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Volumn 443, Issue 7107, 2006, Pages 45-49

The structure of H5N1 avian influenza neuraminidase suggests new opportunities for drug design

Author keywords

[No Author keywords available]

Indexed keywords

DRUG PRODUCTS; MOLECULAR STRUCTURE; PATIENT TREATMENT; VIRUSES; X RAY CRYSTALLOGRAPHY;

EID: 33748437791     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature05114     Document Type: Article
Times cited : (741)

References (34)
  • 1
    • 0004250845 scopus 로고    scopus 로고
    • (eds Fields, D. B. N., Knipe, M. & Howley, P. M.) (Lippincott-Raven, Philadelphia)
    • Murphy, B. R. & Webster, R. G. in Fields Virology 3rd edn (eds Fields, D. B. N., Knipe, M. & Howley, P. M.) 1397-1445 (Lippincott-Raven, Philadelphia, 1996).
    • (1996) Fields Virology 3rd Edn. , pp. 1397-1445
    • Murphy, B.R.1    Webster, R.G.2
  • 2
    • 0019119577 scopus 로고
    • A revision of the system of nomenclature for influenza viruses: A WHO memorandum
    • World Health Organization. A revision of the system of nomenclature for influenza viruses: a WHO memorandum. Bull. World Health Organ. 58, 585-591 (1980).
    • (1980) Bull. World Health Organ. , vol.58 , pp. 585-591
  • 3
    • 0033080392 scopus 로고    scopus 로고
    • Characterization of the surface proteins of influenza a (H5N1) viruses isolated from humans in 1997-1998
    • Bender, C. et al. Characterization of the surface proteins of influenza A (H5N1) viruses isolated from humans in 1997-1998. Virology 254, 115-123 (1999).
    • (1999) Virology , vol.254 , pp. 115-123
    • Bender, C.1
  • 4
    • 25644439259 scopus 로고    scopus 로고
    • Evolution of H5N1 avian influenza viruses in Asia
    • World Health Organization Global Influenza Program Surveillance Network. Evolution of H5N1 avian influenza viruses in Asia. Emerg. Infect. Dis. 11, 1515-1521 (2005).
    • (2005) Emerg. Infect. Dis. , vol.11 , pp. 1515-1521
  • 5
    • 0028013177 scopus 로고
    • Improved sensitivity of profile searches through the use of sequence weights and gap excision
    • Thompson, J. D., Higgins, D. G. & Gibson, T. J. Improved sensitivity of profile searches through the use of sequence weights and gap excision. Comput. Appl. Biosci. 10, 19-29 (1994).
    • (1994) Comput. Appl. Biosci. , vol.10 , pp. 19-29
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 6
    • 0027287506 scopus 로고
    • Rational design of potent sialidase-based inhibitors of influenza virus replication
    • von Itzstein, M. et al. Rational design of potent sialidase-based inhibitors of influenza virus replication. Nature 363, 418-423 (1993).
    • (1993) Nature , vol.363 , pp. 418-423
    • Von Itzstein, M.1
  • 7
    • 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. 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. 119, 681-690 (1997).
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 681-690
    • Kim, C.U.1
  • 8
    • 0020629047 scopus 로고
    • Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 Å resolution
    • Varghese, J. N., Laver, W. G. & Colman, P. M. Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 Å resolution. Nature 303, 35-40 (1983).
    • (1983) Nature , vol.303 , pp. 35-40
    • Varghese, J.N.1    Laver, W.G.2    Colman, P.M.3
  • 9
    • 0023475950 scopus 로고
    • Three-dimensional structure of neuraminidase of subtype N9 from an avian influenza virus
    • Baker, A. T., Varghese, J. N., Laver, W. G., Air, G. M. & Colman, P. M. Three-dimensional structure of neuraminidase of subtype N9 from an avian influenza virus. Proteins 2, 111-117 (1987).
    • (1987) Proteins , vol.2 , pp. 111-117
    • Baker, A.T.1    Varghese, J.N.2    Laver, W.G.3    Air, G.M.4    Colman, P.M.5
  • 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. The 2.2 Å resolution crystal structure of influenza B neuraminidase and its complex with sialic acid. EMBO J. 11, 49-56 (1992).
    • (1992) EMBO J. , vol.11 , pp. 49-56
    • Burmeister, W.P.1    Ruigrok, R.W.2    Cusack, S.3
  • 11
    • 0003178444 scopus 로고    scopus 로고
    • Anti-viral drug resistance: An oseltamivir treatment-selected influenza A/N2 virus with a R292K mutation in the neuraminidase gene has reduced infectivity in vivo
    • Ives, J. et al. Anti-viral drug resistance: an oseltamivir treatment-selected influenza A/N2 virus with a R292K mutation in the neuraminidase gene has reduced infectivity in vivo. J. Clin. Virol. 18, 251-269 (2000).
    • (2000) J. Clin. Virol. , vol.18 , pp. 251-269
    • Ives, J.1
  • 12
    • 0035865919 scopus 로고    scopus 로고
    • Selection of influenza virus mutants in experimentally infected volunteers treated with oseltamivir
    • Gubareva, L. V., Kaiser, L., Matrosovich, M. N., Soo-Hoo, Y. & Hayden, F. G. Selection of influenza virus mutants in experimentally infected volunteers treated with oseltamivir. J. Infect. Dis. 183, 523-531 (2001).
    • (2001) J. Infect. Dis. , vol.183 , pp. 523-531
    • Gubareva, L.V.1    Kaiser, L.2    Matrosovich, M.N.3    Soo-Hoo, Y.4    Hayden, F.G.5
  • 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. et al. 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 Res. 54, 79-88 (2002).
    • (2002) Antiviral Res. , vol.54 , pp. 79-88
    • Carr, J.1
  • 14
    • 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., Suter, P. & Dutkowski, R. Oseltamivir (Tamiflu) and its potential for use in the event of an influenza pandemic. J. Antimicrob. Chemother. 55 (suppl. 1), i5-i21 (2005).
    • (2005) J. Antimicrob. Chemother. , vol.55 , Issue.SUPPL. 1
    • Ward, P.1    Small, I.2    Smith, J.3    Suter, P.4    Dutkowski, R.5
  • 15
    • 0038209544 scopus 로고    scopus 로고
    • Pyrrolidinobenzoic acid inhibitors of influenza virus neuraminidase: Modifications of essential pyrrolidinone ring substituents
    • Brouillette, W. J. et al. Pyrrolidinobenzoic acid inhibitors of influenza virus neuraminidase: modifications of essential pyrrolidinone ring substituents. Bioorg. Med. Chem. 11, 2739-2749 (2003).
    • (2003) Bioorg. Med. Chem. , vol.11 , pp. 2739-2749
    • Brouillette, W.J.1
  • 17
    • 0020633096 scopus 로고
    • Structure of the catalytic and antigenic sites in influenza virus neuraminidase
    • Colman, P. M., Varghese, J. N. & Laver, W. G. Structure of the catalytic and antigenic sites in influenza virus neuraminidase. Nature 303, 41-44 (1983).
    • (1983) Nature , vol.303 , pp. 41-44
    • Colman, P.M.1    Varghese, J.N.2    Laver, W.G.3
  • 18
    • 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. et al. 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).
    • (1993) J. Mol. Biol. , vol.232 , pp. 1069-1083
    • Bossart-Whitaker, P.1
  • 20
    • 0015959249 scopus 로고
    • Inhibition of neuraminidase activity by derivatives of 2-deoxy-2,3-dehydro-N-acetylneuraminic acid
    • Meindl, P., Bodo, G., Palese, P., Schulman, J. & Tuppy, H. Inhibition of neuraminidase activity by derivatives of 2-deoxy-2,3-dehydro-N- acetylneuraminic acid. Virology 58, 457-463 (1974).
    • (1974) Virology , vol.58 , pp. 457-463
    • Meindl, P.1    Bodo, G.2    Palese, P.3    Schulman, J.4    Tuppy, H.5
  • 21
    • 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, Y. 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. 43, 3482-3486 (2000).
    • (2000) J. Med. Chem. , vol.43 , pp. 3482-3486
    • Babu, Y.S.1
  • 22
    • 27644439501 scopus 로고    scopus 로고
    • Susceptibilities of antiviral-resistant influenza viruses to novel neuraminidase inhibitors
    • Mishin, V. P., Hayden, F. G. & Gubareva, L. V. Susceptibilities of antiviral-resistant influenza viruses to novel neuraminidase inhibitors. Antimicrob. Agents Chemother. 49, 4515-4520 (2005).
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 4515-4520
    • Mishin, V.P.1    Hayden, F.G.2    Gubareva, L.V.3
  • 23
    • 0036894107 scopus 로고    scopus 로고
    • Mechanism by which mutations at His 274 alter sensitivity of influenza a virus N1 neuraminidase to oseltamivir carboxylate and zanamivir
    • Wang, M. Z., Tai, C. Y. & Mendel, D. B. Mechanism by which mutations at His 274 alter sensitivity of influenza A virus N1 neuraminidase to oseltamivir carboxylate and zanamivir. Antimicrob. Agents Chemother. 46, 3809-3816 (2002).
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 3809-3816
    • Wang, M.Z.1    Tai, C.Y.2    Mendel, D.B.3
  • 24
    • 25844474747 scopus 로고    scopus 로고
    • Neuraminidase inhibitor-resistant influenza viruses may differ substantially in fitness and transmissibility
    • Yen, H. L. et al. Neuraminidase inhibitor-resistant influenza viruses may differ substantially in fitness and transmissibility. Antimicrob. Agents Chemother. 49, 4075-4084 (2005).
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 4075-4084
    • Yen, H.L.1
  • 25
    • 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. et al. 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).
    • (1998) Structure , vol.6 , pp. 735-746
    • Varghese, J.N.1
  • 26
    • 27144468290 scopus 로고    scopus 로고
    • Avian flu: Isolation of drug-resistant H5N1 virus
    • Le, Q. M. et al. Avian flu: isolation of drug-resistant H5N1 virus. Nature 437, 1108 (2005).
    • (2005) Nature , vol.437 , pp. 1108
    • Le, Q.M.1
  • 27
    • 4444369826 scopus 로고    scopus 로고
    • Resistant influenza A viruses in children treated with oseltamivir: Descriptive study
    • Kiso, M. et al. Resistant influenza A viruses in children treated with oseltamivir: descriptive study. Lancet 364, 759-765 (2004).
    • (2004) Lancet , vol.364 , pp. 759-765
    • Kiso, M.1
  • 28
    • 29144528757 scopus 로고    scopus 로고
    • Oseltamivir resistance during treatment of influenza A (H5N1) infection
    • de Jong, M. D. et al. Oseltamivir resistance during treatment of influenza A (H5N1) infection. N. Engl. J. Med. 353, 2667-2672 (2005).
    • (2005) N. Engl. J. Med. , vol.353 , pp. 2667-2672
    • De Jong, M.D.1
  • 29
    • 27144431628 scopus 로고    scopus 로고
    • Transmission of equine influenza virus to dogs
    • Crawford, P. C. et al. Transmission of equine influenza virus to dogs. Science 310, 482-485 (2005).
    • (2005) Science , vol.310 , pp. 482-485
    • Crawford, P.C.1
  • 30
    • 0035949581 scopus 로고    scopus 로고
    • X-ray structures of H5 avian and H9 swine influenza virus hemagglutinins bound to avian and human receptor analogs
    • Ha, Y., Stevens, D. J., Skehel, J. J. & Wiley, D. C. X-ray structures of H5 avian and H9 swine influenza virus hemagglutinins bound to avian and human receptor analogs. Proc. Natl Acad. Sci. USA 98, 11181-11186 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 11181-11186
    • Ha, Y.1    Stevens, D.J.2    Skehel, J.J.3    Wiley, D.C.4
  • 31
    • 0003976860 scopus 로고
    • (eds Sawyer, L., Isaacs, N. & Bailey, S.) (SERC Daresbury Laboratory, Warrington)
    • Otwinowski, Z. & Minor, W. in Data Collection and Processing (eds Sawyer, L., Isaacs, N. & Bailey, S.) 556-562 (SERC Daresbury Laboratory, Warrington, 1993).
    • (1993) Data Collection and Processing , pp. 556-562
    • Otwinowski, Z.1    Minor, W.2
  • 32
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr D 50, 760-763 (1994).
    • (1994) Acta Crystallogr D , vol.50 , pp. 760-763
  • 33
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brunger, A. T. et al. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brunger, A.T.1
  • 34
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zhou, J. Y., Cowan, S. W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zhou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4


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