메뉴 건너뛰기




Volumn 7, Issue 9, 2012, Pages

Exploring the Mechanism of Zanamivir Resistance in a Neuraminidase Mutant: A Molecular Dynamics Study

Author keywords

[No Author keywords available]

Indexed keywords

MUTANT PROTEIN; SIALIDASE; ZANAMIVIR;

EID: 84866106043     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0044057     Document Type: Article
Times cited : (13)

References (50)
  • 3
    • 0037468827 scopus 로고    scopus 로고
    • Ecological and immunological determinants of influenza evolution
    • Ferguson NM, Galvani AP, Bush RM, (2003) Ecological and immunological determinants of influenza evolution. Nature 422: 428-433.
    • (2003) Nature , vol.422 , pp. 428-433
    • Ferguson, N.M.1    Galvani, A.P.2    Bush, R.M.3
  • 4
    • 0344395604 scopus 로고    scopus 로고
    • Are we ready for pandemic influenza?
    • Webby RJ, Webster RG, (2003) Are we ready for pandemic influenza? Science 302: 1519-1522.
    • (2003) Science , vol.302 , pp. 1519-1522
    • Webby, R.J.1    Webster, R.G.2
  • 5
    • 31344462092 scopus 로고    scopus 로고
    • Pandemic influenza threat and preparedness
    • Fauci AS, (2006) Pandemic influenza threat and preparedness. Emerg Infect Dis 12: 73-77.
    • (2006) Emerg Infect Dis , vol.12 , pp. 73-77
    • Fauci, A.S.1
  • 6
    • 25444501243 scopus 로고    scopus 로고
    • Drug therapy - Neuraminidase inhibitors for influenza
    • Moscona A, (2005) Drug therapy- Neuraminidase inhibitors for influenza. New England Journal of Medicine 353: 1363-1373.
    • (2005) New England Journal of Medicine , vol.353 , pp. 1363-1373
    • Moscona, A.1
  • 7
    • 67649297821 scopus 로고    scopus 로고
    • Emergence and pandemic potential of swine-origin H1N1 influenza virus
    • Neumann G, Noda T, Kawaoka Y, (2009) Emergence and pandemic potential of swine-origin H1N1 influenza virus. Nature 459: 931-939.
    • (2009) Nature , vol.459 , pp. 931-939
    • Neumann, G.1    Noda, T.2    Kawaoka, Y.3
  • 8
    • 70449127983 scopus 로고    scopus 로고
    • New prospects for the rational design of antivirals
    • Nistal-Villan E, Garcia-Sastre A, (2009) New prospects for the rational design of antivirals. Nature Medicine 15: 1253-1254.
    • (2009) Nature Medicine , vol.15 , pp. 1253-1254
    • Nistal-Villan, E.1    Garcia-Sastre, A.2
  • 9
    • 33344475829 scopus 로고    scopus 로고
    • Antiviral resistance in influenza viruses-implications for management and pandemic response
    • Hayden FG, (2006) Antiviral resistance in influenza viruses-implications for management and pandemic response. N Engl J Med 354: 785-788.
    • (2006) N Engl J Med , vol.354 , pp. 785-788
    • Hayden, F.G.1
  • 12
    • 1242285459 scopus 로고    scopus 로고
    • A new millennium conundrum: how to use a powerful class of influenza anti-neuraminidase drugs (NAIs) in the community
    • Oxford J, Balasingam S, Lambkin R, (2004) A new millennium conundrum: how to use a powerful class of influenza anti-neuraminidase drugs (NAIs) in the community. Journal of Antimicrobial Chemotherapy 53: 133-136.
    • (2004) Journal of Antimicrobial Chemotherapy , vol.53 , pp. 133-136
    • Oxford, J.1    Balasingam, S.2    Lambkin, R.3
  • 13
    • 0036224388 scopus 로고    scopus 로고
    • Influenza virus carrying neuraminidase with reduced sensitivity to oseltamivir carboxylate has altered properties in vitro and is compromised for infectivity and replicative ability in vivo
    • Carr J, Ives J, Kelly L, Lambkin R, Oxford J, et al. (2002) Influenza virus carrying neuraminidase with reduced sensitivity to oseltamivir carboxylate has altered properties in vitro and is compromised for infectivity and replicative ability in vivo. Antiviral Research 54: 79-88.
    • (2002) Antiviral Research , vol.54 , pp. 79-88
    • Carr, J.1    Ives, J.2    Kelly, L.3    Lambkin, R.4    Oxford, J.5
  • 14
    • 46249111790 scopus 로고    scopus 로고
    • Crystal structures of oseltamivir-resistant influenza virus neuraminidase mutants
    • 1258-U1261
    • Collins PJ, Haire LF, Lin YP, Liu JF, Russell RJ, et al. (2008) Crystal structures of oseltamivir-resistant influenza virus neuraminidase mutants. Nature 453: 1258-U1261.
    • (2008) Nature , vol.453
    • Collins, P.J.1    Haire, L.F.2    Lin, Y.P.3    Liu, J.F.4    Russell, R.J.5
  • 15
    • 77954079771 scopus 로고    scopus 로고
    • Effect of Neuraminidase Inhibitor-Resistant Mutations on Pathogenicity of Clade 2.2 A/Turkey/15/06 (H5N1) Influenza Virus in Ferrets
    • Ilyushina NA, Seiler JP, Rehg JE, Webster RG, Govorkova EA, (2010) Effect of Neuraminidase Inhibitor-Resistant Mutations on Pathogenicity of Clade 2.2 A/Turkey/15/06 (H5N1) Influenza Virus in Ferrets. Plos Pathogens 6.
    • (2010) Plos Pathogens , vol.6
    • Ilyushina, N.A.1    Seiler, J.P.2    Rehg, J.E.3    Webster, R.G.4    Govorkova, E.A.5
  • 16
    • 85086811993 scopus 로고    scopus 로고
    • Emergence of a Multidrug-Resistant Pandemic Influenza A (H1N1) Virus (vol 363, pg 1381, 2010)
    • Van Der Vries E, (2011) Emergence of a Multidrug-Resistant Pandemic Influenza A (H1N1) Virus (vol 363, pg 1381, 2010). New England Journal of Medicine 364: 1182-1182.
    • (2011) New England Journal of Medicine , vol.364 , pp. 1182
    • van der Vries, E.1
  • 17
    • 80052834610 scopus 로고    scopus 로고
    • Novel Genotyping and Quantitative Analysis of Neuraminidase Inhibitor Resistance-Associated Mutations in Influenza A Viruses by Single-Nucleotide Polymorphism Analysis
    • Duan S, Boltz DA, Li J, Oshansky CM, Marjuki H, et al. (2011) Novel Genotyping and Quantitative Analysis of Neuraminidase Inhibitor Resistance-Associated Mutations in Influenza A Viruses by Single-Nucleotide Polymorphism Analysis. Antimicrobial Agents and Chemotherapy 55: 4718-4727.
    • (2011) Antimicrobial Agents and Chemotherapy , vol.55 , pp. 4718-4727
    • Duan, S.1    Boltz, D.A.2    Li, J.3    Oshansky, C.M.4    Marjuki, H.5
  • 18
    • 33845384187 scopus 로고    scopus 로고
    • Resistance to anti-influenza drugs: adamantanes and neuraminidase inhibitors
    • Hurt AC, Ho HT, Barr I, (2006) Resistance to anti-influenza drugs: adamantanes and neuraminidase inhibitors. Expert Rev Anti Infect Ther 4: 795-805.
    • (2006) Expert Rev Anti Infect Ther , vol.4 , pp. 795-805
    • Hurt, A.C.1    Ho, H.T.2    Barr, I.3
  • 19
    • 70349728568 scopus 로고    scopus 로고
    • Zanamivir-resistant influenza viruses with a novel neuraminidase mutation
    • Hurt AC, Holien JK, Parker M, Kelso A, Barr IG, (2009) Zanamivir-resistant influenza viruses with a novel neuraminidase mutation. J Virol 83: 10366-10373.
    • (2009) J Virol , vol.83 , pp. 10366-10373
    • Hurt, A.C.1    Holien, J.K.2    Parker, M.3    Kelso, A.4    Barr, I.G.5
  • 20
    • 57749118013 scopus 로고    scopus 로고
    • Origins of resistance conferred by the R292K neuraminidase mutation via molecular dynamics and free energy calculations
    • Chachra R, Rizzo RC, (2008) Origins of resistance conferred by the R292K neuraminidase mutation via molecular dynamics and free energy calculations. Journal of Chemical Theory and Computation 4: 1526-1540.
    • (2008) Journal of Chemical Theory and Computation , vol.4 , pp. 1526-1540
    • Chachra, R.1    Rizzo, R.C.2
  • 21
    • 33748437791 scopus 로고    scopus 로고
    • The structure of H5N1 avian influenza neuraminidase suggests new opportunities for drug design
    • Russell RJ, Haire LF, Stevens DJ, Collins PJ, Lin YP, et al. (2006) The structure of H5N1 avian influenza neuraminidase suggests new opportunities for drug design. Nature 443: 45-49.
    • (2006) Nature , vol.443 , pp. 45-49
    • Russell, R.J.1    Haire, L.F.2    Stevens, D.J.3    Collins, P.J.4    Lin, Y.P.5
  • 22
    • 0035175679 scopus 로고    scopus 로고
    • PDBsum: summaries and analyses of PDB structures
    • Laskowski RA, (2001) PDBsum: summaries and analyses of PDB structures. Nucleic Acids Research 29: 221-222.
    • (2001) Nucleic Acids Research , vol.29 , pp. 221-222
    • Laskowski, R.A.1
  • 24
    • 0028922586 scopus 로고
    • Ligplot - a Program to Generate Schematic Diagrams of Protein Ligand Interactions
    • Wallace AC, Laskowski RA, Thornton JM, (1995) Ligplot- a Program to Generate Schematic Diagrams of Protein Ligand Interactions. Protein Engineering 8: 127-134.
    • (1995) Protein Engineering , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 25
    • 77749316142 scopus 로고    scopus 로고
    • Optimizing the Performance of Bias-Exchange Metadynamics: Folding a 48-Residue LysM Domain Using a Coarse-Grained Model
    • Cossio P, Marinelli F, Laio A, Pietrucci F, (2010) Optimizing the Performance of Bias-Exchange Metadynamics: Folding a 48-Residue LysM Domain Using a Coarse-Grained Model. Journal of Physical Chemistry B 114: 3259-3265.
    • (2010) Journal of Physical Chemistry B , vol.114 , pp. 3259-3265
    • Cossio, P.1    Marinelli, F.2    Laio, A.3    Pietrucci, F.4
  • 26
    • 58149299971 scopus 로고    scopus 로고
    • Metadynamics: a method to simulate rare events and reconstruct the free energy in biophysics, chemistry and material science
    • Laio A, Gervasio FL, (2008) Metadynamics: a method to simulate rare events and reconstruct the free energy in biophysics, chemistry and material science. Reports on Progress in Physics 71.
    • (2008) Reports on Progress in Physics , vol.71
    • Laio, A.1    Gervasio, F.L.2
  • 33
    • 55249083577 scopus 로고    scopus 로고
    • Structural Characterization of the 1918 Influenza Virus H1N1 Neuraminidase
    • Xu XJ, Zhu XY, Dwek RA, Stevens J, Wilson IA, (2008) Structural Characterization of the 1918 Influenza Virus H1N1 Neuraminidase. Journal of Virology 82: 10493-10501.
    • (2008) Journal of Virology , vol.82 , pp. 10493-10501
    • Xu, X.J.1    Zhu, X.Y.2    Dwek, R.A.3    Stevens, J.4    Wilson, I.A.5
  • 34
    • 77957767268 scopus 로고    scopus 로고
    • The 2009 pandemic H1N1 neuraminidase N1 lacks the 150-cavity in its active site
    • Li Q, Qi J, Zhang W, Vavricka CJ, Shi Y, et al. The 2009 pandemic H1N1 neuraminidase N1 lacks the 150-cavity in its active site. Nat Struct Mol Biol 17: 1266-1268.
    • Nat Struct Mol Biol , vol.17 , pp. 1266-1268
    • Li, Q.1    Qi, J.2    Zhang, W.3    Vavricka, C.J.4    Shi, Y.5
  • 35
    • 33645278326 scopus 로고    scopus 로고
    • Avian flu: influenza virus receptors in the human airway
    • Shinya K, Ebina M, Yamada S, Ono M, Kasai N, et al. (2006) Avian flu: influenza virus receptors in the human airway. Nature 440: 435-436.
    • (2006) Nature , vol.440 , pp. 435-436
    • Shinya, K.1    Ebina, M.2    Yamada, S.3    Ono, M.4    Kasai, N.5
  • 36
    • 0001398008 scopus 로고    scopus 로고
    • How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules?
    • Wang JM, Cieplak P, Kollman PA, (2000) How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules? Journal of Computational Chemistry 21: 1049-1074.
    • (2000) Journal of Computational Chemistry , vol.21 , pp. 1049-1074
    • Wang, J.M.1    Cieplak, P.2    Kollman, P.A.3
  • 39
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: a package for molecular simulation and trajectory analysis
    • Lindahl E, Hess B, van der Spoel D, (2001) GROMACS 3.0: a package for molecular simulation and trajectory analysis. Journal of Molecular Modeling 7: 306-317.
    • (2001) Journal of Molecular Modeling , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    van der Spoel, D.3
  • 41
    • 77952251127 scopus 로고    scopus 로고
    • Linking Well-Tempered Metadynamics Simulations with Experiments
    • Barducci A, Bonomi M, Parrinello M, (2010) Linking Well-Tempered Metadynamics Simulations with Experiments. Biophysical Journal 98: L44-L46.
    • (2010) Biophysical Journal , vol.98
    • Barducci, A.1    Bonomi, M.2    Parrinello, M.3
  • 44
    • 38349091489 scopus 로고    scopus 로고
    • Well-tempered metadynamics: A smoothly converging and tunable free-energy method
    • Barducci A, Bussi G, Parrinello M, (2008) Well-tempered metadynamics: A smoothly converging and tunable free-energy method. Physical Review Letters 100.
    • (2008) Physical Review Letters , vol.100
    • Barducci, A.1    Bussi, G.2    Parrinello, M.3
  • 45
    • 33750040264 scopus 로고    scopus 로고
    • Free-energy landscape for beta hairpin folding from combined parallel tempering and metadynamics
    • Bussi G, Gervasio FL, Laio A, Parrinello M, (2006) Free-energy landscape for beta hairpin folding from combined parallel tempering and metadynamics. Journal of the American Chemical Society 128: 13435-13441.
    • (2006) Journal of the American Chemical Society , vol.128 , pp. 13435-13441
    • Bussi, G.1    Gervasio, F.L.2    Laio, A.3    Parrinello, M.4
  • 47
    • 2942548219 scopus 로고    scopus 로고
    • Reconstructing the density of states by history-dependent metadynamics
    • Micheletti C, Laio A, Parrinello M, (2004) Reconstructing the density of states by history-dependent metadynamics. Physical Review Letters 92.
    • (2004) Physical Review Letters , vol.92
    • Micheletti, C.1    Laio, A.2    Parrinello, M.3
  • 50
    • 46849105028 scopus 로고    scopus 로고
    • Ensemble-based virtual screening reveals potential novel antiviral compounds for avian influenza neuraminidase
    • Cheng LS, Amaro RE, Xu D, Li WW, Arzberger PW, et al. (2008) Ensemble-based virtual screening reveals potential novel antiviral compounds for avian influenza neuraminidase. Journal of Medicinal Chemistry 51: 3878-3894.
    • (2008) Journal of Medicinal Chemistry , vol.51 , pp. 3878-3894
    • Cheng, L.S.1    Amaro, R.E.2    Xu, D.3    Li, W.W.4    Arzberger, P.W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.