메뉴 건너뛰기




Volumn 22, Issue 12, 2016, Pages 975-983

Functional balance between neuraminidase and haemagglutinin in influenza viruses

Author keywords

Antiviral resistance; Haemagglutinin; Haemagglutinin Neuraminidase balance; Host adaptation; Influenza viruses; Neuraminidase

Indexed keywords

ANTIVIRUS AGENT; VIRUS HEMAGGLUTININ; VIRUS SIALIDASE; INFLUENZA VIRUS HEMAGGLUTININ; SIALIDASE; VIRAL PROTEIN;

EID: 85006324202     PISSN: 1198743X     EISSN: 14690691     Source Type: Journal    
DOI: 10.1016/j.cmi.2016.07.007     Document Type: Review
Times cited : (112)

References (64)
  • 1
    • 85006245463 scopus 로고    scopus 로고
    • WHO | Monthly Risk Assessment Summary
    • WHO [accessed 18.12.15]
    • [1] World Health Organization, WHO | Monthly Risk Assessment Summary. 2015, WHO http://www.who.int/influenza/human_animal_interface/HAI_Risk_Assessment/en/ [accessed 18.12.15].
    • (2015)
    • World Health Organization1
  • 2
    • 79960384534 scopus 로고    scopus 로고
    • Influenza A viruses: new research developments
    • [2] Medina, R.A., García-Sastre, A., Influenza A viruses: new research developments. Nat Rev Microbiol 9 (2011), 590–603.
    • (2011) Nat Rev Microbiol , vol.9 , pp. 590-603
    • Medina, R.A.1    García-Sastre, A.2
  • 3
    • 85006308544 scopus 로고    scopus 로고
    • CIDRAP. Avian Flu Scan. CIDRAP n.d. [accessed 17.08.15].
    • [3] CIDRAP. Avian Flu Scan. CIDRAP n.d. http://www.cidrap.umn.edu/news-perspective?key=&page=1&f[0]=field_related_topics%3A49 [accessed 17.08.15].
  • 5
    • 79955537438 scopus 로고    scopus 로고
    • Importance of viral genomic composition in modulating glycoprotein content on the surface of influenza virus particles
    • [5] Moulès, V., Terrier, O., Yver, M., Riteau, B., Moriscot, C., Ferraris, O., et al. Importance of viral genomic composition in modulating glycoprotein content on the surface of influenza virus particles. Virology 414 (2011), 51–62.
    • (2011) Virology , vol.414 , pp. 51-62
    • Moulès, V.1    Terrier, O.2    Yver, M.3    Riteau, B.4    Moriscot, C.5    Ferraris, O.6
  • 6
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin
    • [6] Skehel, J.J., Wiley, D.C., Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu Rev Biochem 69 (2000), 531–569.
    • (2000) Annu Rev Biochem , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 7
    • 84887290174 scopus 로고    scopus 로고
    • New world bats harbor diverse influenza A viruses
    • [7] Tong, S., Zhu, X., Li, Y., Shi, M., Zhang, J., Bourgeois, M., et al. New world bats harbor diverse influenza A viruses. PLoS Pathog, 9, 2013, e1003657.
    • (2013) PLoS Pathog , vol.9 , pp. e1003657
    • Tong, S.1    Zhu, X.2    Li, Y.3    Shi, M.4    Zhang, J.5    Bourgeois, M.6
  • 8
    • 33748437791 scopus 로고    scopus 로고
    • The structure of H5N1 avian influenza neuraminidase suggests new opportunities for drug design
    • [8] Russell, R.J., Haire, L.F., Stevens, D.J., Collins, P.J., Lin, Y.P., Blackburn, G.M., et al. The structure of H5N1 avian influenza neuraminidase suggests new opportunities for drug design. Nature 443 (2006), 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
  • 9
    • 29444433087 scopus 로고    scopus 로고
    • Glycan microarray analysis of the hemagglutinins from modern and pandemic influenza viruses reveals different receptor specificities
    • [9] Stevens, J., Blixt, O., Glaser, L., Taubenberger, J.K., Palese, P., Paulson, J.C., et al. Glycan microarray analysis of the hemagglutinins from modern and pandemic influenza viruses reveals different receptor specificities. J Mol Biol 355 (2006), 1143–1155.
    • (2006) J Mol Biol , vol.355 , pp. 1143-1155
    • Stevens, J.1    Blixt, O.2    Glaser, L.3    Taubenberger, J.K.4    Palese, P.5    Paulson, J.C.6
  • 10
    • 33645278326 scopus 로고    scopus 로고
    • Avian flu: influenza virus receptors in the human airway
    • [10] Shinya, K., Ebina, M., Yamada, S., Ono, M., Kasai, N., Kawaoka, Y., Avian flu: influenza virus receptors in the human airway. Nature 440 (2006), 435–436.
    • (2006) Nature , vol.440 , pp. 435-436
    • Shinya, K.1    Ebina, M.2    Yamada, S.3    Ono, M.4    Kasai, N.5    Kawaoka, Y.6
  • 11
    • 35348888890 scopus 로고    scopus 로고
    • Human and avian influenza viruses target different cells in the lower respiratory tract of humans and other mammals
    • [11] Van Riel, D., Munster, V.J., de Wit, E., Rimmelzwaan, G.F., Fouchier, R.A.M., Osterhaus, A.D.M.E., et al. Human and avian influenza viruses target different cells in the lower respiratory tract of humans and other mammals. Am J Pathol 171 (2007), 1215–1223.
    • (2007) Am J Pathol , vol.171 , pp. 1215-1223
    • Van Riel, D.1    Munster, V.J.2    de Wit, E.3    Rimmelzwaan, G.F.4    Fouchier, R.A.M.5    Osterhaus, A.D.M.E.6
  • 12
    • 33645981586 scopus 로고    scopus 로고
    • Structure and receptor specificity of the hemagglutinin from an H5N1 influenza virus
    • [12] Stevens, J., Blixt, O., Tumpey, T.M., Taubenberger, J.K., Paulson, J.C., 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
  • 13
    • 33846820412 scopus 로고    scopus 로고
    • A two-amino acid change in the hemagglutinin of the 1918 influenza virus abolishes transmission
    • [13] Tumpey, T.M., Maines, T.R., Hoeven, N.V., Glaser, L., Solórzano, A., Pappas, C., et al. A two-amino acid change in the hemagglutinin of the 1918 influenza virus abolishes transmission. Science 315 (2007), 655–659.
    • (2007) Science , vol.315 , pp. 655-659
    • Tumpey, T.M.1    Maines, T.R.2    Hoeven, N.V.3    Glaser, L.4    Solórzano, A.5    Pappas, C.6
  • 14
    • 84888024210 scopus 로고    scopus 로고
    • Substitutions near the receptor binding site determine major antigenic change during influenza virus evolution
    • [14] Koel, B.F., Burke, D.F., Bestebroer, T.M., van der Vliet, S., Zondag, G.C.M., Vervaet, G., et al. Substitutions near the receptor binding site determine major antigenic change during influenza virus evolution. Science 342 (2013), 976–979.
    • (2013) Science , vol.342 , pp. 976-979
    • Koel, B.F.1    Burke, D.F.2    Bestebroer, T.M.3    van der Vliet, S.4    Zondag, G.C.M.5    Vervaet, G.6
  • 16
    • 84874761652 scopus 로고    scopus 로고
    • Influenza HA subtypes demonstrate divergent phenotypes for cleavage activation and pH of fusion: implications for host range and adaptation
    • [16] Galloway, S.E., Reed, M.L., Russell, C.J., Steinhauer, D.A., Influenza HA subtypes demonstrate divergent phenotypes for cleavage activation and pH of fusion: implications for host range and adaptation. PLoS Pathog, 9, 2013.
    • (2013) PLoS Pathog , vol.9
    • Galloway, S.E.1    Reed, M.L.2    Russell, C.J.3    Steinhauer, D.A.4
  • 17
    • 84958093018 scopus 로고    scopus 로고
    • H1N1 Swine influenza viruses differ from avian precursors by a higher pH optimum of membrane fusion
    • [17] Baumann, J., Kouassi, N.M., Foni, E., Klenk, H.-D., Matrosovich, M., H1N1 Swine influenza viruses differ from avian precursors by a higher pH optimum of membrane fusion. J Virol 90 (2016), 1569–1577.
    • (2016) J Virol , vol.90 , pp. 1569-1577
    • Baumann, J.1    Kouassi, N.M.2    Foni, E.3    Klenk, H.-D.4    Matrosovich, M.5
  • 18
    • 84857863488 scopus 로고    scopus 로고
    • The multibasic cleavage site of the hemagglutinin of highly pathogenic A/Vietnam/1203/2004 (H5N1) avian influenza virus acts as a virulence factor in a host-specific manner in mammals
    • [18] Suguitan, A.L., Matsuoka, Y., Lau, Y.-F., Santos, C.P., Vogel, L., Cheng, L.I., et al. The multibasic cleavage site of the hemagglutinin of highly pathogenic A/Vietnam/1203/2004 (H5N1) avian influenza virus acts as a virulence factor in a host-specific manner in mammals. J Virol 86 (2012), 2706–2714.
    • (2012) J Virol , vol.86 , pp. 2706-2714
    • Suguitan, A.L.1    Matsuoka, Y.2    Lau, Y.-F.3    Santos, C.P.4    Vogel, L.5    Cheng, L.I.6
  • 19
    • 84858374093 scopus 로고    scopus 로고
    • The multibasic cleavage site in h5n1 virus is critical for systemic spread along the olfactory and hematogenous routes in ferrets
    • [19] Schrauwen, E.J.A., Herfst, S., Leijten, L.M., van Run, P., Bestebroer, T.M., Linster, M., et al. The multibasic cleavage site in h5n1 virus is critical for systemic spread along the olfactory and hematogenous routes in ferrets. J Virol 86 (2012), 3975–3984.
    • (2012) J Virol , vol.86 , pp. 3975-3984
    • Schrauwen, E.J.A.1    Herfst, S.2    Leijten, L.M.3    van Run, P.4    Bestebroer, T.M.5    Linster, M.6
  • 20
    • 79956332420 scopus 로고    scopus 로고
    • Insertion of a multibasic cleavage site in the haemagglutinin of human influenza H3N2 virus does not increase pathogenicity in ferrets
    • [20] Schrauwen, E.J.A., Bestebroer, T.M., Munster, V.J., de Wit, E., Herfst, S., Rimmelzwaan, G.F., et al. Insertion of a multibasic cleavage site in the haemagglutinin of human influenza H3N2 virus does not increase pathogenicity in ferrets. J Gen Virol 92 (2011), 1410–1415.
    • (2011) J Gen Virol , vol.92 , pp. 1410-1415
    • Schrauwen, E.J.A.1    Bestebroer, T.M.2    Munster, V.J.3    de Wit, E.4    Herfst, S.5    Rimmelzwaan, G.F.6
  • 21
    • 0037196586 scopus 로고    scopus 로고
    • Importance of hemagglutinin glycosylation for the biological functions of influenza virus
    • [21] Klenk, H.-D., Wagner, R., Heuer, D., Wolff, T., Importance of hemagglutinin glycosylation for the biological functions of influenza virus. Virus Res 82 (2002), 73–75.
    • (2002) Virus Res , vol.82 , pp. 73-75
    • Klenk, H.-D.1    Wagner, R.2    Heuer, D.3    Wolff, T.4
  • 22
    • 0036090557 scopus 로고    scopus 로고
    • Functional balance between haemagglutinin and neuraminidase in influenza virus infections
    • [22] Wagner, R., Matrosovich, M., Klenk, H.-D., Functional balance between haemagglutinin and neuraminidase in influenza virus infections. Rev Med Virol 12 (2002), 159–166.
    • (2002) Rev Med Virol , vol.12 , pp. 159-166
    • Wagner, R.1    Matrosovich, M.2    Klenk, H.-D.3
  • 23
  • 24
    • 0026508847 scopus 로고
    • The 2.2 A resolution crystal structure of influenza B neuraminidase and its complex with sialic acid
    • [24] Burmeister, W.P., Ruigrok, R.W., Cusack, S., The 2.2 A resolution crystal structure of influenza B neuraminidase and its complex with sialic acid. EMBO J 11 (1992), 49–56.
    • (1992) EMBO J , vol.11 , pp. 49-56
    • Burmeister, W.P.1    Ruigrok, R.W.2    Cusack, S.3
  • 25
    • 0029065437 scopus 로고
    • N1 neuraminidase of influenza virus A/FPV/Rostock/34 has haemadsorbing activity
    • [25] Hausmann, J., Kretzschmar, E., Garten, W., Klenk, H.D., N1 neuraminidase of influenza virus A/FPV/Rostock/34 has haemadsorbing activity. J Gen Virol 76:Pt 7 (1995), 1719–1728.
    • (1995) J Gen Virol , vol.76 , pp. 1719-1728
    • Hausmann, J.1    Kretzschmar, E.2    Garten, W.3    Klenk, H.D.4
  • 26
    • 67349192219 scopus 로고    scopus 로고
    • Functional significance of the hemadsorption activity of influenza virus neuraminidase and its alteration in pandemic viruses
    • [26] Uhlendorff, J., Matrosovich, T., Klenk, H.-D., Matrosovich, M., Functional significance of the hemadsorption activity of influenza virus neuraminidase and its alteration in pandemic viruses. Arch Virol 154 (2009), 945–957.
    • (2009) Arch Virol , vol.154 , pp. 945-957
    • Uhlendorff, J.1    Matrosovich, T.2    Klenk, H.-D.3    Matrosovich, M.4
  • 28
    • 0026054562 scopus 로고
    • The N2 neuraminidase of human influenza virus has acquired a substrate specificity complementary to the hemagglutinin receptor specificity
    • [28] Baum, L.G., Paulson, J.C., The N2 neuraminidase of human influenza virus has acquired a substrate specificity complementary to the hemagglutinin receptor specificity. Virology 180 (1991), 10–15.
    • (1991) Virology , vol.180 , pp. 10-15
    • Baum, L.G.1    Paulson, J.C.2
  • 29
    • 0032811051 scopus 로고    scopus 로고
    • Amino acid residues contributing to the substrate specificity of the influenza A virus neuraminidase
    • [29] Kobasa, D., Kodihalli, S., Luo, M., Castrucci, M.R., Donatelli, I., Suzuki, Y., et al. Amino acid residues contributing to the substrate specificity of the influenza A virus neuraminidase. J Virol 73 (1999), 6743–6751.
    • (1999) J Virol , vol.73 , pp. 6743-6751
    • Kobasa, D.1    Kodihalli, S.2    Luo, M.3    Castrucci, M.R.4    Donatelli, I.5    Suzuki, Y.6
  • 30
    • 84876723582 scopus 로고    scopus 로고
    • Attenuation of an influenza A virus due to alteration of its hemagglutinin-neuraminidase functional balance in mice
    • [30] Gen, F., Yamada, S., Kato, K., Akashi, H., Kawaoka, Y., Horimoto, T., Attenuation of an influenza A virus due to alteration of its hemagglutinin-neuraminidase functional balance in mice. Arch Virol 158 (2013), 1003–1011.
    • (2013) Arch Virol , vol.158 , pp. 1003-1011
    • Gen, F.1    Yamada, S.2    Kato, K.3    Akashi, H.4    Kawaoka, Y.5    Horimoto, T.6
  • 31
    • 0033934134 scopus 로고    scopus 로고
    • Interdependence of hemagglutinin glycosylation and neuraminidase as regulators of influenza virus growth: a study by reverse genetics
    • [31] Wagner, R., Wolff, T., Herwig, A., Pleschka, S., Klenk, H.-D., Interdependence of hemagglutinin glycosylation and neuraminidase as regulators of influenza virus growth: a study by reverse genetics. J Virol 74 (2000), 6316–6323.
    • (2000) J Virol , vol.74 , pp. 6316-6323
    • Wagner, R.1    Wolff, T.2    Herwig, A.3    Pleschka, S.4    Klenk, H.-D.5
  • 32
    • 0035813039 scopus 로고    scopus 로고
    • Glycosylation of haemagglutinin and stalk-length of neuraminidase combine to regulate the growth of avian influenza viruses in tissue culture
    • [32] Baigent, S.J., McCauley, J.W., Glycosylation of haemagglutinin and stalk-length of neuraminidase combine to regulate the growth of avian influenza viruses in tissue culture. Virus Res 79 (2001), 177–185.
    • (2001) Virus Res , vol.79 , pp. 177-185
    • Baigent, S.J.1    McCauley, J.W.2
  • 33
    • 84887137511 scopus 로고    scopus 로고
    • A mutant influenza virus that uses an N1 neuraminidase as the receptor-binding protein
    • [33] Hooper, K.A., Bloom, J.D., A mutant influenza virus that uses an N1 neuraminidase as the receptor-binding protein. J Virol 87 (2013), 12531–12540.
    • (2013) J Virol , vol.87 , pp. 12531-12540
    • Hooper, K.A.1    Bloom, J.D.2
  • 34
    • 77953315080 scopus 로고    scopus 로고
    • Neuraminidase receptor binding variants of human influenza A(H3N2) viruses resulting from substitution of aspartic acid 151 in the catalytic site: a role in virus attachment?
    • [34] Lin, Y.P., Gregory, V., Collins, P., Kloess, J., Wharton, S., Cattle, N., et al. Neuraminidase receptor binding variants of human influenza A(H3N2) viruses resulting from substitution of aspartic acid 151 in the catalytic site: a role in virus attachment?. J Virol 84 (2010), 6769–6781.
    • (2010) J Virol , vol.84 , pp. 6769-6781
    • Lin, Y.P.1    Gregory, V.2    Collins, P.3    Kloess, J.4    Wharton, S.5    Cattle, N.6
  • 35
    • 33846343627 scopus 로고    scopus 로고
    • Evolution of the susceptibility to antiviral drugs of A/H3N2 influenza viruses isolated in France from 2002 to 2005
    • [35] Ferraris, O., Kessler, N., Valette, M., Lina, B., Evolution of the susceptibility to antiviral drugs of A/H3N2 influenza viruses isolated in France from 2002 to 2005. Vaccine 24 (2006), 6656–6659.
    • (2006) Vaccine , vol.24 , pp. 6656-6659
    • Ferraris, O.1    Kessler, N.2    Valette, M.3    Lina, B.4
  • 36
    • 84860466711 scopus 로고    scopus 로고
    • Rescue of a h3n2 influenza virus containing a deficient neuraminidase protein by a hemagglutinin with a low receptor-binding affinity
    • [36] Richard, M., Erny, A., Caré, B., Traversier, A., Barthélémy, M., Hay, A., et al. Rescue of a h3n2 influenza virus containing a deficient neuraminidase protein by a hemagglutinin with a low receptor-binding affinity. PLoS One, 7, 2012, e33880.
    • (2012) PLoS One , vol.7 , pp. e33880
    • Richard, M.1    Erny, A.2    Caré, B.3    Traversier, A.4    Barthélémy, M.5    Hay, A.6
  • 37
    • 33750119810 scopus 로고    scopus 로고
    • Glycan microarray technologies: tools to survey host specificity of influenza viruses
    • [37] Stevens, J., Blixt, O., Paulson, J.C., Wilson, I.A., Glycan microarray technologies: tools to survey host specificity of influenza viruses. Nat Rev Microbiol 4 (2006), 857–864.
    • (2006) Nat Rev Microbiol , vol.4 , pp. 857-864
    • Stevens, J.1    Blixt, O.2    Paulson, J.C.3    Wilson, I.A.4
  • 38
    • 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
    • [38] Wetherall, N.T., Trivedi, T., Zeller, J., Hodges-Savola, C., McKimm-Breschkin, J.L., Zambon, M., et al. 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
  • 39
    • 84962062601 scopus 로고    scopus 로고
    • Capture and characterization of influenza A virus from primary samples using glycan bead arrays
    • [39] Cohen, M., Fisher, C.J., Huang, M.L., Lindsay, L.L., Plancarte, M., Boyce, W.M., et al. Capture and characterization of influenza A virus from primary samples using glycan bead arrays. Virology 493 (2016), 128–135.
    • (2016) Virology , vol.493 , pp. 128-135
    • Cohen, M.1    Fisher, C.J.2    Huang, M.L.3    Lindsay, L.L.4    Plancarte, M.5    Boyce, W.M.6
  • 40
    • 84905981660 scopus 로고    scopus 로고
    • Functional balance between the hemagglutinin and neuraminidase of influenza A(H1N1)pdm09 HA D222 Variants
    • [40] Casalegno, J.-S., Ferraris, O., Escuret, V., Bouscambert, M., Bergeron, C., Linès, L., et al. Functional balance between the hemagglutinin and neuraminidase of influenza A(H1N1)pdm09 HA D222 Variants. PLoS One, 9, 2014.
    • (2014) PLoS One , vol.9
    • Casalegno, J.-S.1    Ferraris, O.2    Escuret, V.3    Bouscambert, M.4    Bergeron, C.5    Linès, L.6
  • 41
    • 84866181427 scopus 로고    scopus 로고
    • Functional balance of the hemagglutinin and neuraminidase activities accompanies the emergence of the 2009 H1N1 influenza pandemic
    • [41] Xu, R., Zhu, X., McBride, R., Nycholat, C.M., Yu, W., Paulson, J.C., et al. Functional balance of the hemagglutinin and neuraminidase activities accompanies the emergence of the 2009 H1N1 influenza pandemic. J Virol 86 (2012), 9221–9232.
    • (2012) J Virol , vol.86 , pp. 9221-9232
    • Xu, R.1    Zhu, X.2    McBride, R.3    Nycholat, C.M.4    Yu, W.5    Paulson, J.C.6
  • 42
    • 84929650048 scopus 로고    scopus 로고
    • Pandemic swine H1N1 influenza viruses with almost undetectable neuraminidase activity are not transmitted via aerosols in ferrets and are inhibited by human mucus but not swine mucus
    • [42] Zanin, M., Marathe, B., Wong, S.-S., Yoon, S.-W., Collin, E., Oshansky, C., et al. Pandemic swine H1N1 influenza viruses with almost undetectable neuraminidase activity are not transmitted via aerosols in ferrets and are inhibited by human mucus but not swine mucus. J Virol 89 (2015), 5935–5948.
    • (2015) J Virol , vol.89 , pp. 5935-5948
    • Zanin, M.1    Marathe, B.2    Wong, S.-S.3    Yoon, S.-W.4    Collin, E.5    Oshansky, C.6
  • 43
    • 84924872589 scopus 로고    scopus 로고
    • Biophysical measurement of the balance of influenza a hemagglutinin and neuraminidase activities
    • [43] Benton, D.J., Martin, S.R., Wharton, S.A., McCauley, J.W., Biophysical measurement of the balance of influenza a hemagglutinin and neuraminidase activities. J Biol Chem 290 (2015), 6516–6521.
    • (2015) J Biol Chem , vol.290 , pp. 6516-6521
    • Benton, D.J.1    Martin, S.R.2    Wharton, S.A.3    McCauley, J.W.4
  • 44
    • 0032927194 scopus 로고    scopus 로고
    • The surface glycoproteins of h5 influenza viruses isolated from humans, chickens, and wild aquatic birds have distinguishable properties
    • [44] Matrosovich, M., Zhou, N., Kawaoka, Y., Webster, R., The surface glycoproteins of h5 influenza viruses isolated from humans, chickens, and wild aquatic birds have distinguishable properties. J Virol 73 (1999), 1146–1155.
    • (1999) J Virol , vol.73 , pp. 1146-1155
    • Matrosovich, M.1    Zhou, N.2    Kawaoka, Y.3    Webster, R.4
  • 45
    • 80052186216 scopus 로고    scopus 로고
    • Hemagglutinin–neuraminidase balance confers respiratory-droplet transmissibility of the pandemic H1N1 influenza virus in ferrets
    • [45] Yen, H.-L., Liang, C.-H., Wu, C.-Y., Forrest, H.L., Ferguson, A., Choy, K.-T., et al. Hemagglutinin–neuraminidase balance confers respiratory-droplet transmissibility of the pandemic H1N1 influenza virus in ferrets. Proc Natl Acad Sci U S A 108 (2011), 14264–14269.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 14264-14269
    • Yen, H.-L.1    Liang, C.-H.2    Wu, C.-Y.3    Forrest, H.L.4    Ferguson, A.5    Choy, K.-T.6
  • 46
    • 23844487765 scopus 로고    scopus 로고
    • A single amino acid substitution in 1918 influenza virus hemagglutinin changes receptor binding specificity
    • [46] Glaser, L., Stevens, J., Zamarin, D., Wilson, I.A., García-Sastre, A., Tumpey, T.M., et al. A single amino acid substitution in 1918 influenza virus hemagglutinin changes receptor binding specificity. J Virol 79 (2005), 11533–11536.
    • (2005) J Virol , vol.79 , pp. 11533-11536
    • Glaser, L.1    Stevens, J.2    Zamarin, D.3    Wilson, I.A.4    García-Sastre, A.5    Tumpey, T.M.6
  • 48
    • 84923367482 scopus 로고    scopus 로고
    • Epistatic interactions between neuraminidase mutations facilitated the emergence of the oseltamivir-resistant H1N1 influenza viruses
    • [48] Duan, S., Govorkova, E.A., Bahl, J., Zaraket, H., Baranovich, T., Seiler, P., et al. Epistatic interactions between neuraminidase mutations facilitated the emergence of the oseltamivir-resistant H1N1 influenza viruses. Nat Commun, 5, 2014, 5029.
    • (2014) Nat Commun , vol.5 , pp. 5029
    • Duan, S.1    Govorkova, E.A.2    Bahl, J.3    Zaraket, H.4    Baranovich, T.5    Seiler, P.6
  • 49
    • 48249156625 scopus 로고    scopus 로고
    • Enzymatic properties of the neuraminidase of seasonal H1N1 influenza viruses provide insights for the emergence of natural resistance to oseltamivir
    • [49] Rameix-Welti, M.-A., Enouf, V., Cuvelier, F., Jeannin, P., van der Werf, S., Enzymatic properties of the neuraminidase of seasonal H1N1 influenza viruses provide insights for the emergence of natural resistance to oseltamivir. PLoS Pathog, 4, 2008, e1000103.
    • (2008) PLoS Pathog , vol.4 , pp. e1000103
    • Rameix-Welti, M.-A.1    Enouf, V.2    Cuvelier, F.3    Jeannin, P.4    van der Werf, S.5
  • 51
    • 84924811650 scopus 로고    scopus 로고
    • Identification of amino acid substitutions supporting antigenic change of influenza A(H1N1)pdm09 viruses
    • [51] Koel, B.F., Mögling, R., Chutinimitkul, S., Fraaij, P.L., Burke, D.F., van der Vliet, S., et al. Identification of amino acid substitutions supporting antigenic change of influenza A(H1N1)pdm09 viruses. J Virol 89 (2015), 3763–3775.
    • (2015) J Virol , vol.89 , pp. 3763-3775
    • Koel, B.F.1    Mögling, R.2    Chutinimitkul, S.3    Fraaij, P.L.4    Burke, D.F.5    van der Vliet, S.6
  • 53
    • 77958459368 scopus 로고    scopus 로고
    • WHO guidelines for pharmacological management of pandemic influenza A(H1N1) 2009 and other influenza viruses
    • WHO Geneva
    • [53] World Health Organization, WHO guidelines for pharmacological management of pandemic influenza A(H1N1) 2009 and other influenza viruses. 2010, WHO, Geneva.
    • (2010)
    • World Health Organization1
  • 54
    • 0037770271 scopus 로고    scopus 로고
    • Overexpression of the alpha-2,6-sialyltransferase in MDCK cells increases influenza virus sensitivity to neuraminidase inhibitors
    • [54] Matrosovich, M., Matrosovich, T., Carr, J., Roberts, N.A., Klenk, H.-D., Overexpression of the alpha-2,6-sialyltransferase in MDCK cells increases influenza virus sensitivity to neuraminidase inhibitors. J Virol 77 (2003), 8418–8425.
    • (2003) J Virol , vol.77 , pp. 8418-8425
    • Matrosovich, M.1    Matrosovich, T.2    Carr, J.3    Roberts, N.A.4    Klenk, H.-D.5
  • 55
    • 84869067378 scopus 로고    scopus 로고
    • Comparable fitness and transmissibility between oseltamivir-resistant pandemic 2009 and seasonal H1N1 influenza viruses with the H275Y neuraminidase mutation
    • [55] Wong, D.D.Y., Choy, K.-T., Chan, R.W.Y., Sia, S.F., Chiu, H.-P., Cheung, P.P.H., et al. Comparable fitness and transmissibility between oseltamivir-resistant pandemic 2009 and seasonal H1N1 influenza viruses with the H275Y neuraminidase mutation. J Virol 86 (2012), 10558–10570.
    • (2012) J Virol , vol.86 , pp. 10558-10570
    • Wong, D.D.Y.1    Choy, K.-T.2    Chan, R.W.Y.3    Sia, S.F.4    Chiu, H.-P.5    Cheung, P.P.H.6
  • 56
    • 84873154021 scopus 로고    scopus 로고
    • Characterization of oseltamivir-resistant influenza A(H1N1)pdm09 viruses in Taiwan in 2009–2011
    • [56] Yang, J.-R., Huang, Y.-P., Chang, F.-Y., Hsu, L.-C., Huang, H.-Y., Pan, Y.-T., et al. Characterization of oseltamivir-resistant influenza A(H1N1)pdm09 viruses in Taiwan in 2009–2011. J Med Virol 85 (2013), 379–387.
    • (2013) J Med Virol , vol.85 , pp. 379-387
    • Yang, J.-R.1    Huang, Y.-P.2    Chang, F.-Y.3    Hsu, L.-C.4    Huang, H.-Y.5    Pan, Y.-T.6
  • 57
    • 37349007892 scopus 로고    scopus 로고
    • Mutations of neuraminidase implicated in neuraminidase inhibitors resistance
    • [57] Ferraris, O., Lina, B., Mutations of neuraminidase implicated in neuraminidase inhibitors resistance. J Clin Virol Off Publ Pan Am Soc Clin Virol 41 (2008), 13–19.
    • (2008) J Clin Virol Off Publ Pan Am Soc Clin Virol , vol.41 , pp. 13-19
    • Ferraris, O.1    Lina, B.2
  • 58
    • 2442494839 scopus 로고    scopus 로고
    • Molecular mechanisms of influenza virus resistance to neuraminidase inhibitors
    • [58] 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
  • 60
    • 81255208234 scopus 로고    scopus 로고
    • The antiviral resistance of influenza virus
    • [60] Escuret, V., Ferraris, O., Lina, B., The antiviral resistance of influenza virus. Therapy 8 (2011), 741–762.
    • (2011) Therapy , vol.8 , pp. 741-762
    • Escuret, V.1    Ferraris, O.2    Lina, B.3
  • 61
    • 84920192213 scopus 로고    scopus 로고
    • Molecular mechanism of the enhanced viral fitness contributed by secondary mutations in the hemagglutinin protein of oseltamivir resistant H1N1 influenza viruses: modeling studies of antibody and receptor binding
    • [61] Behera, A.K., Basu, S., Cherian, S.S., Molecular mechanism of the enhanced viral fitness contributed by secondary mutations in the hemagglutinin protein of oseltamivir resistant H1N1 influenza viruses: modeling studies of antibody and receptor binding. Gene 557 (2015), 19–27.
    • (2015) Gene , vol.557 , pp. 19-27
    • Behera, A.K.1    Basu, S.2    Cherian, S.S.3
  • 62
    • 84855949218 scopus 로고    scopus 로고
    • Amino acid changes in hemagglutinin contribute to the replication of oseltamivir-resistant H1N1 influenza viruses
    • [62] Ginting, T.E., Shinya, K., Kyan, Y., Makino, A., Matsumoto, N., Kaneda, S., et al. Amino acid changes in hemagglutinin contribute to the replication of oseltamivir-resistant H1N1 influenza viruses. J Virol 86 (2012), 121–127.
    • (2012) J Virol , vol.86 , pp. 121-127
    • Ginting, T.E.1    Shinya, K.2    Kyan, Y.3    Makino, A.4    Matsumoto, N.5    Kaneda, S.6
  • 63
    • 84355165239 scopus 로고    scopus 로고
    • The 2008–2009 H1N1 influenza virus exhibits reduced susceptibility to antibody inhibition: Implications for the prevalence of oseltamivir resistant variant viruses
    • [63] Wu, W.L., Lau, S.-Y., Chen, Y., Wang, G., Mok, B.W.-Y., Wen, X., et al. The 2008–2009 H1N1 influenza virus exhibits reduced susceptibility to antibody inhibition: Implications for the prevalence of oseltamivir resistant variant viruses. Antiviral Res 93 (2012), 144–153.
    • (2012) Antiviral Res , vol.93 , pp. 144-153
    • Wu, W.L.1    Lau, S.-Y.2    Chen, Y.3    Wang, G.4    Mok, B.W.-Y.5    Wen, X.6
  • 64
    • 77956556232 scopus 로고    scopus 로고
    • Influenza hemagglutinin and neuraminidase membrane glycoproteins
    • [64] Gamblin, S.J., Skehel, J.J., Influenza hemagglutinin and neuraminidase membrane glycoproteins. J Biol Chem 285 (2010), 28403–28409.
    • (2010) J Biol Chem , vol.285 , pp. 28403-28409
    • Gamblin, S.J.1    Skehel, J.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.