메뉴 건너뛰기




Volumn 129, Issue 2, 2007, Pages 241-245

Characterization of human H1N1 influenza virus variants selected in vitro with zanamivir in the presence of sialic acid-containing molecules

Author keywords

Human influenza virus susceptibility; Neuraminidase inhibitor; Sialic acid containing molecules; Zanamivir in vitro selection

Indexed keywords

FETUIN; SIALIC ACID DERIVATIVE; SIALIDASE INHIBITOR; ZANAMIVIR;

EID: 35348821830     PISSN: 01681702     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.virusres.2007.07.010     Document Type: Article
Times cited : (8)

References (23)
  • 1
    • 4344672299 scopus 로고    scopus 로고
    • A reverse genetics study of resistance to neuraminidase inhibitors in an influenza A/H1N1 virus
    • Abed Y., Goyette N., and Boivin G. A reverse genetics study of resistance to neuraminidase inhibitors in an influenza A/H1N1 virus. Antivir. Ther. 9 (2004) 577-581
    • (2004) Antivir. Ther. , vol.9 , pp. 577-581
    • Abed, Y.1    Goyette, N.2    Boivin, G.3
  • 2
    • 3042866207 scopus 로고
    • The biologically active proteins of influenza virus: neuraminidase
    • Kilbourne E.D. (Ed), Academic Press, New York, NY
    • Bucher D., and Palese P. The biologically active proteins of influenza virus: neuraminidase. In: Kilbourne E.D. (Ed). The Influenza Viruses and Influenza (1975), Academic Press, New York, NY 83-123
    • (1975) The Influenza Viruses and Influenza , pp. 83-123
    • Bucher, D.1    Palese, P.2
  • 3
    • 0027243201 scopus 로고
    • Sequence and structure alignment of paramyxovirus hemagglutinin-neuraminidase with influenza virus neuraminidase
    • Colman P.M., Hoyne P.A., and Lawrence M.C. Sequence and structure alignment of paramyxovirus hemagglutinin-neuraminidase with influenza virus neuraminidase. J. Virol. 67 (1993) 2972-2980
    • (1993) J. Virol. , vol.67 , pp. 2972-2980
    • Colman, P.M.1    Hoyne, P.A.2    Lawrence, M.C.3
  • 4
    • 0026698245 scopus 로고
    • A solid-phase enzyme-linked assay for influenza virus receptor-binding activity
    • Gambaryan A.S., and Matrosovich M.N. A solid-phase enzyme-linked assay for influenza virus receptor-binding activity. J. Virol. Methods 39 (1992) 111-123
    • (1992) J. Virol. Methods , vol.39 , pp. 111-123
    • Gambaryan, A.S.1    Matrosovich, M.N.2
  • 5
    • 2442494839 scopus 로고    scopus 로고
    • Molecular mechanisms of influenza virus resistance to neuraminidase inhibitors
    • Gubareva L.V. Molecular mechanisms of influenza virus resistance to neuraminidase inhibitors. Virus Res. 103 (2004) 199-203
    • (2004) Virus Res. , vol.103 , pp. 199-203
    • Gubareva, L.V.1
  • 6
    • 0031724750 scopus 로고    scopus 로고
    • Evidence for zanamivir resistance in an immunocompromised child infected with influenza B virus
    • Gubareva L.V., Matrosovich M.N., Brenner M.K., Bethell R.C., and Webster R.G. Evidence for zanamivir resistance in an immunocompromised child infected with influenza B virus. J. Infect. Dis. 178 (1998) 1257-1262
    • (1998) J. Infect. Dis. , vol.178 , pp. 1257-1262
    • Gubareva, L.V.1    Matrosovich, M.N.2    Brenner, M.K.3    Bethell, R.C.4    Webster, R.G.5
  • 7
    • 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., and Hayden F.G. Selection of influenza virus mutants in experimentally infected volunteers treated with oseltamivir. J. Infect. Dis. 183 (2001) 523-531
    • (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
  • 8
    • 0036294323 scopus 로고    scopus 로고
    • The H274Y mutation in the influenza A/H1N1 neuraminidase active site following oseltamivir phosphate treatment leave virus severely compromised both in vitro and in vivo
    • Ives J.A., Carr J.A., Mendel D.B., Tai C.Y., Lambkin R., Kelly L., Oxford J.S., Hayden F.G., and Roberts N.A. The H274Y mutation in the influenza A/H1N1 neuraminidase active site following oseltamivir phosphate treatment leave virus severely compromised both in vitro and in vivo. Antiviral Res. 55 (2002) 307-317
    • (2002) Antiviral Res. , vol.55 , pp. 307-317
    • Ives, J.A.1    Carr, J.A.2    Mendel, D.B.3    Tai, C.Y.4    Lambkin, R.5    Kelly, L.6    Oxford, J.S.7    Hayden, F.G.8    Roberts, N.A.9
  • 9
    • 0037341410 scopus 로고    scopus 로고
    • Natural and synthetic sialic acid-containing inhibitors of influenza virus receptor binding
    • Matrosovich M., and Klenk H.-D. Natural and synthetic sialic acid-containing inhibitors of influenza virus receptor binding. Rev. Med. Virol. 13 (2003) 85-97
    • (2003) Rev. Med. Virol. , vol.13 , pp. 85-97
    • Matrosovich, M.1    Klenk, H.-D.2
  • 10
    • 7644241814 scopus 로고    scopus 로고
    • Neuraminidase is important for the initiation of influenza virus infection in human airway epithelium
    • Matrosovich M.N., Matrosovich T.Y., Gray T., Roberts N.A., and Klenk H.D. Neuraminidase is important for the initiation of influenza virus infection in human airway epithelium. J. Virol. 78 (2004) 12665-12667
    • (2004) J. Virol. , vol.78 , pp. 12665-12667
    • Matrosovich, M.N.1    Matrosovich, T.Y.2    Gray, T.3    Roberts, N.A.4    Klenk, H.D.5
  • 11
    • 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 J.L., Sahasrabudhe A., Blick T.J., McDonald M., Colman P.M., Hart G.J., Bethell R.C., and Varghese J.N. Mutations in a conserved residue in the influenza virus neuraminidase active site decreases sensitivity to Neu5Ac2en-derived inhibitors. J. Virol. 72 (1998) 2456-2462
    • (1998) J. Virol. , vol.72 , pp. 2456-2462
    • McKimm-Breschkin, J.L.1    Sahasrabudhe, A.2    Blick, T.J.3    McDonald, M.4    Colman, P.M.5    Hart, G.J.6    Bethell, R.C.7    Varghese, J.N.8
  • 14
    • 0018421350 scopus 로고
    • Fluorometric assay of neuraminidase with a sodium (4-methylumbelliferyl-alpha-d-N-acetylneuraminate) substrate
    • Potier M., Mameli L., Belisle M., Dallaire L., and Melancon S.B. Fluorometric assay of neuraminidase with a sodium (4-methylumbelliferyl-alpha-d-N-acetylneuraminate) substrate. Anal. Biochem. 94 (1979) 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
  • 16
    • 33645981586 scopus 로고    scopus 로고
    • Structure and receptor specificity of the hemagglutinin from an H5N1 influenza virus
    • Stevens J., Blixt O., Tumpey T.M., Taubenberger J.K., Paulson J.C., and Wilson I.A. Structure and receptor specificity of the hemagglutinin from an H5N1 influenza virus. Science 312 (2006) 404-410
    • (2006) Science , vol.312 , pp. 404-410
    • Stevens, J.1    Blixt, O.2    Tumpey, T.M.3    Taubenberger, J.K.4    Paulson, J.C.5    Wilson, I.A.6
  • 17
    • 21144441367 scopus 로고    scopus 로고
    • Sialobiology of influenza: molecular mechanism of host range variation of influenza viruses
    • Suzuki Y. Sialobiology of influenza: molecular mechanism of host range variation of influenza viruses. Biol. Pharm. Bull. 28 (2005) 399-408
    • (2005) Biol. Pharm. Bull. , vol.28 , pp. 399-408
    • Suzuki, Y.1
  • 18
    • 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 M.Z., Tai C.Y., and Mendel D.B. Mechanism by which mutations at his274 alter sensitivity of influenza a virus N1 neuraminidase to oseltamivir carboxylate and zanamivir. Antimicrob. Agents Chemother. 46 (2002) 3809-3816
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 3809-3816
    • Wang, M.Z.1    Tai, C.Y.2    Mendel, D.B.3
  • 19
    • 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 N.T., Trivedi T., Zeller J., Hodges-Savola C., McKimm-Breschkin J.L., Zambon M., and Hayden F.G. 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. 41 (2003) 742-750
    • (2003) J. Clin. Microbiol. , vol.41 , pp. 742-750
    • Wetherall, N.T.1    Trivedi, T.2    Zeller, J.3    Hodges-Savola, C.4    McKimm-Breschkin, J.L.5    Zambon, M.6    Hayden, F.G.7
  • 21
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution
    • Wilson I.A., Skehel J.J., and Wiley D.C. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution. Nature 289 (1981) 366-373
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 23
    • 33748645733 scopus 로고    scopus 로고
    • Importance of neuraminidase active-site residues to the neuraminidase inhibitor resistance of influenza viruses
    • Yen H.L., Hoffmann E., Taylor G., Scholtissek C., Monto A.S., Webster R.G., and Govorkova E.A. Importance of neuraminidase active-site residues to the neuraminidase inhibitor resistance of influenza viruses. J. Virol. 80 (2006) 8787-8795
    • (2006) J. Virol. , vol.80 , pp. 8787-8795
    • Yen, H.L.1    Hoffmann, E.2    Taylor, G.3    Scholtissek, C.4    Monto, A.S.5    Webster, R.G.6    Govorkova, E.A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.