메뉴 건너뛰기




Volumn 237, Issue , 2016, Pages 192-199

Platform for determining the inhibition profile of neuraminidase inhibitors in an influenza virus N1 background

Author keywords

Antiviral; Drug design; Enzyme kinetics; Fitness; Resistance; Susceptibility

Indexed keywords

AMINO ACID; OSELTAMIVIR; SIALIDASE INHIBITOR; ZANAMIVIR; ENZYME INHIBITOR; SIALIDASE; VIRAL PROTEIN;

EID: 84988836003     PISSN: 01660934     EISSN: 18790984     Source Type: Journal    
DOI: 10.1016/j.jviromet.2016.09.014     Document Type: Article
Times cited : (5)

References (51)
  • 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., 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
    • 33845637926 scopus 로고    scopus 로고
    • Impact of neuraminidase mutations conferring influenza resistance to neuraminidase inhibitors in the N1 and N2 genetic backgrounds
    • Abed, Y., Baz, M., Boivin, G., Impact of neuraminidase mutations conferring influenza resistance to neuraminidase inhibitors in the N1 and N2 genetic backgrounds. Antivir. Ther. 11 (2006), 971–976.
    • (2006) Antivir. Ther. , vol.11 , pp. 971-976
    • Abed, Y.1    Baz, M.2    Boivin, G.3
  • 3
    • 84892467702 scopus 로고    scopus 로고
    • Impact of potential permissive neuraminidase mutations on viral fitness of the H275Y oseltamivir-resistant influenza A (H1N1) pdm09 virus in vitro, in mice and in ferrets
    • Abed, Y., Pizzorno, A., Bouhy, X., Rhéaume, C., Boivin, G., Impact of potential permissive neuraminidase mutations on viral fitness of the H275Y oseltamivir-resistant influenza A (H1N1) pdm09 virus in vitro, in mice and in ferrets. J. Virol. 88 (2014), 1652–1658.
    • (2014) J. Virol. , vol.88 , pp. 1652-1658
    • Abed, Y.1    Pizzorno, A.2    Bouhy, X.3    Rhéaume, C.4    Boivin, G.5
  • 4
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling
    • Arnold, K., Bordoli, L., Kopp, J., Schwede, T., The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 22 (2006), 195–201.
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 7
    • 77953262416 scopus 로고    scopus 로고
    • Permissive secondary mutations enable the evolution of influenza oseltamivir resistance
    • Bloom, J.D., Gong, L.I., Baltimore, D., Permissive secondary mutations enable the evolution of influenza oseltamivir resistance. Science 328 (2010), 1272–1275.
    • (2010) Science , vol.328 , pp. 1272-1275
    • Bloom, J.D.1    Gong, L.I.2    Baltimore, D.3
  • 8
    • 79951529603 scopus 로고    scopus 로고
    • Pandemic H1N1 2009 influenza virus with the H275Y oseltamivir resistance neuraminidase mutation shows a small compromise in enzyme activity and viral fitness
    • Brookes, D.W., Miah, S., Lackenby, A., Hartgroves, L., Barclay, W.S., Pandemic H1N1 2009 influenza virus with the H275Y oseltamivir resistance neuraminidase mutation shows a small compromise in enzyme activity and viral fitness. J. Antimicrob. Chemother. 66 (2010), 466–470.
    • (2010) J. Antimicrob. Chemother. , vol.66 , pp. 466-470
    • Brookes, D.W.1    Miah, S.2    Lackenby, A.3    Hartgroves, L.4    Barclay, W.S.5
  • 10
    • 84893107987 scopus 로고    scopus 로고
    • Comparative dynamics and distribution of influenza drug resistance acquisition to protein M2 and neuraminidase inhibitors
    • Garcia, V., Aris-Brosou, S., Comparative dynamics and distribution of influenza drug resistance acquisition to protein M2 and neuraminidase inhibitors. Mol. Biol. Evol. 31 (2014), 355–363.
    • (2014) Mol. Biol. Evol. , vol.31 , pp. 355-363
    • Garcia, V.1    Aris-Brosou, S.2
  • 11
    • 0032544055 scopus 로고    scopus 로고
    • A novel mechanism for the acquisition of virulence by a human influenza A virus
    • Goto, H., Kawaoka, Y., A novel mechanism for the acquisition of virulence by a human influenza A virus. Proc. Natl. Acad. Sci. U. S. A. 95 (1998), 10224–10228.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 10224-10228
    • Goto, H.1    Kawaoka, Y.2
  • 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 (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
  • 13
    • 69249212321 scopus 로고    scopus 로고
    • Automated comparative protein structure modeling with SWISS-MODEL and Swiss-PdbViewer: a historical perspective
    • Guex, N., Peitsch, M.C., Schwede, T., Automated comparative protein structure modeling with SWISS-MODEL and Swiss-PdbViewer: a historical perspective. Electrophoresis 30 (2009), S162–S173.
    • (2009) Electrophoresis , vol.30 , pp. S162-S173
    • Guex, N.1    Peitsch, M.C.2    Schwede, T.3
  • 15
    • 70349728568 scopus 로고    scopus 로고
    • Zanamivir-resistant influenza viruses with a novel neuraminidase mutation
    • Hurt, A.C., Holien, J.K., Parker, M., Kelso, A., Barr, I.G., Zanamivir-resistant influenza viruses with a novel neuraminidase mutation. J. Virol. 83 (2009), 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
  • 16
    • 77955842998 scopus 로고    scopus 로고
    • Assessing the development of oseltamivir and zanamivir resistance in A (H5N1) influenza viruses using a ferret model
    • Hurt, A.C., Lowther, S., Middleton, D., Barr, I.G., Assessing the development of oseltamivir and zanamivir resistance in A (H5N1) influenza viruses using a ferret model. Antivir. Res. 87 (2010), 361–366.
    • (2010) Antivir. Res. , vol.87 , pp. 361-366
    • Hurt, A.C.1    Lowther, S.2    Middleton, D.3    Barr, I.G.4
  • 18
    • 84901417047 scopus 로고    scopus 로고
    • The epidemiology and spread of drug resistant human influenza viruses
    • Hurt, A.C., The epidemiology and spread of drug resistant human influenza viruses. Curr. Opin. Virol. 8 (2014), 22–29.
    • (2014) Curr. Opin. Virol. , vol.8 , pp. 22-29
    • Hurt, A.C.1
  • 19
    • 41949085484 scopus 로고    scopus 로고
    • Monitoring influenza virus content in vaccine production: precise assays for the quantitation of hemagglutination and neuraminidase activity
    • Kalbfuss, B., Knöchlein, A., Kröber, T., Reichl, U., Monitoring influenza virus content in vaccine production: precise assays for the quantitation of hemagglutination and neuraminidase activity. Biologicals 36 (2008), 145–161.
    • (2008) Biologicals , vol.36 , pp. 145-161
    • Kalbfuss, B.1    Knöchlein, A.2    Kröber, T.3    Reichl, U.4
  • 25
    • 84983559700 scopus 로고    scopus 로고
    • Zanamivir-resistant influenza viruses with Q136K or Q136R neuraminidase residue mutations can arise during MDCK cell culture creating challenges for antiviral susceptibility monitoring
    • Little, K., Leang, S.K., Butler, J., Baas, C., Harrower, B., Mosse, J., Barr, I.G., Hurt, A.C., Zanamivir-resistant influenza viruses with Q136K or Q136R neuraminidase residue mutations can arise during MDCK cell culture creating challenges for antiviral susceptibility monitoring. Euro Surveill., 20, 2015.
    • (2015) Euro Surveill. , vol.20
    • Little, K.1    Leang, S.K.2    Butler, J.3    Baas, C.4    Harrower, B.5    Mosse, J.6    Barr, I.G.7    Hurt, A.C.8
  • 26
    • 84881593284 scopus 로고    scopus 로고
    • Determination of neuraminidase kinetic constants using whole influenza virus preparations and correction for spectroscopic interference by a fluorogenic substrate
    • Marathe, B.M., Leveque, V., Klumpp, K., Webster, R.G., Govorkova, E.A., Determination of neuraminidase kinetic constants using whole influenza virus preparations and correction for spectroscopic interference by a fluorogenic substrate. PLoS One, 8, 2013, e71401.
    • (2013) PLoS One , vol.8 , pp. e71401
    • Marathe, B.M.1    Leveque, V.2    Klumpp, K.3    Webster, R.G.4    Govorkova, E.A.5
  • 27
    • 84888815602 scopus 로고    scopus 로고
    • Reduced susceptibility to all neuraminidase inhibitors of influenza H1N1 viruses with haemagglutinin mutations and mutations in non-conserved residues of the neuraminidase
    • McKimm-Breschkin, J.L., Williams, J., Barrett, S., Jachno, K., McDonald, M., Mohr, P.G., Saito, T., Tashiro, M., Reduced susceptibility to all neuraminidase inhibitors of influenza H1N1 viruses with haemagglutinin mutations and mutations in non-conserved residues of the neuraminidase. J. Antimicrob. Chemother. 68 (2013), 2210–2221.
    • (2013) J. Antimicrob. Chemother. , vol.68 , pp. 2210-2221
    • McKimm-Breschkin, J.L.1    Williams, J.2    Barrett, S.3    Jachno, K.4    McDonald, M.5    Mohr, P.G.6    Saito, T.7    Tashiro, M.8
  • 28
    • 84888815602 scopus 로고    scopus 로고
    • Reduced susceptibility to all neuraminidase inhibitors of influenza H1N1 viruses with haemagglutinin mutations and mutations in non-conserved residues of the neuraminidase
    • McKimm-Breschkin, J.L., Williams, J., Barrett, S., Jachno, K., McDonald, M., Mohr, P.G., Saito, T., Tashiro, M., Reduced susceptibility to all neuraminidase inhibitors of influenza H1N1 viruses with haemagglutinin mutations and mutations in non-conserved residues of the neuraminidase. J. Antimicrob. Chemother. 68 (2013), 2210–2221.
    • (2013) J. Antimicrob. Chemother. , vol.68 , pp. 2210-2221
    • McKimm-Breschkin, J.L.1    Williams, J.2    Barrett, S.3    Jachno, K.4    McDonald, M.5    Mohr, P.G.6    Saito, T.7    Tashiro, M.8
  • 31
    • 77956116079 scopus 로고    scopus 로고
    • Assessment of pandemic and seasonal influenza A (H1N1) virus susceptibility to neuraminidase inhibitors in three enzyme activity inhibition assays
    • Nguyen, H.T., Sheu, T.G., Mishin, V.P., Klimov, A.I., Gubareva, L.V., Assessment of pandemic and seasonal influenza A (H1N1) virus susceptibility to neuraminidase inhibitors in three enzyme activity inhibition assays. Antimicrob. Agents Chemother. 54 (2010), 3671–3677.
    • (2010) Antimicrob. Agents Chemother. , vol.54 , pp. 3671-3677
    • Nguyen, H.T.1    Sheu, T.G.2    Mishin, V.P.3    Klimov, A.I.4    Gubareva, L.V.5
  • 32
    • 84860334106 scopus 로고    scopus 로고
    • Neuraminidase inhibitor resistance in influenza viruses and laboratory testing methods
    • Nguyen, H.T., Fry, A.M., Gubareva, L.V., Neuraminidase inhibitor resistance in influenza viruses and laboratory testing methods. Antivir. Ther. 17 (2012), 159–173.
    • (2012) Antivir. Ther. , vol.17 , pp. 159-173
    • Nguyen, H.T.1    Fry, A.M.2    Gubareva, L.V.3
  • 34
    • 84871833332 scopus 로고    scopus 로고
    • Assays for monitoring susceptibility of influenza viruses to neuraminidase inhibitors
    • Okomo-Adhiambo, M., Sheu, T.G., Gubareva, L.V., Assays for monitoring susceptibility of influenza viruses to neuraminidase inhibitors. Influenza Other Respir. Viruses 7:Suppl. 1 (2012), 44–49.
    • (2012) Influenza Other Respir. Viruses , vol.7 , pp. 44-49
    • Okomo-Adhiambo, M.1    Sheu, T.G.2    Gubareva, L.V.3
  • 35
    • 84865478417 scopus 로고    scopus 로고
    • Virus load kinetics and resistance development during oseltamivir treatment in infants and children infected with Influenza A(H1N1) 2009 and Influenza B viruses
    • Rath, B., von Kleist, M., Tief, F., Karsch, K., Tuerk, E., Muehlhans, S., Louis, F., Skopnik, H., Schweiger, B., Duwe, S., Virus load kinetics and resistance development during oseltamivir treatment in infants and children infected with Influenza A(H1N1) 2009 and Influenza B viruses. Pediatr. Infect. Dis. J. 31 (2012), 899–905.
    • (2012) Pediatr. Infect. Dis. J. , vol.31 , pp. 899-905
    • Rath, B.1    von Kleist, M.2    Tief, F.3    Karsch, K.4    Tuerk, E.5    Muehlhans, S.6    Louis, F.7    Skopnik, H.8    Schweiger, B.9    Duwe, S.10
  • 36
    • 33745158157 scopus 로고
    • A simple method of estimating fifty per cent endpoint
    • Reed, L.J., Muench, H., A simple method of estimating fifty per cent endpoint. Am. J. Hyg. 27 (1938), 493–497.
    • (1938) Am. J. Hyg. , vol.27 , pp. 493-497
    • Reed, L.J.1    Muench, H.2
  • 41
    • 77957330207 scopus 로고    scopus 로고
    • Emergence of a multidrug-resistant pandemic influenza A (H1N1) virus
    • van der Vries, E., Stelma, F.F., Boucher, C.A., Emergence of a multidrug-resistant pandemic influenza A (H1N1) virus. N. Engl. J. Med. 363 (2010), 1381–1382.
    • (2010) N. Engl. J. Med. , vol.363 , pp. 1381-1382
    • van der Vries, E.1    Stelma, F.F.2    Boucher, C.A.3
  • 43
    • 36749056771 scopus 로고    scopus 로고
    • The war against influenza: discovery and development of sialidase inhibitors
    • von Itzstein, M., The war against influenza: discovery and development of sialidase inhibitors. Nat. Rev. Drug Discov. 6 (2007), 967–974.
    • (2007) Nat. Rev. Drug Discov. , vol.6 , pp. 967-974
    • von Itzstein, M.1
  • 45
    • 84988899981 scopus 로고    scopus 로고
    • Clinical features of severe cases of pandemic influenza - Pandemic (H1N1) 2009 briefing note 13. World Health Organization Global Alert and Response
    • Web. Jul 2016
    • WHO, Clinical features of severe cases of pandemic influenza - Pandemic (H1N1) 2009 briefing note 13. World Health Organization Global Alert and Response. 2009 Web. Jul 2016, http://www.who.int/csr/disease/swineflu/notes/h1n1_clinical_features_20091016/en/.
    • (2009)
    • WHO1
  • 46
    • 84867469314 scopus 로고    scopus 로고
    • Meetings of the WHO working group on surveillance of influenza antiviral susceptibility—Geneva, November 2011 and June 2012;
    • Web. Jul 2016
    • WHO, Meetings of the WHO working group on surveillance of influenza antiviral susceptibility—Geneva, November 2011 and June 2012;. Wkly. Epidemiol. Rec. 87:39 (2012), 369–374 Web. Jul 2016, http://www.who.int/wer/2012/wer8739.pdf.
    • (2012) Wkly. Epidemiol. Rec. , vol.87 , Issue.39 , pp. 369-374
    • WHO1
  • 47
    • 84988832090 scopus 로고    scopus 로고
    • World Health Organization Regional Office for Europe recommendations on influenza vaccination during the 2014/2015 winter season
    • Web. Jul 2016
    • WHO, World Health Organization Regional Office for Europe recommendations on influenza vaccination during the 2014/2015 winter season. 2014 Web. Jul 2016, http://www.euro.who.int/__data/assets/pdf_file/0006/259404/WHO-Regional-Office-for-Europe-recommendations-on-influenza-vaccination-during-the-2014-2015-winter-season-Eng.pdf?ua=1.
    • (2014)
    • WHO1
  • 48
    • 84988874604 scopus 로고    scopus 로고
    • online. Laboratory methodologies for testing the antiviral susceptibility of influenza viruses: Neuraminidase inhibitor (NAI), Web. Jul,.
    • WHO, online. Laboratory methodologies for testing the antiviral susceptibility of influenza viruses: Neuraminidase inhibitor (NAI), Web. Jul 2016, http://www.who.int/influenza/gisrs_laboratory/antiviral_susceptibility/nai_phenotyping/en/.
    • (2016)
  • 49
    • 0027162942 scopus 로고
    • 4-Guanidino-2,4-dideoxy-2,3-dehydro-N-acetylneuraminic acid is a highly effective inhibitor both of the sialidase (neuraminidase) and of growth of a wide range of influenza A and B viruses in vitro
    • Woods, J.M., Bethell, R.C., Coates, J.A., Healy, N., Hiscox, S.A., Pearson, B.A., Ryan, D.M., Ticehurst, J., Tilling, J., Walcott, S.M., et al. 4-Guanidino-2,4-dideoxy-2,3-dehydro-N-acetylneuraminic acid is a highly effective inhibitor both of the sialidase (neuraminidase) and of growth of a wide range of influenza A and B viruses in vitro. Antimicrob. Agents Chemother. 37 (1993), 1473–1479.
    • (1993) Antimicrob. Agents Chemother. , vol.37 , pp. 1473-1479
    • Woods, J.M.1    Bethell, R.C.2    Coates, J.A.3    Healy, N.4    Hiscox, S.A.5    Pearson, B.A.6    Ryan, D.M.7    Ticehurst, J.8    Tilling, J.9    Walcott, S.M.10
  • 50
    • 55249083577 scopus 로고    scopus 로고
    • Structural characterization of the 1918 influenza virus H1N1 neuraminidase
    • Xu, X., Zhu, X., Dwek, R.A., Stevens, J., Wilson, I.A., Structural characterization of the 1918 influenza virus H1N1 neuraminidase. J. Virol. 82 (2008), 10493–10501.
    • (2008) J. Virol. , vol.82 , pp. 10493-10501
    • Xu, X.1    Zhu, X.2    Dwek, R.A.3    Stevens, J.4    Wilson, I.A.5
  • 51
    • 36048996081 scopus 로고    scopus 로고
    • Neuraminidase inhibitor-resistant recombinant A/Vietnam/1203/04 (H5N1) influenza viruses retain their replication efficiency and pathogenicity in vitro and in vivo
    • Yen, H.L., Ilyushina, N.A., Salomon, R., Hoffmann, E., Webster, R.G., Govorkova, E.A., Neuraminidase inhibitor-resistant recombinant A/Vietnam/1203/04 (H5N1) influenza viruses retain their replication efficiency and pathogenicity in vitro and in vivo. J. Virol. 81 (2007), 12418–12426.
    • (2007) J. Virol. , vol.81 , pp. 12418-12426
    • Yen, H.L.1    Ilyushina, N.A.2    Salomon, R.3    Hoffmann, E.4    Webster, R.G.5    Govorkova, E.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.