674(00)80280-9.
    • (1997) Cell , vol.89 , pp. 951-961
    • Marcotrigiano, J.1    Gingras, A.-C.2    Sonenberg, N.3    Burley, S.K.4
  • 6
    • 0017621466 scopus 로고
    • The 5=-termini of heterogeneous nuclear RNA: a comparison among molecules of different sizes and ages
    • Schibler U, Perry RP. 1977. The 5=-termini of heterogeneous nuclear RNA: a comparison among molecules of different sizes and ages. Nucleic Acids Res 4:4133-4150. http://dx.doi.org/10.1093/nar/4.12.4133.
    • (1977) Nucleic Acids Res , vol.4 , pp. 4133-4150
    • Schibler, U.1    Perry, R.P.2
  • 7
    • 0016770156 scopus 로고
    • Methylated nucleotides block 5= terminus of HeLa cell messenger RNA
    • Wei CM, Gershowitz A, Moss B. 1975. Methylated nucleotides block 5= terminus of HeLa cell messenger RNA. Cell 4:379-386. http://dx.doi.org /10.1016/0092-8674(75)90158-0.
    • (1975) Cell , vol.4 , pp. 379-386
    • Wei, C.M.1    Gershowitz, A.2    Moss, B.3
  • 9
    • 83855162132 scopus 로고    scopus 로고
    • Conventional and unconventional mechanisms for capping viral mRNA
    • Decroly E, Ferron F, Lescar J, Canard B. 2012. Conventional and unconventional mechanisms for capping viral mRNA. Nat Rev Microbiol 10:51-65. http://dx.doi.org/10.1038/nrmicro2675.
    • (2012) Nat Rev Microbiol , vol.10 , pp. 51-65
    • Decroly, E.1    Ferron, F.2    Lescar, J.3    Canard, B.4
  • 10
    • 0019503319 scopus 로고
    • Comparative analysis of RNA genomes of mouse hepatitis viruses
    • Lai MM, Stohlman SA. 1981. Comparative analysis of RNA genomes of mouse hepatitis viruses. J Virol 38:661-670.
    • (1981) J Virol , vol.38 , pp. 661-670
    • Lai, M.M.1    Stohlman, S.A.2
  • 11
    • 0020024485 scopus 로고
    • Further characterization of mRNAs of mouse hepatitis virus: presence of common 5-=end nucleotides
    • Lai MM, Patton CD, Stohlman SA. 1982. Further characterization of mRNAs of mouse hepatitis virus: presence of common 5-=end nucleotides. J Virol 41:557-565.
    • (1982) J Virol , vol.41 , pp. 557-565
    • Lai, M.M.1    Patton, C.D.2    Stohlman, S.A.3
  • 12
    • 33746317830 scopus 로고    scopus 로고
    • The molecular biology of coronaviruses
    • Masters PS. 2006. The molecular biology of coronaviruses. Adv Virus Res 66:193-292. http://dx.doi.org/10.1016/S0065-3527(06)66005-3.
    • (2006) Adv Virus Res , vol.66 , pp. 193-292
    • Masters, P.S.1
  • 14
    • 2442679084 scopus 로고    scopus 로고
    • Multiple enzymatic activities associated with severe acute respiratory syndrome coronavirus helicase
    • Ivanov KA, Thiel V, Dobbe JC, van der Meer Y, Snijder EJ, Ziebuhr J. 2004. Multiple enzymatic activities associated with severe acute respiratory syndrome coronavirus helicase. J Virol 78:5619-5632. http://dx.doi .org/10.1128/JVI.78.11.5619-5632.2004.
    • (2004) J Virol , vol.78 , pp. 5619-5632
    • Ivanov, K.A.1    Thiel, V.2    Dobbe, J.C.3    van der Meer, Y.4    Snijder, E.J.5    Ziebuhr, J.6
  • 17
    • 0038681984 scopus 로고    scopus 로고
    • mRNA cap-1 methyltransferase in the SARS genome
    • von Grotthuss M, Wyrwicz LS, Rychlewski L. 2003. mRNA cap-1 methyltransferase in the SARS genome. Cell 113:701-702. http://dx.doi.org/10 .1016/S0092-8674(03)00424-0.
    • (2003) Cell , vol.113 , pp. 701-702
    • von Grotthuss, M.1    Wyrwicz, L.S.2    Rychlewski, L.3
  • 18
    • 47749138964 scopus 로고    scopus 로고
    • Coronavirus nonstructural protein 16 is a cap-0 binding enzyme possessing (nucleoside-2=O)-methyltransferase activity
    • Decroly E, Imbert I, Coutard B, Bouvet M, Selisko B, Alvarez K, Gorbalenya AE, Snijder EJ, Canard B. 2008. Coronavirus nonstructural protein 16 is a cap-0 binding enzyme possessing (nucleoside-2=O)-methyltransferase activity. J Virol 82:8071-8084. http://dx.doi.org/10 .1128/JVI.00407-08.
    • (2008) J Virol , vol.82 , pp. 8071-8084
    • Decroly, E.1    Imbert, I.2    Coutard, B.3    Bouvet, M.4    Selisko, B.5    Alvarez, K.6    Gorbalenya, A.E.7    Snijder, E.J.8    Canard, B.9
  • 20
    • 80055066817 scopus 로고    scopus 로고
    • Biochemical and structural insights into the mechanisms of SARS coronavirus RNA ribose 2=-Omethylation 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. 2011. Biochemical and structural insights into the mechanisms of SARS coronavirus RNA ribose 2=-Omethylation by nsp16/nsp10 protein complex. PLoS Pathog 7:e1002294. http://dx.doi.org/10.1371/journal.ppat.1002294.
    • (2011) PLoS Pathog , vol.7
    • 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
  • 23
    • 84896981937 scopus 로고    scopus 로고
    • Attenuation and restoration of severe acute respiratory syndrome coronavirus mutant lacking 2=-Omethyltransferase activity
    • Menachery VD, Yount BL, Jr, Josset L, Gralinski LE, Scobey T, Agnihothram S, Katze MG, Baric RS. 2014. Attenuation and restoration of severe acute respiratory syndrome coronavirus mutant lacking 2=-Omethyltransferase activity. J Virol 88:4251-4264. http://dx.doi.org/10 .1128/JVI.03571-13.
    • (2014) J Virol , vol.88 , pp. 4251-4264
    • Menachery, V.D.1    Yount, B.L.2    Josset, L.3    Gralinski, L.E.4    Scobey, T.5    Agnihothram, S.6    Katze, M.G.7    Baric, R.S.8
  • 25
    • 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. 2009. Functional screen reveals SARS coronavirus nonstructural protein nsp14 as a novel cap N7 methyltransferase. Proc Natl Acad Sci U S A 106:3484-3489. http://dx.doi.org/10.1073/pnas.0808790106.
    • (2009) Proc Natl Acad Sci U S A , 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
  • 26
    • 84878197216 scopus 로고    scopus 로고
    • Structure-function analysis of severe acute respiratory syndrome coronavirus RNA cap guanine-N7-methyltransferase
    • Chen Y, Tao J, Sun Y, Wu A, Su C, Gao G, Cai H, Qiu S, Wu Y, Ahola T, Guo D. 2013. Structure-function analysis of severe acute respiratory syndrome coronavirus RNA cap guanine-N7-methyltransferase. J Virol 87:6296-6305. http://dx.doi.org/10.1128/JVI.00061-13.
    • (2013) J Virol , vol.87 , pp. 6296-6305
    • Chen, Y.1    Tao, J.2    Sun, Y.3    Wu, A.4    Su, C.5    Gao, G.6    Cai, H.7    Qiu, S.8    Wu, Y.9    Ahola, T.10    Guo, D.11
  • 27
    • 0030023675 scopus 로고    scopus 로고
    • Molecular anatomy of mouse hepatitis virus persistence: coevolution of increased host cell resistance and virus virulence
    • Chen W, Baric RS. 1996. Molecular anatomy of mouse hepatitis virus persistence: coevolution of increased host cell resistance and virus virulence. J Virol 70:3947-3960.
    • (1996) J Virol , vol.70 , pp. 3947-3960
    • Chen, W.1    Baric, R.S.2
  • 28
    • 0036838992 scopus 로고    scopus 로고
    • Systematic assembly of a full-length infectious cDNA of mouse hepatitis virus strain A59
    • Yount B, Denison MR, Weiss SR, Baric RS. 2002. Systematic assembly of a full-length infectious cDNA of mouse hepatitis virus strain A59. J Virol 76:11065-11078. http://dx.doi.org/10.1128/JVI.76.21.11065-11078.2002.
    • (2002) J Virol , vol.76 , pp. 11065-11078
    • Yount, B.1    Denison, M.R.2    Weiss, S.R.3    Baric, R.S.4
  • 29
    • 84899070072 scopus 로고    scopus 로고
    • Coronavirus replicase-reporter fusions provide quantitative analysis of replication and replication complex formation
    • Freeman MC, Graham RL, Lu X, Peek CT, Denison MR. 2014. Coronavirus replicase-reporter fusions provide quantitative analysis of replication and replication complex formation. J Virol 88:5319-5327. http://dx .doi.org/10.1128/JVI.00021-14.
    • (2014) J Virol , vol.88 , pp. 5319-5327
    • Freeman, M.C.1    Graham, R.L.2    Lu, X.3    Peek, C.T.4    Denison, M.R.5
  • 30
    • 36048969246 scopus 로고    scopus 로고
    • High fidelity of murine hepatitis virus replication is decreased in nsp14 exoribonuclease mutants
    • Eckerle LD, Lu X, Sperry SM, Choi L, Denison MR. 2007. High fidelity of murine hepatitis virus replication is decreased in nsp14 exoribonuclease mutants. J Virol 81:12135-12144. http://dx.doi.org/10 .1128/JVI.01296-07.
    • (2007) J Virol , vol.81 , pp. 12135-12144
    • Eckerle, L.D.1    Lu, X.2    Sperry, S.M.3    Choi, L.4    Denison, M.R.5
  • 31
    • 84883438898 scopus 로고    scopus 로고
    • Coronaviruses lacking exoribonuclease activity are susceptible to lethal mutagenesis: evidence for proofreading and potential therapeutics
    • Smith EC, Blanc H, Vignuzzi M, Denison MR. 2013. Coronaviruses lacking exoribonuclease activity are susceptible to lethal mutagenesis: evidence for proofreading and potential therapeutics. PLoS Pathog 9:e1003565. http://dx.doi.org/10.1371/journal.ppat.1003565.
    • (2013) PLoS Pathog , vol.9
    • Smith, E.C.1    Blanc, H.2    Vignuzzi, M.3    Denison, M.R.4
  • 32
    • 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. 2015. Structural basis and functional analysis of the SARS coronavirus nsp14-nsp10 complex. Proc Natl Acad Sci U S A 112:9436-9441. http://dx.doi.org/10.1073/pnas.1508686112.
    • (2015) Proc Natl Acad Sci U S A , 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
  • 34
    • 84929603486 scopus 로고    scopus 로고
    • Mutations in coronavirus nonstructural protein 10 decrease virus replication fidelity
    • Smith EC, Case JB, Blanc H, Isakov O, Shomron N, Vignuzzi M, Denison MR. 2015. Mutations in coronavirus nonstructural protein 10 decrease virus replication fidelity. J Virol 89:6418-6426. http://dx.doi.org /10.1128/JVI.00110-15.
    • (2015) J Virol , vol.89 , pp. 6418-6426
    • Smith, E.C.1    Case, J.B.2    Blanc, H.3    Isakov, O.4    Shomron, N.5    Vignuzzi, M.6    Denison, M.R.7
  • 35
    • 34250836810 scopus 로고    scopus 로고
    • Inhibition of the alpha/beta interferon response by mouse hepatitis virus at multiple levels
    • Roth-Cross JK, Martínez-Sobrido L, Scott EP, García-Sastre A, Weiss SR. 2007. Inhibition of the alpha/beta interferon response by mouse hepatitis virus at multiple levels. J Virol 81:7189-7199. http://dx.doi.org/10 .1128/JVI.00013-07.
    • (2007) J Virol , vol.81 , pp. 7189-7199
    • Roth-Cross, J.K.1    Martínez-Sobrido, L.2    Scott, E.P.3    García-Sastre, A.4    Weiss, S.R.5
  • 36
    • 0036715591 scopus 로고    scopus 로고
    • Viruses and interferon: a fight for supremacy
    • Katze MG, He Y, Gale M. 2002. Viruses and interferon: a fight for supremacy. Nat Rev Immunol 2:675-687. http://dx.doi.org/10.1038/nri888.
    • (2002) Nat Rev Immunol , vol.2 , pp. 675-687
    • Katze, M.G.1    He, Y.2    Gale, M.3
  • 37
    • 5044229348 scopus 로고    scopus 로고
    • Molecular mechanisms of translational control
    • Gebauer FAT, Hentze MW. 2004. Molecular mechanisms of translational control. Nat Rev Mol Cell Biol 5:827-835.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 827-835
    • Gebauer, F.A.T.1    Hentze, M.W.2
  • 38
    • 27144504142 scopus 로고    scopus 로고
    • Amino acid residues within conserved domain VI of the vesicular stomatitis virus large polymerase protein essential for mRNA cap methyltransferase activity
    • Li J, Fontaine-Rodriguez EC, Whelan SPJ. 2005. Amino acid residues within conserved domain VI of the vesicular stomatitis virus large polymerase protein essential for mRNA cap methyltransferase activity. J Virol 79:13373-13384. http://dx.doi.org/10.1128/JVI.79.21.13373-13384.2005.
    • (2005) J Virol , vol.79 , pp. 13373-13384
    • Li, J.1    Fontaine-Rodriguez, E.C.2    Whelan, S.P.J.3
  • 39
    • 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
  • 40
    • 84871484827 scopus 로고    scopus 로고
    • The broad-spectrum antiviral functions of IFIT and IFITM proteins
    • Diamond MS, Farzan M. 2013. The broad-spectrum antiviral functions of IFIT and IFITM proteins. Nat Rev Immunol 13:46-57. http://dx.doi.org/10.1038/nri3344.
    • (2013) Nat Rev Immunol , vol.13 , pp. 46-57
    • Diamond, M.S.1    Farzan, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.