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Volumn 58, Issue 4, 2006, Pages 723-732

Mutations conferring zanamivir resistance in human influenza virus N2 neuraminidases compromise virus fitness and are not stably maintained in vitro

Author keywords

Baculovirus; Drug resistance; Oseltamivir; Reverse genetics

Indexed keywords

4 ACETAMIDO 5 AMINO 3 (1 ETHYLPROPOXY) 1 CYCLOHEXENE 1 CARBOXYLIC ACID; ADENINE; GUANINE; N ACETYLNEURAMINIC ACID DERIVATIVE; OSELTAMIVIR; PERAMIVIR; TYROSINE; VIRUS SIALIDASE; ZANAMIVIR;

EID: 33748702675     PISSN: 03057453     EISSN: 14602091     Source Type: Journal    
DOI: 10.1093/jac/dkl321     Document Type: Article
Times cited : (88)

References (41)
  • 1
    • 0026665418 scopus 로고
    • The structure of the complex between influenza virus neuraminidase and sialic acid, the viral receptor
    • Varghese JN, McKimm-Breschkin JL, Caldwell JB et al. The structure of the complex between influenza virus neuraminidase and sialic acid, the viral receptor. Proteins 1992; 14: 327-32.
    • (1992) Proteins , vol.14 , pp. 327-332
    • Varghese, J.N.1    McKimm-Breschkin, J.L.2    Caldwell, J.B.3
  • 2
    • 0027287506 scopus 로고
    • Rational design of potent sialidase-based inhibitors of influenza virus replication
    • von Itzstein M, Wu WY, Kok GB et al. Rational design of potent sialidase-based inhibitors of influenza virus replication. Nature 1993; 363: 418-23.
    • (1993) Nature , vol.363 , pp. 418-423
    • von Itzstein, M.1    Wu, W.Y.2    Kok, G.B.3
  • 3
    • 0031048319 scopus 로고    scopus 로고
    • Influenza neuraminidase inhibitors possessing a novel hydrophobic interaction in the enzyme active site: Design, synthesis, and structural analysis of carbocyclic sialic acid analogues with potent anti-influenza activity
    • Kim CU, Lew W, Williams MA et al. Influenza neuraminidase inhibitors possessing a novel hydrophobic interaction in the enzyme active site:dEsign, synthesis, and structural analysis of carbocyclic sialic acid analogues with potent anti-influenza activity. J Am Chem Soc 1997; 119: 681-90.
    • (1997) J Am Chem Soc , vol.119 , pp. 681-690
    • Kim, C.U.1    Lew, W.2    Williams, M.A.3
  • 4
    • 0034699492 scopus 로고    scopus 로고
    • BCX-1812 (RWJ-270201): Discovery of a novel, highly potent, orally active, and selective influenza neuraminidase inhibitor through structure-based drug design
    • Babu YS, Chand P, Bantia S et al. BCX-1812 (RWJ-270201): Discovery of a novel, highly potent, orally active, and selective influenza neuraminidase inhibitor through structure-based drug design. J Med Chem 2000; 43: 3482-6.
    • (2000) J Med Chem , vol.43 , pp. 3482-3486
    • Babu, Y.S.1    Chand, P.2    Bantia, S.3
  • 5
    • 33748680857 scopus 로고    scopus 로고
    • BioCryst. (5 December date last accessed)
    • BioCryst. Peramivir Today. http://www.biocryst.com/pdf/ peramivirfacts.pdf. (5 December 2005, date last accessed).
    • (2005) Peramivir Today
  • 6
    • 0037161611 scopus 로고    scopus 로고
    • Structural studies of the resistance of influenza virus neuramindase to inhibitors
    • Smith BJ, McKimm-Breschkin JL, McDonald M et al. Structural studies of the resistance of influenza virus neuramindase to inhibitors. J Med Chem 2002; 45: 2207-12.
    • (2002) J Med Chem , vol.45 , pp. 2207-2212
    • Smith, B.J.1    McKimm-Breschkin, J.L.2    McDonald, M.3
  • 7
    • 0032526697 scopus 로고    scopus 로고
    • Drug design against a shifting target: A structural basis for resistance to inhibitors in a variant of influenza virus neuraminidase
    • Varghese JN, Smith PW, Sollis SL et al. Drug design against a shifting target: A structural basis for resistance to inhibitors in a variant of influenza virus neuraminidase. Structure 1998; 6: 735-46.
    • (1998) Structure , vol.6 , pp. 735-746
    • Varghese, J.N.1    Smith, P.W.2    Sollis, S.L.3
  • 8
    • 0030028671 scopus 로고    scopus 로고
    • Characterization of mutants of influenza A virus selected with the neuraminidase inhibitor 4-guanidino-Neu5Ac2en
    • Gubareva LV, Bethell R, Hart GJ et al. Characterization of mutants of influenza A virus selected with the neuraminidase inhibitor 4-guanidino-Neu5Ac2en. J Virol 1996; 70: 1818-27.
    • (1996) J Virol , vol.70 , pp. 1818-1827
    • Gubareva, L.V.1    Bethell, R.2    Hart, G.J.3
  • 9
    • 0031000886 scopus 로고    scopus 로고
    • Catalytic and framework mutations in the neurominidase active site of influenza viruses that are resistant to 4-guanidino-Neu5Ac2en
    • Gubareva LV, Robinson MJ, Bethell RC et al. Catalytic and framework mutations in the neurominidase active site of influenza viruses that are resistant to 4-guanidino-Neu5Ac2en. J Virol 1997; 71: 3385-90.
    • (1997) J Virol , vol.71 , pp. 3385-3390
    • Gubareva, L.V.1    Robinson, M.J.2    Bethell, R.C.3
  • 10
    • 0031911783 scopus 로고    scopus 로고
    • Mutations in a conserved residue in the influenza virus neuraminidase active site decreases sensitivity to Neu5Ac2en-derived inhibitors
    • McKimm-Breschkin JL, Sahasrabudhe A, Blick TJ et al. Mutations in a conserved residue in the influenza virus neuraminidase active site decreases sensitivity to Neu5Ac2en-derived inhibitors. J Virol 1998; 72: 2456-62.
    • (1998) J Virol , vol.72 , pp. 2456-2462
    • McKimm-Breschkin, J.L.1    Sahasrabudhe, A.2    Blick, T.J.3
  • 11
    • 0029585928 scopus 로고
    • Generation and characterization of an influenza virus neuraminidase variant with decreased sensitivity to the neuraminidase-specific inhibitor 4-guanidino-Neu5Ac2en
    • Blick TJ, Tiong T, Sahasrabudhe A et al. Generation and characterization of an influenza virus neuraminidase variant with decreased sensitivity to the neuraminidase-specific inhibitor 4-guanidino-Neu5Ac2en. Virology 1995; 214: 475-84.
    • (1995) Virology , vol.214 , pp. 475-484
    • Blick, T.J.1    Tiong, T.2    Sahasrabudhe, A.3
  • 12
    • 0033590206 scopus 로고    scopus 로고
    • In vitro selection and characterisation of influenza B/Beijing/1/87 isolates with altered susceptibility to zanamivir
    • Barnett JM, Cadman A, Burrell FM et al. In vitro selection and characterisation of influenza B/Beijing/1/87 isolates with altered susceptibility to zanamivir. Virology 1999; 265: 286-95.
    • (1999) Virology , vol.265 , pp. 286-295
    • Barnett, J.M.1    Cadman, A.2    Burrell, F.M.3
  • 13
    • 4644280355 scopus 로고    scopus 로고
    • In vitro generation and characterisation of an influenza B variant with reduced sensitivity to neuraminidase inhibitors
    • Cheam AL, Barr IG, Hampson AW et al. In vitro generation and characterisation of an influenza B variant with reduced sensitivity to neuraminidase inhibitors. Antiviral Res 2004; 63: 177-81.
    • (2004) Antiviral Res , vol.63 , pp. 177-181
    • Cheam, A.L.1    Barr, I.G.2    Hampson, A.W.3
  • 14
    • 0029560199 scopus 로고
    • Molecular basis for the resistance of influenza viruses to 4-guanidino-Neu5Ac2en
    • Staschke KA, Colacino JM, Baxter AJ et al. Molecular basis for the resistance of influenza viruses to 4-guanidino-Neu5Ac2en. Virology 1995; 214: 642-6.
    • (1995) Virology , vol.214 , pp. 642-646
    • Staschke, K.A.1    Colacino, J.M.2    Baxter, A.J.3
  • 15
    • 0031724750 scopus 로고    scopus 로고
    • Evidence for zanamivir resistance in an immunocompromised child infected with influenza B virus
    • Gubareva LV, Matrosovich MN, Brenner MK et al. Evidence for zanamivir resistance in an immunocompromised child infected with influenza B virus. J Infect Dis 1998; 178: 1257-62.
    • (1998) J Infect Dis , vol.178 , pp. 1257-1262
    • Gubareva, L.V.1    Matrosovich, M.N.2    Brenner, M.K.3
  • 16
    • 18144394370 scopus 로고    scopus 로고
    • Management of influenza virus infections with neuraminidase inhibitors: Detection, incidence, and implications of drug resistance
    • McKimm-Breschkin JL. Management of influenza virus infections with neuraminidase inhibitors: Detection, incidence, and implications of drug resistance. Treat Respir Med 2005; 4: 107-16.
    • (2005) Treat Respir Med , vol.4 , pp. 107-116
    • McKimm-Breschkin, J.L.1
  • 17
    • 27144468290 scopus 로고    scopus 로고
    • Avian flu: Isolation of drug-resistant H5N1 virus
    • Le QM, Kiso M, Someya K et al. Avian flu: Isolation of drug-resistant H5N1 virus. Nature 2005; 437: 1108.
    • (2005) Nature , vol.437 , pp. 1108
    • Le, Q.M.1    Kiso, M.2    Someya, K.3
  • 18
    • 4444369826 scopus 로고    scopus 로고
    • Resistant influenza A viruses in children treated with oseltamivir: Descriptive study
    • Kiso M, Mitamura K, Sakai-Tagawa Y et al. Resistant influenza A viruses in children treated with oseltamivir: Descriptive study. Lancet 2004; 364: 759-65.
    • (2004) Lancet , vol.364 , pp. 759-765
    • Kiso, M.1    Mitamura, K.2    Sakai-Tagawa, Y.3
  • 19
    • 14744293108 scopus 로고    scopus 로고
    • Oseltamivir (Tamiflu) and its potential for use in the event of an influenza pandemic
    • Ward P, Small I, Smith J et al. Oseltamivir (Tamiflu) and its potential for use in the event of an influenza pandemic. J Antimicrob Chemother 2005; 55 Suppl 1: I5-21.
    • (2005) J Antimicrob Chemother , vol.55 , Issue.SUPPL. 1
    • Ward, P.1    Small, I.2    Smith, J.3
  • 20
    • 14744304629 scopus 로고    scopus 로고
    • Characterization of recombinant influenza B viruses with key neuraminidase inhibitor resistance mutations
    • Jackson D, Barclay W, Zurcher T. Characterization of recombinant influenza B viruses with key neuraminidase inhibitor resistance mutations. J Antimicrob Chemother 2005; 55: 162-9.
    • (2005) J Antimicrob Chemother , vol.55 , pp. 162-169
    • Jackson, D.1    Barclay, W.2    Zurcher, T.3
  • 21
    • 12244295453 scopus 로고    scopus 로고
    • Evaluation of neuraminidase enzyme assays using different substrates to measure susceptibility of influenza virus clinical isolates to neuraminidase inhibitors: Report of the neuraminidase inhibitor susceptibility network
    • Wetherall NT, Trivedi T, Zeller J et al. Evaluation of neuraminidase enzyme assays using different substrates to measure susceptibility of influenza virus clinical isolates to neuraminidase inhibitors: Report of the neuraminidase inhibitor susceptibility network. J Clin Microbiol 2003; 41: 742-50.
    • (2003) J Clin Microbiol , vol.41 , pp. 742-750
    • Wetherall, N.T.1    Trivedi, T.2    Zeller, J.3
  • 22
    • 4344672299 scopus 로고    scopus 로고
    • A reverse genetics study of resistance to neuraminidase inhibitors in an influenza A/H1N1 virus
    • Abed Y, Goyette N, Boivin G. A reverse genetics study of resistance to neuraminidase inhibitors in an influenza A/H1N1 virus. Antivir Ther 2004; 9: 577-81.
    • (2004) Antivir Ther , vol.9 , pp. 577-581
    • Abed, Y.1    Goyette, N.2    Boivin, G.3
  • 23
    • 0036828039 scopus 로고    scopus 로고
    • A reverse genetics approach for recovery of recombinant influenza B viruses entirely from cDNA
    • Jackson D, Cadman A, Zurcher T et al. A reverse genetics approach for recovery of recombinant influenza B viruses entirely from cDNA. J Virol 2002; 76: 11744-7.
    • (2002) J Virol , vol.76 , pp. 11744-11747
    • Jackson, D.1    Cadman, A.2    Zurcher, T.3
  • 24
    • 0023957688 scopus 로고
    • Analysis of clustered point mutations in the human ribosomal RNA gene promoter by transient expression in vivo
    • Jones MH, Learned RM, Tjian R. Analysis of clustered point mutations in the human ribosomal RNA gene promoter by transient expression in vivo. Proc Natl Acad Sci USA 1988; 85: 669-73.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 669-673
    • Jones, M.H.1    Learned, R.M.2    Tjian, R.3
  • 25
    • 0028008470 scopus 로고
    • Influenza virus NS1 protein inhibits pre-mRNA splicing and blocks mRNA nucleocytoplasmic transport
    • Fortes P, Beloso A, Ortin J. Influenza virus NS1 protein inhibits pre-mRNA splicing and blocks mRNA nucleocytoplasmic transport. EMBO J 1994; 13: 704-12.
    • (1994) EMBO J , vol.13 , pp. 704-712
    • Fortes, P.1    Beloso, A.2    Ortin, J.3
  • 26
    • 0027998896 scopus 로고
    • Synthesis of biologically active influenza virus core proteins using a vaccinia virus-T7 RNA polymerase expression system
    • Mena I, de la Luna S, Albo C et al. Synthesis of biologically active influenza virus core proteins using a vaccinia virus-T7 RNA polymerase expression system. J Gen Virol 1994; 75: 2109-14.
    • (1994) J Gen Virol , vol.75 , pp. 2109-2114
    • Mena, I.1    de la Luna, S.2    Albo, C.3
  • 27
    • 0031585559 scopus 로고    scopus 로고
    • Mutations affecting the sensitivity of the influenza virus neuraminidase to 4-guanidino-2, 4-dideoxy-2,3-dehydro-N-acetylneuraminic acid
    • Goto H, Bethell RC, Kawaoka Y. Mutations affecting the sensitivity of the influenza virus neuraminidase to 4-guanidino-2, 4-dideoxy-2,3-dehydro-N-acetylneuraminic acid. Virology 1997; 238: 265-72.
    • (1997) Virology , vol.238 , pp. 265-272
    • Goto, H.1    Bethell, R.C.2    Kawaoka, Y.3
  • 28
    • 0034194390 scopus 로고    scopus 로고
    • Development of a sensitive chemiluminescent neuraminidase assay for the determination of influenza virus susceptibility to zanamivir
    • Buxton RC, Edwards B, Juo RR et al. Development of a sensitive chemiluminescent neuraminidase assay for the determination of influenza virus susceptibility to zanamivir. Anal Biochem 2000; 280: 291-300.
    • (2000) Anal Biochem , vol.280 , pp. 291-300
    • Buxton, R.C.1    Edwards, B.2    Juo, R.R.3
  • 29
    • 0030296267 scopus 로고    scopus 로고
    • Mutation in the influenza virus neuraminidase gene resulting in decreased sensitivity to the neuraminidase inhibitor 4-guanidino. Neu5Ac2en leads to instability of the enzyme
    • McKimm-Breschkin JL, McDonald M, Blick TJ et al. Mutation in the influenza virus neuraminidase gene resulting in decreased sensitivity to the neuraminidase inhibitor 4-guanidino. Neu5Ac2en leads to instability of the enzyme. Virology 1996; 225: 240-2.
    • (1996) Virology , vol.225 , pp. 240-242
    • McKimm-Breschkin, J.L.1    McDonald, M.2    Blick, T.J.3
  • 30
    • 0023226739 scopus 로고
    • Antigenic structure and variation in an influenza virus N9 neuraminidase
    • Webster RG, Air GM, Metzger DW et al. Antigenic structure and variation in an influenza virus N9 neuraminidase. J Virol 1987; 61: 2910-6.
    • (1987) J Virol , vol.61 , pp. 2910-2916
    • Webster, R.G.1    Air, G.M.2    Metzger, D.W.3
  • 31
    • 0025877463 scopus 로고
    • A new method for the purification of the influenza A virus neuraminidase
    • McKimm-Breschkin JL, Caldwell JB, Guthrie RE et al. A new method for the purification of the influenza A virus neuraminidase. J Virol Methods 1991; 32: 121-4.
    • (1991) J Virol Methods , vol.32 , pp. 121-124
    • McKimm-Breschkin, J.L.1    Caldwell, J.B.2    Guthrie, R.E.3
  • 32
    • 0037636478 scopus 로고    scopus 로고
    • Neuraminidase sequence analysis and susceptibilities of influenza virus clinical isolates to zanamivir and oseltamivir
    • McKimm-Breschkin J, Trivedi T, Hampson A et al. Neuraminidase sequence analysis and susceptibilities of influenza virus clinical isolates to zanamivir and oseltamivir. Antimicrob Agents Chemother 2003; 47: 2264-72.
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 2264-2272
    • McKimm-Breschkin, J.1    Trivedi, T.2    Hampson, A.3
  • 33
    • 0003178444 scopus 로고    scopus 로고
    • An oseltamivir treatment-selected influenza A:N2 virus with a R292K mutation in the neuraminidase gene has reduced infectivity in vivo
    • Ives J, Carr J, Roberts NA et al. An oseltamivir treatment-selected influenza A:N2 virus with a R292K mutation in the neuraminidase gene has reduced infectivity in vivo. J Clinical Virol 2000; 18: 251-69.
    • (2000) J Clinical Virol , vol.18 , pp. 251-269
    • Ives, J.1    Carr, J.2    Roberts, N.A.3
  • 34
    • 0036894107 scopus 로고    scopus 로고
    • Mechanism by which mutations at his274 alter sensitivity of influenza a virus n1 neuraminidase to oseltamivir carboxylate and zanamivir
    • Wang MZ, Tai CY, Mendel DB. Mechanism by which mutations at his274 alter sensitivity of influenza a virus n1 neuraminidase to oseltamivir carboxylate and zanamivir. Antimicrob Agents Chemother 2002; 46: 3809-16.
    • (2002) Antimicrob Agents Chemother , vol.46 , pp. 3809-3816
    • Wang, M.Z.1    Tai, C.Y.2    Mendel, D.B.3
  • 35
    • 0033961667 scopus 로고    scopus 로고
    • Monitoring of viral susceptibility: New challenges with the development of influenza NA inhibitors
    • Tisdale M. Monitoring of viral susceptibility: New challenges with the development of influenza NA inhibitors. Rev Med Virol 2000; 10: 45-55.
    • (2000) Rev Med Virol , vol.10 , pp. 45-55
    • Tisdale, M.1
  • 36
    • 0033897803 scopus 로고    scopus 로고
    • Resistance of influenza viruses to neuraminidase inhibitors - A review
    • McKimm-Breschkin JL. Resistance of influenza viruses to neuraminidase inhibitors - a review. Antiviral Res 2000; 47: 1-17.
    • (2000) Antiviral Res , vol.47 , pp. 1-17
    • McKimm-Breschkin, J.L.1
  • 37
    • 0030671283 scopus 로고    scopus 로고
    • Structural evidence for a second sialic acid binding site in avian influenza virus neuraminidases
    • Varghese JN, Colman PM, van Donkelaar A et al. Structural evidence for a second sialic acid binding site in avian influenza virus neuraminidases. Proc Natl Acad Sci USA 1997; 94: 11808-12.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11808-11812
    • Varghese, J.N.1    Colman, P.M.2    van Donkelaar, A.3
  • 38
    • 0036091649 scopus 로고    scopus 로고
    • In vitro selection and characterization of influenza A (A/N9) virus variants resistant to a novel neuraminidase inhibitor
    • A-315675
    • Molla A, Kati W, Carrick R et al. In vitro selection and characterization of influenza A (A/N9) virus variants resistant to a novel neuraminidase inhibitor, A-315675. J Virol 2002; 76: 5380-6.
    • (2002) J Virol , vol.76 , pp. 5380-5386
    • Molla, A.1    Kati, W.2    Carrick, R.3
  • 39
    • 0025874138 scopus 로고
    • Refined atomic structures of N9 subtype influenza virus neuraminidase and escape mutants
    • Tulip WR, Varghese JN, Baker AT et al. Refined atomic structures of N9 subtype influenza virus neuraminidase and escape mutants. J Mol Biol 1991; 221: 487-97.
    • (1991) J Mol Biol , vol.221 , pp. 487-497
    • Tulip, W.R.1    Varghese, J.N.2    Baker, A.T.3
  • 40
    • 0023475950 scopus 로고
    • Three-dimensional structure of neuraminidase of subtype N9 from an avian influenza virus
    • Baker AT, Varghese JN, Laver WG et al. Three-dimensional structure of neuraminidase of subtype N9 from an avian influenza virus. Proteins 1987; 2: 111-7.
    • (1987) Proteins , vol.2 , pp. 111-117
    • Baker, A.T.1    Varghese, J.N.2    Laver, W.G.3
  • 41
    • 0029003145 scopus 로고
    • Three-dimensional structure of the complex of 4-guanidino-Neu5Ac2en and influenza virus neuraminidase
    • Varghese JN, Epa VC, Colman PM. Three-dimensional structure of the complex of 4-guanidino-Neu5Ac2en and influenza virus neuraminidase. Protein Sci 1995; 4: 1081-7.
    • (1995) Protein Sci , vol.4 , pp. 1081-1087
    • Varghese, J.N.1    Epa, V.C.2    Colman, P.M.3


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