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Volumn 68, Issue 2, 2014, Pages 291-299

Insight into the Oseltamivir Resistance R292K Mutation in H5N1 Influenza Virus: A Molecular Docking and Molecular Dynamics Approach

Author keywords

Molecular docking; Molecular dynamic simulation; Neuraminidase; Oseltamivir resistance; Potential of mean force

Indexed keywords

ANTIVIRUS AGENT; OSELTAMIVIR; SIALIDASE;

EID: 84893968205     PISSN: 10859195     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12013-013-9709-2     Document Type: Article
Times cited : (14)

References (48)
  • 2
    • 10744231351 scopus 로고    scopus 로고
    • Re-emergence of fatal human influenza A subtype H5N1 disease
    • Peiris, J. S., Yu, W. C., Leung, C. W., Cheung, C. Y., Ng, W. F., Nicholls, J. M., et al. (2004). Re-emergence of fatal human influenza A subtype H5N1 disease. Lancet, 363, 617-619.
    • (2004) Lancet , vol.363 , pp. 617-619
    • Peiris, J.S.1    Yu, W.C.2    Leung, C.W.3    Cheung, C.Y.4    Ng, W.F.5    Nicholls, J.M.6
  • 3
    • 19944431476 scopus 로고    scopus 로고
    • Characterization of H5N1 influenza A viruses isolated during the 2003-2004 influenza outbreaks in Japan
    • Mase, M., Tsukamoto, K., Imada, T., Imai, K., Tanimura, N., Nakamura, K., et al. (2005). Characterization of H5N1 influenza A viruses isolated during the 2003-2004 influenza outbreaks in Japan. Virology, 332, 167-176.
    • (2005) Virology , vol.332 , pp. 167-176
    • Mase, M.1    Tsukamoto, K.2    Imada, T.3    Imai, K.4    Tanimura, N.5    Nakamura, K.6
  • 5
    • 67650921421 scopus 로고    scopus 로고
    • The special neuraminidase stalk-motif responsible for increased virulence and pathogenesis of H5N1 influenza A virus
    • Zhou, H., Yu, Z., Hu, Y., Tu, J., Zou, W., et al. (2009). The special neuraminidase stalk-motif responsible for increased virulence and pathogenesis of H5N1 influenza A virus. PLoS ONE, 4, e6277.
    • (2009) PLoS ONE , vol.4
    • Zhou, H.1    Yu, Z.2    Hu, Y.3    Tu, J.4    Zou, W.5
  • 6
    • 0017664543 scopus 로고
    • Evidence from studies with a cross-linking reagent that the haemagglutinin of influenza virus is a trimer
    • Wiley, D. C., Skehel, J. J., & Waterfield, M. (1977). Evidence from studies with a cross-linking reagent that the haemagglutinin of influenza virus is a trimer. Virology, 79, 446-448.
    • (1977) Virology , vol.79 , pp. 446-448
    • Wiley, D.C.1    Skehel, J.J.2    Waterfield, M.3
  • 7
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution
    • Wilson, I. A., Skehel, J. J., & Wiley, D. C. (1981). Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution. Nature, 289, 366-373.
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 8
    • 77954056442 scopus 로고    scopus 로고
    • Enhancement of the influenza A hemagglutinin (HA)-mediated cell-cell fusion and virus entry by the viral neuraminidase (NA)
    • Su, B., Wurtzer, S., Rameix-Welti, M. A., Dwyer, D., van der Werf, S., Naffakh, N., et al. (2009). Enhancement of the influenza A hemagglutinin (HA)-mediated cell-cell fusion and virus entry by the viral neuraminidase (NA). PLoS ONE, 4, e8495.
    • (2009) PLoS ONE , vol.4
    • Su, B.1    Wurtzer, S.2    Rameix-Welti, M.A.3    Dwyer, D.4    van der Werf, S.5    Naffakh, N.6
  • 9
    • 67649227029 scopus 로고    scopus 로고
    • Emergence of a novel swine-origin influenza A virus (S-OIV) H1N1 virus in humans
    • Peiris, J. S., Poon, L. L., & Guan, Y. (2009). Emergence of a novel swine-origin influenza A virus (S-OIV) H1N1 virus in humans. Journal of Clinical Virology, 4, 169-173.
    • (2009) Journal of Clinical Virology , vol.4 , pp. 169-173
    • Peiris, J.S.1    Poon, L.L.2    Guan, Y.3
  • 10
    • 0027287506 scopus 로고
    • Rational design of potent sialidase-based inhibitors of influenza virus replication
    • von Itzstein, M., Wu, W. Y., Kok, G. B., Pegg, M. S., Dyason, J. C., Jin, B., et al. (1993). Rational design of potent sialidase-based inhibitors of influenza virus replication. Nature, 363, 418-423.
    • (1993) Nature , vol.363 , pp. 418-423
    • von Itzstein, M.1    Wu, W.Y.2    Kok, G.B.3    Pegg, M.S.4    Dyason, J.C.5    Jin, B.6
  • 11
    • 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, C. U., Lew, W., Williams, M. A., Liu, H., Zhang, L., Swaminathan, S., et al. (1997). 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. Journal of the American Chemical Society, 119, 681-690.
    • (1997) Journal of the American Chemical Society , vol.119 , pp. 681-690
    • Kim, C.U.1    Lew, W.2    Williams, M.A.3    Liu, H.4    Zhang, L.5    Swaminathan, S.6
  • 12
    • 0034603350 scopus 로고    scopus 로고
    • Influenza virus neuraminidase inhibitors
    • Gubareva, L. V., Kaiser, L., & Hayden, F. G. (2000). Influenza virus neuraminidase inhibitors. Lancet, 355, 827-835.
    • (2000) Lancet , vol.355 , pp. 827-835
    • Gubareva, L.V.1    Kaiser, L.2    Hayden, F.G.3
  • 13
    • 0015371575 scopus 로고
    • A 2 (N2) neuraminidase of the X-7 influenza virus recombinant: Determination of molecular size and subunit composition of the active unit
    • Bucher, D. J., & Kilbourne, E. D. (1972). A 2 (N2) neuraminidase of the X-7 influenza virus recombinant: Determination of molecular size and subunit composition of the active unit. Journal of Virology, 10, 60-66.
    • (1972) Journal of Virology , vol.10 , pp. 60-66
    • Bucher, D.J.1    Kilbourne, E.D.2
  • 16
    • 4444369826 scopus 로고    scopus 로고
    • Resistant influenza A viruses in children treated with oseltamivir: Descriptive study
    • Kiso, M., Mitamura, K., Sakai-Tagawa, Y., Shiraishi, K., Kawakami, C., Kimura, K., et al. (2004). Resistant influenza A viruses in children treated with oseltamivir: Descriptive study. Lancet, 364, 759-765.
    • (2004) Lancet , vol.364 , pp. 759-765
    • Kiso, M.1    Mitamura, K.2    Sakai-Tagawa, Y.3    Shiraishi, K.4    Kawakami, C.5    Kimura, K.6
  • 18
    • 34047226373 scopus 로고    scopus 로고
    • Emergence of influenza B viruses with reduced sensitivity to neuraminidase inhibitors
    • Hatakeyama, S., Sugaya, N., Ito, M., Yamazaki, M., Ichikawa, M., Kimura, K., et al. (2007). Emergence of influenza B viruses with reduced sensitivity to neuraminidase inhibitors. JAMA, 297, 1435-1442.
    • (2007) Jama , vol.297 , pp. 1435-1442
    • Hatakeyama, S.1    Sugaya, N.2    Ito, M.3    Yamazaki, M.4    Ichikawa, M.5    Kimura, K.6
  • 19
    • 75549083042 scopus 로고    scopus 로고
    • Oseltamivir-resistant influenza A (H1N1) viruses detected in Europe during season 2007-8 had epidemiologic and clinical characteristics similar to co-circulating susceptible A(H1N1) viruses
    • Ciancio, B. C., Meerhoff, T. J., Kramarz, P., Bonmarin, I., Borgen, K., et al. (2009). Oseltamivir-resistant influenza A (H1N1) viruses detected in Europe during season 2007-8 had epidemiologic and clinical characteristics similar to co-circulating susceptible A(H1N1) viruses. Eurosurveillance, 14, 19412.
    • (2009) Eurosurveillance , vol.14 , pp. 19412
    • Ciancio, B.C.1    Meerhoff, T.J.2    Kramarz, P.3    Bonmarin, I.4    Borgen, K.5
  • 20
    • 80054950510 scopus 로고    scopus 로고
    • Molecular dynamics simulations and drug discovery
    • Durrant, J. D., & McCammon, J. A. (2011). Molecular dynamics simulations and drug discovery. BMC Biology, 9, 71-79.
    • (2011) BMC Biology , vol.9 , pp. 71-79
    • Durrant, J.D.1    McCammon, J.A.2
  • 21
    • 84861481032 scopus 로고    scopus 로고
    • Exploring the cause of oseltamivir resistance against mutant H274Y neuraminidase by molecular simulation approach
    • Karthick, V., Shanthi, V., Rajasekaran, R., & Ramanathan, K. (2012). Exploring the cause of oseltamivir resistance against mutant H274Y neuraminidase by molecular simulation approach. Applied Biochemistry and Biotechnology, 167, 237-249.
    • (2012) Applied Biochemistry and Biotechnology , vol.167 , pp. 237-249
    • Karthick, V.1    Shanthi, V.2    Rajasekaran, R.3    Ramanathan, K.4
  • 22
    • 84873077420 scopus 로고    scopus 로고
    • In silico analysis of drug-resistant mutant of neuraminidase (N294S) against oseltamivir
    • Karthick, V., Shanthi, V., Rajasekaran, R., & Ramanathan, K. (2012). In silico analysis of drug-resistant mutant of neuraminidase (N294S) against oseltamivir. Protoplasma, 250, 197-207.
    • (2012) Protoplasma , vol.250 , pp. 197-207
    • Karthick, V.1    Shanthi, V.2    Rajasekaran, R.3    Ramanathan, K.4
  • 23
    • 57749118013 scopus 로고    scopus 로고
    • Origins of resistance conferred by the R292K neuraminidase mutation via molecular dynamics and free energy calculations
    • Chachra, R., & Rizzo, R. C. (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
  • 24
    • 46849105028 scopus 로고    scopus 로고
    • Ensemble-based virtual screening reveals potential novel antiviral compounds for avian influenza neuraminidase
    • Cheng, L. S., Amaro, R. E., Xu, D., Li, W. W., Arzberger, P. W., & McCammon, J. A. (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    McCammon, J.A.6
  • 25
    • 77956556232 scopus 로고    scopus 로고
    • Influenza hemagglutinin and neuraminidase membrane glycoproteins
    • Gamblin, S. J., & Skehel, J. J. (2010). Influenza hemagglutinin and neuraminidase membrane glycoproteins. The Journal of Biological Chemistry, 285, 28403-28409.
    • (2010) The Journal of Biological Chemistry , vol.285 , pp. 28403-28409
    • Gamblin, S.J.1    Skehel, J.J.2
  • 26
    • 33748437791 scopus 로고    scopus 로고
    • The structure of H5N1 avian influenza neuraminidase suggests new opportunities for drug design
    • Russell, R. J., Haire, L. F., Stevens, D. J., Collins, P. J., Lin, Y. P., Blackburn, G. M., 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    Blackburn, G.M.6
  • 27
    • 36749056771 scopus 로고    scopus 로고
    • The war against influenza: Discovery and development of sialidase inhibitors
    • Von Itzstein, M. (2007). The war against influenza: Discovery and development of sialidase inhibitors. Nature Reviews Drug Discovery, 6, 967-974.
    • (2007) Nature Reviews Drug Discovery , vol.6 , pp. 967-974
    • Von Itzstein, M.1
  • 28
    • 42449129769 scopus 로고    scopus 로고
    • Potential of mean force calculations of ligand binding to ion channels from Jarzynski's equality and umbrella sampling
    • Baştug, T., Chen, P. C., Patra, S. M., & Kuyucak, S. (2008). Potential of mean force calculations of ligand binding to ion channels from Jarzynski's equality and umbrella sampling. Journal of Chemical Physics, 128, 155104.
    • (2008) Journal of Chemical Physics , vol.128 , pp. 155104
    • Baştug, T.1    Chen, P.C.2    Patra, S.M.3    Kuyucak, S.4
  • 29
    • 78651282170 scopus 로고    scopus 로고
    • g_wham-A free weighted histogram analysis implementation including robust error and autocorrelation estimates
    • Hub, J. S., de Groot, B. L., & van der Spoel, D. (2010). g_wham-A free weighted histogram analysis implementation including robust error and autocorrelation estimates. Journal of Chemical Theory and Computation, 6, 3713-3720.
    • (2010) Journal of Chemical Theory and Computation , vol.6 , pp. 3713-3720
    • Hub, J.S.1    de Groot, B.L.2    van der Spoel, D.3
  • 31
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex, N., & Peitsch, M. C. (1997). SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling. Electrophoresis, 18, 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 32
    • 33344474627 scopus 로고    scopus 로고
    • A complete small molecule dataset from the protein data bank
    • Feldman, J., Snyder, K. A., Ticoll, A., Pintilie, G., & Hogue, C. W. (2006). A complete small molecule dataset from the protein data bank. FEBS Letters, 580, 1649-1653.
    • (2006) FEBS Letters , vol.580 , pp. 1649-1653
    • Feldman, J.1    Snyder, K.A.2    Ticoll, A.3    Pintilie, G.4    Hogue, C.W.5
  • 33
    • 31444452744 scopus 로고
    • Automatic generation of 3D-atomic coordinates for organic molecules
    • Gasteiger, J., Rudolph, C., & Sadowski, J. (1990). Automatic generation of 3D-atomic coordinates for organic molecules. Tetrahedron Computer Methodology, 3, 537-547.
    • (1990) Tetrahedron Computer Methodology , vol.3 , pp. 537-547
    • Gasteiger, J.1    Rudolph, C.2    Sadowski, J.3
  • 34
    • 34547575992 scopus 로고    scopus 로고
    • Firestar-Prediction of functionally important residues using structural templates and alignment reliability
    • Lopez, G., Valencia, A., & Tress, M. L. (2007). Firestar-Prediction of functionally important residues using structural templates and alignment reliability. Nucleic Acids Research, 35, 573-577.
    • (2007) Nucleic Acids Research , vol.35 , pp. 573-577
    • Lopez, G.1    Valencia, A.2    Tress, M.L.3
  • 35
    • 0020633096 scopus 로고
    • Structure of the catalytic and antigenic sites in influenza virus neuraminidase
    • Colman, P. M., Varghese, J. N., & Laver, W. G. (1983). Structure of the catalytic and antigenic sites in influenza virus neuraminidase. Nature, 303, 41-44.
    • (1983) Nature , vol.303 , pp. 41-44
    • Colman, P.M.1    Varghese, J.N.2    Laver, W.G.3
  • 36
    • 84555167532 scopus 로고    scopus 로고
    • Poster presentation: molecular docking using ArgusLab: An efficient shape-based search algorithm and the AScore scoring function
    • Philadelphia, PA
    • Thompson, M. A. (2004). Poster presentation: molecular docking using ArgusLab: An efficient shape-based search algorithm and the AScore scoring function. In Fall ACS Meeting, Philadelphia, PA.
    • (2004) Fall ACS Meeting
    • Thompson, M.A.1
  • 39
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess, B., Kutzner, C., Spoel, D., & Lindahl, E. (2008). GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation. Journal of Chemical Theory and Computation, 4, 435-447.
    • (2008) Journal of Chemical Theory and Computation , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Spoel, D.3    Lindahl, E.4
  • 42
    • 7544226311 scopus 로고    scopus 로고
    • PRODRG-a tool for high-throughput crystallography of protein-ligand complexes
    • Schuttelkopf, A. W., & van Aalten, D. M. F. (2004). PRODRG-a tool for high-throughput crystallography of protein-ligand complexes. Acta Crystallographica, 60, 1355-1363.
    • (2004) Acta Crystallographica , vol.60 , pp. 1355-1363
    • Schuttelkopf, A.W.1    van Aalten, D.M.F.2
  • 43
    • 0033104039 scopus 로고    scopus 로고
    • New tricks for modelers from the crystallography toolkit: The particle mesh Ewald algorithm and its use in nucleic acid simulations
    • Darden, T., Perera, L., Li, L., & Pedersen, L. (1999). New tricks for modelers from the crystallography toolkit: The particle mesh Ewald algorithm and its use in nucleic acid simulations. Structure, 7, 55-60.
    • (1999) Structure , vol.7 , pp. 55-60
    • Darden, T.1    Perera, L.2    Li, L.3    Pedersen, L.4
  • 44
    • 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
  • 47
    • 84866106043 scopus 로고    scopus 로고
    • Exploring the mechanism of zanamivir resistance in a neuraminidase mutant: A molecular dynamics study
    • Han, N., Liu, X., & Mu, Y. (2012). Exploring the mechanism of zanamivir resistance in a neuraminidase mutant: A molecular dynamics study. PLoS ONE, 7, e44057.
    • (2012) PLoS ONE , vol.7
    • Han, N.1    Liu, X.2    Mu, Y.3
  • 48
    • 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, J. N., Smith, P. W., Sollis, S. L., Blick, T. J., Sahasrabudhe, A., McKimm-Breschkin, J. L., et al. (1998). Drug design against a shifting target: A structural basis for resistance to inhibitors in a variant of influenza virus neuraminidase. Structure, 6, 735-746.
    • (1998) Structure , vol.6 , pp. 735-746
    • Varghese, J.N.1    Smith, P.W.2    Sollis, S.L.3    Blick, T.J.4    Sahasrabudhe, A.5    McKimm-Breschkin, J.L.6


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