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Volumn 258, Issue 2, 1998, Pages 320-331

Site-directed mutagenesis of catalytic residues of influenza virus neuraminidase as an aid to drug design

Author keywords

Active site mutants; Enzyme kinetics; Influenza virus; Neuraminidase

Indexed keywords

ARGININE; ASPARTIC ACID; GLUTAMIC ACID; GLYCOPROTEIN; SIALIC ACID; TYROSINE; VIRUS SIALIDASE;

EID: 0032401593     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2580320.x     Document Type: Article
Times cited : (52)

References (44)
  • 1
    • 0028813628 scopus 로고
    • Influenza type a virus neuraminidase does not play a role in viral entry, replication, assembly or budding
    • Liu, C., Eichelberger, M. C., Compans, R. W. & Air, G. M. (1995) Influenza type A virus neuraminidase does not play a role in viral entry, replication, assembly or budding, J. Virol. 69, 1099-1106.
    • (1995) J. Virol. , vol.69 , pp. 1099-1106
    • Liu, C.1    Eichelberger, M.C.2    Compans, R.W.3    Air, G.M.4
  • 2
    • 0016272701 scopus 로고
    • Characterization of temperature-sensitive influenza virus mutants defective in neuraminidase
    • Palese, P., Tobita, K., Ueda, M. & Compans, R. W. (1974) Characterization of temperature-sensitive influenza virus mutants defective in neuraminidase, Virology 61, 397-410.
    • (1974) Virology , vol.61 , pp. 397-410
    • Palese, P.1    Tobita, K.2    Ueda, M.3    Compans, R.W.4
  • 5
    • 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., Bischofberger, N., Chen, M. S., Mendel, D. B., Tai, C. Y., Laver, W. G. & Stevens, R. C. (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, J. Am. Chem. Soc. 119, 681-690.
    • (1997) J. Am. Chem. Soc. , 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    Bischofberger, N.7    Chen, M.S.8    Mendel, D.B.9    Tai, C.Y.10    Laver, W.G.11    Stevens, R.C.12
  • 6
    • 0029099621 scopus 로고
    • Structure-based inhibitors of Influenza virus sialidase. A benzoic acid lead with novel interaction
    • Singh, S., Jedrzejas, M. J., Air, G. M., Luo, M., Laver, W. G. & Brouillette, W. J. (1995) Structure-based inhibitors of Influenza virus sialidase. A benzoic acid lead with novel interaction, J. Med. Chem. 38, 3217-3225.
    • (1995) J. Med. Chem. , vol.38 , pp. 3217-3225
    • Singh, S.1    Jedrzejas, M.J.2    Air, G.M.3    Luo, M.4    Laver, W.G.5    Brouillette, W.J.6
  • 8
    • 0027930960 scopus 로고
    • Structure of influenza virus neuraminidase B/Lee/40 complexed with sialic acid and a dehydro-analog at 1.8 Å resolution: Implications for the catalytic mechanism
    • Janakiraman, M. N., White, C. L., Laver, W. G., Air, G. M. & Luo, M. (1994) Structure of influenza virus neuraminidase B/Lee/40 complexed with sialic acid and a dehydro-analog at 1.8 Å resolution: implications for the catalytic mechanism, Biochemistry 33, 8172-8179.
    • (1994) Biochemistry , vol.33 , pp. 8172-8179
    • Janakiraman, M.N.1    White, C.L.2    Laver, W.G.3    Air, G.M.4    Luo, M.5
  • 9
    • 0027292125 scopus 로고
    • Three-dimensional structure of influenza A N9 neuraminidase and its complex with the inhibitor 2-deoxy 2,3-dehydro-N-acetyl neuraminic acid
    • Bossart-Whitaker, P., Carson, M., Babu, Y. S., Smith, C. D., Laver, W. G. & Air, G. M. (1993) Three-dimensional structure of influenza A N9 neuraminidase and its complex with the inhibitor 2-deoxy 2,3-dehydro-N-acetyl neuraminic acid, J. Mol. Biol. 232, 1069-1083.
    • (1993) J. Mol. Biol. , vol.232 , pp. 1069-1083
    • Bossart-Whitaker, P.1    Carson, M.2    Babu, Y.S.3    Smith, C.D.4    Laver, W.G.5    Air, G.M.6
  • 10
    • 0026508847 scopus 로고
    • The 2.2 Å resolution crystal structure of influenza B neuraminidase and its complex with sialic acid
    • Burmeister, W. P., Ruigrok, R. W. & Cusack, S. (1992) The 2.2 Å resolution crystal structure of influenza B neuraminidase and its complex with sialic acid, EMBO J. 11, 49-56.
    • (1992) EMBO J. , vol.11 , pp. 49-56
    • Burmeister, W.P.1    Ruigrok, R.W.2    Cusack, S.3
  • 11
    • 0026755388 scopus 로고
    • Evidence for a sialosyl cation transition-state complex in the reaction of sialidase from influenza virus
    • Chong, A. K., Pegg, M. S., Taylor, N. R. & von Itzstein, M. (1992) Evidence for a sialosyl cation transition-state complex in the reaction of sialidase from influenza virus, Eur. J. Biochem. 207, 335-343.
    • (1992) Eur. J. Biochem. , vol.207 , pp. 335-343
    • Chong, A.K.1    Pegg, M.S.2    Taylor, N.R.3    Von Itzstein, M.4
  • 12
    • 0028325249 scopus 로고
    • Molecular modeling studies on ligand binding to sialidase from influenza virus and the mechanism of catalysis
    • Taylor, N. R. & von Itzstein, M. (1994) Molecular modeling studies on ligand binding to sialidase from influenza virus and the mechanism of catalysis, J. Med. Chem. 37, 616-624.
    • (1994) J. Med. Chem. , vol.37 , pp. 616-624
    • Taylor, N.R.1    Von Itzstein, M.2
  • 13
    • 0023101787 scopus 로고
    • Effects of site-specific mutation on structure and activity of influenza virus B/Lee/40 neuraminidase
    • Wei, X., Els, M. C., Webster, R. G. & Air, G. M. (1987) Effects of site-specific mutation on structure and activity of influenza virus B/Lee/40 neuraminidase, Virology 156, 253-258.
    • (1987) Virology , vol.156 , pp. 253-258
    • Wei, X.1    Els, M.C.2    Webster, R.G.3    Air, G.M.4
  • 14
    • 0025312399 scopus 로고
    • Antigenic, sequence and crystal variation in influenza B neuraminidase
    • Air, G. M., Laver, W. G., Luo, M., Stray, S. J., Legrone, G. & Webster, R. G. (1990) Antigenic, sequence and crystal variation in influenza B neuraminidase, Virology 177, 578-587.
    • (1990) Virology , vol.177 , pp. 578-587
    • Air, G.M.1    Laver, W.G.2    Luo, M.3    Stray, S.J.4    Legrone, G.5    Webster, R.G.6
  • 15
    • 0020971324 scopus 로고
    • Oligonucleotide-directed mutagenesis of DNA fragments cloned into M13 vectors
    • Zoller, M. & Smith, M. (1983) Oligonucleotide-directed mutagenesis of DNA fragments cloned into M13 vectors, Methods Enzymol. 100, 468-500.
    • (1983) Methods Enzymol. , vol.100 , pp. 468-500
    • Zoller, M.1    Smith, M.2
  • 16
    • 0025769402 scopus 로고
    • Transfer of the hemagglutinin activity of influenza virus neuraminidase subtype N9 into an N2 background
    • Nuss, J. M. & Air, G. M. (1991) Transfer of the hemagglutinin activity of influenza virus neuraminidase subtype N9 into an N2 background, Virology 183, 496-504.
    • (1991) Virology , vol.183 , pp. 496-504
    • Nuss, J.M.1    Air, G.M.2
  • 18
    • 0000233999 scopus 로고
    • Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase
    • Fuerst, T. R., Niles, E. G., Studier, F. W. & Moss, B. (1986) Eukaryotic transient-expression system based on recombinant vaccinia virus that synthesizes bacteriophage T7 RNA polymerase, Proc. Natl Acad. Sci. USA 83, 8122-8126.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 8122-8126
    • Fuerst, T.R.1    Niles, E.G.2    Studier, F.W.3    Moss, B.4
  • 19
    • 0018421350 scopus 로고
    • Fluorometric assay of neuraminidase with a sodium (4-methylumbelliferyl)-α-D-N-acetylneuraminate substrate
    • Potier, M., Mameli, L., Belisle, M., Dallaire, L. & Melancon, S. B. (1979) Fluorometric assay of neuraminidase with a sodium (4-methylumbelliferyl)-α-D-N-acetylneuraminate substrate, Anal. Biochem. 94, 287-296.
    • (1979) Anal. Biochem. , vol.94 , pp. 287-296
    • Potier, M.1    Mameli, L.2    Belisle, M.3    Dallaire, L.4    Melancon, S.B.5
  • 20
    • 0023664836 scopus 로고
    • Site-directed mutation of the active site of influenza neuraminidase and implications for the catalytic mechanism
    • Lentz, M. R., Webster, R. G. & Air, G. M. (1987) Site-directed mutation of the active site of influenza neuraminidase and implications for the catalytic mechanism, Biochemistry 26, 5351-5358.
    • (1987) Biochemistry , vol.26 , pp. 5351-5358
    • Lentz, M.R.1    Webster, R.G.2    Air, G.M.3
  • 21
    • 0018001498 scopus 로고
    • m values of Influenza virus neuraminidases for a new fluorogenic substrate, 4-methylumbelliferone N-acetyl neuraminic acid ketoside
    • m values of Influenza virus neuraminidases for a new fluorogenic substrate, 4-methylumbelliferone N-acetyl neuraminic acid ketoside, Anal. Biochem. 88, 461-467.
    • (1978) Anal. Biochem. , vol.88 , pp. 461-467
    • Thomas, J.J.1    Folger, E.C.2    Nist, D.L.3    Thomas, B.J.4    Jones, R.H.5
  • 22
    • 0022658320 scopus 로고
    • Loss of enzyme activity in a sitedirected mutant of influenza neuraminidase compared to expressed wild-type protein
    • Lentz, M. R. & Air, G. M. (1986) Loss of enzyme activity in a sitedirected mutant of influenza neuraminidase compared to expressed wild-type protein, Virology 148, 74-83.
    • (1986) Virology , vol.148 , pp. 74-83
    • Lentz, M.R.1    Air, G.M.2
  • 23
    • 0018092715 scopus 로고
    • Crystallization and peptide maps of neuraminidase 'heads' from H2N2 and H3N2 influenza virus strains
    • Laver, W. G. (1978) Crystallization and peptide maps of neuraminidase 'heads' from H2N2 and H3N2 influenza virus strains, Virology 86, 78-87.
    • (1978) Virology , vol.86 , pp. 78-87
    • Laver, W.G.1
  • 24
    • 0024846089 scopus 로고
    • Amplification, expression, and packaging of a foreign gene by influenza virus
    • Luytjes, W., Krystal, M., Enami, M., Parvin, J. D. & Palese, P. (1989) Amplification, expression, and packaging of a foreign gene by influenza virus, Cell 59, 1107-1113.
    • (1989) Cell , vol.59 , pp. 1107-1113
    • Luytjes, W.1    Krystal, M.2    Enami, M.3    Parvin, J.D.4    Palese, P.5
  • 25
    • 0025895628 scopus 로고
    • Three-dimensional structure of the neuraminidase of influenza virus A/Tokyo/3/67 at 2.2 Å resolution
    • Varghese, J. N. & Colman, P. M. (1991) Three-dimensional structure of the neuraminidase of influenza virus A/Tokyo/3/67 at 2.2 Å resolution, J. Mol. Biol. 221, 473-486.
    • (1991) J. Mol. Biol. , vol.221 , pp. 473-486
    • Varghese, J.N.1    Colman, P.M.2
  • 26
    • 0027521664 scopus 로고
    • Salmonella typhimurium neuraminidase acts with inversion of configuration
    • Guo, X. & Sinnott, M. (1993) Salmonella typhimurium neuraminidase acts with inversion of configuration, Biochem. J. 296, 291-292.
    • (1993) Biochem. J. , vol.296 , pp. 291-292
    • Guo, X.1    Sinnott, M.2
  • 27
    • 0027364312 scopus 로고
    • Crystal structure of a bacterial sialidase (from Salmonella typhimurium LT2) shows the same fold as an influenza virus neuraminidase
    • Crennell, S. J., Garman, E. F., Laver, W. G., Vimr, E. R. & Taylor, G. L. (1993) Crystal structure of a bacterial sialidase (from Salmonella typhimurium LT2) shows the same fold as an influenza virus neuraminidase, Proc. Natl Acad. Sci. USA 90, 9852-9856.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 9852-9856
    • Crennell, S.J.1    Garman, E.F.2    Laver, W.G.3    Vimr, E.R.4    Taylor, G.L.5
  • 28
    • 0028773635 scopus 로고
    • Crystal structure of Vibrio cholerae neuraminidase reveals dual lectin-like domains in addition to the catalytic domain
    • Crennell, S., Garman, E., Laver, G., Vimr, E. & Taylor, G. (1994) Crystal structure of Vibrio cholerae neuraminidase reveals dual lectin-like domains in addition to the catalytic domain, Structure 2, 535-544.
    • (1994) Structure , vol.2 , pp. 535-544
    • Crennell, S.1    Garman, E.2    Laver, G.3    Vimr, E.4    Taylor, G.5
  • 29
    • 0018167605 scopus 로고
    • Mechanism of Arthrobacter sialophilus neuraminidase: The binding of substrates and transition-state analogs
    • Miller, C. A., Wang, P. & Flashner, M. (1978) Mechanism of Arthrobacter sialophilus neuraminidase: The binding of substrates and transition-state analogs, Biochem. Biophys. Res. Commun. 83, 1479-1487.
    • (1978) Biochem. Biophys. Res. Commun. , vol.83 , pp. 1479-1487
    • Miller, C.A.1    Wang, P.2    Flashner, M.3
  • 30
    • 0025830606 scopus 로고
    • Characterisation of an ionisable group involved in binding and catalysis by sialidase from influenza virus
    • Chong, A. K., Pegg, M. S. & von Itzstein, M. (1991) Characterisation of an ionisable group involved in binding and catalysis by sialidase from influenza virus, Biochem. Int. 24, 165-171.
    • (1991) Biochem. Int. , vol.24 , pp. 165-171
    • Chong, A.K.1    Pegg, M.S.2    Von Itzstein, M.3
  • 31
    • 0028082996 scopus 로고
    • Catalysis by two sialidases with the same protein fold but different stereo-chemical courses: A mechanistic comparison of the enzymes from Influenza A virus and Salmonella typhimurium
    • Guo, X., Laver, W. G., Vimr, E. & Sinnott, M. (1994) Catalysis by two sialidases with the same protein fold but different stereo-chemical courses: a mechanistic comparison of the enzymes from Influenza A virus and Salmonella typhimurium, J. Am. Chem. Soc. 116, 5572-5578.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 5572-5578
    • Guo, X.1    Laver, W.G.2    Vimr, E.3    Sinnott, M.4
  • 32
    • 0029149686 scopus 로고
    • Effect of substrate aglycon on enzyme mechanism in the reaction of sialidase from influenza virus
    • Tiralongo, J., Pegg, M. S. & von Itzstein, M. (1995) Effect of substrate aglycon on enzyme mechanism in the reaction of sialidase from influenza virus, FEBS Lett. 372, 148-150.
    • (1995) FEBS Lett. , vol.372 , pp. 148-150
    • Tiralongo, J.1    Pegg, M.S.2    Von Itzstein, M.3
  • 33
    • 0026665418 scopus 로고
    • The structure of the complex between influenza virus neuraminidase and sialic acid, the viral receptor
    • Varghese, J. N., McKimm-Breschkin, J. L., Caldwell, J. B., Kortt, A. A. & Colman, P. M. (1992) The structure of the complex between influenza virus neuraminidase and sialic acid, the viral receptor, Proteins 14, 327-332.
    • (1992) Proteins , vol.14 , pp. 327-332
    • Varghese, J.N.1    McKimm-Breschkin, J.L.2    Caldwell, J.B.3    Kortt, A.A.4    Colman, P.M.5
  • 35
    • 0024394652 scopus 로고
    • Kinetic studies on the sialidase of three influenza B and three influenza A virus strains
    • Cabezas, R. A., Milicua, M., Bernal, C. S., Villar, E., Perez, N. & Hannoun, C. (1989) Kinetic studies on the sialidase of three influenza B and three influenza A virus strains, Glycoconjugate J. 6, 219-227.
    • (1989) Glycoconjugate J. , vol.6 , pp. 219-227
    • Cabezas, R.A.1    Milicua, M.2    Bernal, C.S.3    Villar, E.4    Perez, N.5    Hannoun, C.6
  • 36
    • 0030028671 scopus 로고    scopus 로고
    • Characterization of mutants of Influenza A virus selected with the neuraminidase inhibitor 4-Guanidino-Neu5Ac2en
    • Gubareva, L. V., Bethell, R., Hart, G. J., Murti, K. G., Penn, C. R. & Webster, R. G. (1996) Characterization of mutants of Influenza A virus selected with the neuraminidase inhibitor 4-Guanidino-Neu5Ac2en, J. Virol. 70, 1818-1827.
    • (1996) J. Virol. , vol.70 , pp. 1818-1827
    • Gubareva, L.V.1    Bethell, R.2    Hart, G.J.3    Murti, K.G.4    Penn, C.R.5    Webster, R.G.6
  • 38
    • 0000024891 scopus 로고    scopus 로고
    • Selection of influenza virus with reduced sensitivity in vitro to the neuraminidase inhibitor GG167 (4-guanidino-Neu5Ac2en): Changes in hemagglutinin may compensate for loss of neuraminidase activity
    • Brown, L., Hampson, A. & Webster, R., eds
    • Penn, C. R., Barnett, J. M., Bethell, R. C., Fenton, R., Gearing, K. L., Healy, N. & Jowett, A. J. (1996) Selection of influenza virus with reduced sensitivity in vitro to the neuraminidase inhibitor GG167 (4-guanidino-Neu5Ac2en): Changes in hemagglutinin may compensate for loss of neuraminidase activity, in Options for the control of influenza III (Brown, L., Hampson, A. & Webster, R., eds) pp. 735-740.
    • (1996) Options for the Control of Influenza III , pp. 735-740
    • Penn, C.R.1    Barnett, J.M.2    Bethell, R.C.3    Fenton, R.4    Gearing, K.L.5    Healy, N.6    Jowett, A.J.7
  • 40
    • 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, J. L., McDonald, M., Blick, T. J. & Colman, P. M. (1996) 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 225, 240-242.
    • (1996) Virology , vol.225 , pp. 240-242
    • McKimm-Breschkin, J.L.1    McDonald, M.2    Blick, T.J.3    Colman, P.M.4
  • 41
    • 0029003145 scopus 로고
    • Three-dimensional structure of the complex of 4-guanidino-Neu5Ac2en and influenza virus neuraminidase
    • Varghese, J. N., Epa, V. C. & Colman, P. M. (1995) Three-dimensional structure of the complex of 4-guanidino-Neu5Ac2en and influenza virus neuraminidase, Protein Science 4, 1081-1087.
    • (1995) Protein Science , vol.4 , pp. 1081-1087
    • Varghese, J.N.1    Epa, V.C.2    Colman, P.M.3
  • 44
    • 0031956393 scopus 로고    scopus 로고
    • Generation and characterization of a mutant of Influenza A virus selected with the neuraminidase inhibitor BCX-140
    • Bantia, S., Ghate, A. A., Ananth, S. L., Babu, Y. S., Air, G. M. & Walsh, G. M. (1998) Generation and characterization of a mutant of Influenza A virus selected with the neuraminidase inhibitor BCX-140, Antimicrob. Agents Chemother. 42, 801-807.
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 801-807
    • Bantia, S.1    Ghate, A.A.2    Ananth, S.L.3    Babu, Y.S.4    Air, G.M.5    Walsh, G.M.6


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