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Volumn 90, Issue 1, 2016, Pages 117-128

Comparative efficacy of monoclonal antibodies that bind to different epitopes of the 2009 pandemic H1N1 influenza virus neuraminidase

Author keywords

[No Author keywords available]

Indexed keywords

ANTIVIRUS AGENT; EPITOPE; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY 1H5; MONOCLONAL ANTIBODY 4E9; MONOCLONAL ANTIBODY CD6; MONOCLONAL ANTIBODY HF5; UNCLASSIFIED DRUG; VIRUS SIALIDASE; NA PROTEIN, INFLUENZA A VIRUS; PROTEIN BINDING; SIALIDASE; VIRAL PROTEIN; VIRUS ANTIBODY;

EID: 84953857646     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.01756-15     Document Type: Article
Times cited : (47)

References (39)
  • 1
    • 0025124414 scopus 로고
    • Independent and disparate evolution in nature of influenza A virus hemagglutinin and neuraminidase glycoproteins
    • Kilbourne ED, Johansson BE, Grajower B. 1990. Independent and disparate evolution in nature of influenza A virus hemagglutinin and neuraminidase glycoproteins. Proc Natl Acad Sci U S A 87:786-790. http://dx.doi.org/10.1073/pnas.87.2.786.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 786-790
    • Kilbourne, E.D.1    Johansson, B.E.2    Grajower, B.3
  • 2
    • 84862003840 scopus 로고    scopus 로고
    • Influenza neuraminidase
    • Air GM. 2012. Influenza neuraminidase. Influenza Other Respir Viruses 6:245-256. http://dx.doi.org/10.1111/j.1750-2659.2011.00304.x.
    • (2012) Influenza Other Respir Viruses , vol.6 , pp. 245-256
    • Air, G.M.1
  • 3
    • 7644241814 scopus 로고    scopus 로고
    • Neuraminidase is important for the initiation of influenza virus infection in human airway epithelium
    • Matrosovich MN, Matrosovich TY, Gray T, Roberts NA, Klenk HD. 2004. Neuraminidase is important for the initiation of influenza virus infection in human airway epithelium. J Virol 78:12665-12667. http://dx.doi.org/10.1128/JVI.78.22.12665-12667.2004.
    • (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
  • 4
    • 0033934134 scopus 로고    scopus 로고
    • Interde-pendence of hemagglutinin glycosylation and neuraminidase as regulators of influenza virus growth: a study by reverse genetics
    • Wagner R, WolffT, Herwig A, Pleschka S, Klenk HD. 2000. Interde-pendence of hemagglutinin glycosylation and neuraminidase as regulators of influenza virus growth: a study by reverse genetics. J Virol 74:6316-6323. http://dx.doi.org/10.1128/JVI.74.14.6316-6323.2000.
    • (2000) J Virol , vol.74 , pp. 6316-6323
    • Wagner, R.1    Wolff, T.2    Herwig, A.3    Pleschka, S.4    Klenk, H.D.5
  • 5
    • 0017151109 scopus 로고
    • Inhibition of influenza virus replication in tissue culture by 2-deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid (FANA): mechanism of action
    • Palese P, Compans RW. 1976. Inhibition of influenza virus replication in tissue culture by 2-deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid (FANA): mechanism of action. J Gen Virol 33:159-163. http://dx.doi.org/10.1099/0022-1317-33-1-159.
    • (1976) J Gen Virol , vol.33 , pp. 159-163
    • Palese, P.1    Compans, R.W.2
  • 9
    • 84921524431 scopus 로고    scopus 로고
    • Influenza neuraminidase as a vaccine antigen
    • Eichelberger MC, Wan H. 2015. Influenza neuraminidase as a vaccine antigen. Curr Top Microbiol Immunol 386:275-299. http://dx.doi.org/10.1007/82_2014_398.
    • (2015) Curr Top Microbiol Immunol , vol.386 , pp. 275-299
    • Eichelberger, M.C.1    Wan, H.2
  • 10
    • 0015519744 scopus 로고
    • Association of serum antineuraminidase antibody with resistance to influenza in man
    • Murphy BR, Kasel JA, Chanock RM. 1972. Association of serum antineuraminidase antibody with resistance to influenza in man. NEngl J Med 286:1329-1332. http://dx.doi.org/10.1056/NEJM197206222862502.
    • (1972) NEngl J Med , vol.286 , pp. 1329-1332
    • Murphy, B.R.1    Kasel, J.A.2    Chanock, R.M.3
  • 11
    • 0017576286 scopus 로고
    • Clinical and immunologic evaluation of neuraminidasespecific influenza A virus vaccine in humans
    • Ogra PL, Chow T, Beutner KR, Rubi E, Strussenberg J, DeMello S, Rizzone C. 1977. Clinical and immunologic evaluation of neuraminidasespecific influenza A virus vaccine in humans. J Infect Dis 135:499-506. http://dx.doi.org/10.1093/infdis/135.4.499.
    • (1977) J Infect Dis , vol.135 , pp. 499-506
    • Ogra, P.L.1    Chow, T.2    Beutner, K.R.3    Rubi, E.4    Strussenberg, J.5    DeMello, S.6    Rizzone, C.7
  • 12
    • 0016366813 scopus 로고
    • Induction of partial immunity to influenza by a neuraminidase-specific vaccine
    • Couch RB, Kasel JA, Gerin JL, Schulman JL, Kilbourne ED. 1974. Induction of partial immunity to influenza by a neuraminidase-specific vaccine. J Infect Dis 129:411-420. http://dx.doi.org/10.1093/infdis/129.4.411.
    • (1974) J Infect Dis , vol.129 , pp. 411-420
    • Couch, R.B.1    Kasel, J.A.2    Gerin, J.L.3    Schulman, J.L.4    Kilbourne, E.D.5
  • 13
    • 0014251345 scopus 로고
    • Antiviral activity of antiserum specific for an influenza virus neuraminidase
    • Kilbourne ED, Laver WG, Schulman JL, Webster RG. 1968. Antiviral activity of antiserum specific for an influenza virus neuraminidase. J Virol 2:281-288.
    • (1968) J Virol , vol.2 , pp. 281-288
    • Kilbourne, E.D.1    Laver, W.G.2    Schulman, J.L.3    Webster, R.G.4
  • 14
    • 0027483843 scopus 로고
    • Infection-permissive immunization with influenza virus neuraminidase prevents weight loss in infected mice
    • Johansson BE, Grajower B, Kilbourne ED. 1993. Infection-permissive immunization with influenza virus neuraminidase prevents weight loss in infected mice. Vaccine 11:1037-1039. http://dx.doi.org/10.1016/0264-410X(93)90130-P.
    • (1993) Vaccine , vol.11 , pp. 1037-1039
    • Johansson, B.E.1    Grajower, B.2    Kilbourne, E.D.3
  • 15
    • 23844534838 scopus 로고    scopus 로고
    • Immunization against influenza A virus: comparison of conventional inactivated, live-attenuated and recombinant baculovirus produced purified hemagglutinin and neuraminidase vaccines in a murine model system
    • Brett IC, Johansson BE. 2005. Immunization against influenza A virus: comparison of conventional inactivated, live-attenuated and recombinant baculovirus produced purified hemagglutinin and neuraminidase vaccines in a murine model system. Virology 339:273-280. http://dx.doi.org/10.1016/j.virol.2005.06.006.
    • (2005) Virology , vol.339 , pp. 273-280
    • Brett, I.C.1    Johansson, B.E.2
  • 16
    • 0015934548 scopus 로고
    • Effect of neuraminidase antibody on Hong Kong influenza
    • Monto AS, Kendal AP. 1973. Effect of neuraminidase antibody on Hong Kong influenza. Lancet i:623-625.
    • (1973) Lancet , vol.1 , pp. 623-625
    • Monto, A.S.1    Kendal, A.P.2
  • 17
    • 80055041065 scopus 로고    scopus 로고
    • A contributing role for anti-neuraminidase antibodies on immunity to pandemic H1N1 2009 influenza A virus
    • Marcelin G, DuBois R, Rubrum A, Russell CJ, McElhaney JE, Webby RJ. 2011. A contributing role for anti-neuraminidase antibodies on immunity to pandemic H1N1 2009 influenza A virus. PLoS One 6:e26335. http://dx.doi.org/10.1371/journal.pone.0026335.
    • (2011) PLoS One , vol.6
    • Marcelin, G.1    DuBois, R.2    Rubrum, A.3    Russell, C.J.4    McElhaney, J.E.5    Webby, R.J.6
  • 18
    • 0030273447 scopus 로고    scopus 로고
    • Genetic variation in neuraminidase genes of influenza A (H3N2) viruses
    • Xu X, Cox NJ, Bender CA, Regnery HL, Shaw MW. 1996. Genetic variation in neuraminidase genes of influenza A (H3N2) viruses. Virology 224:175-183. http://dx.doi.org/10.1006/viro.1996.0519.
    • (1996) Virology , vol.224 , pp. 175-183
    • Xu, X.1    Cox, N.J.2    Bender, C.A.3    Regnery, H.L.4    Shaw, M.W.5
  • 19
    • 33847610733 scopus 로고    scopus 로고
    • Cross-reactive neuraminidase antibodies afford partial protection against H5N1 in mice and are present in unexposed humans
    • Sandbulte MR, Jimenez GS, Boon AC, Smith LR, Treanor JJ, Webby RJ. 2007. Cross-reactive neuraminidase antibodies afford partial protection against H5N1 in mice and are present in unexposed humans. PLoS Med 4:e59. http://dx.doi.org/10.1371/journal.pmed.0040059.
    • (2007) PLoS Med , vol.4
    • Sandbulte, M.R.1    Jimenez, G.S.2    Boon, A.C.3    Smith, L.R.4    Treanor, J.J.5    Webby, R.J.6
  • 20
    • 84929494198 scopus 로고    scopus 로고
    • Vaccination with adjuvanted recombinant neuraminidase induces broad heterologous, but not heterosubtypic, cross-protection against influenza virus infection in mice
    • Wohlbold TJ, Nachbagauer R, Xu H, Tan GS, Hirsh A, Brokstad KA, Cox RJ, Palese P, Krammer F. 2015. Vaccination with adjuvanted recombinant neuraminidase induces broad heterologous, but not heterosubtypic, cross-protection against influenza virus infection in mice. mBio 6:e02556. http://dx.doi.org/10.1128/mBio.02556-14.
    • (2015) mBio , vol.6
    • Wohlbold, T.J.1    Nachbagauer, R.2    Xu, H.3    Tan, G.S.4    Hirsh, A.5    Brokstad, K.A.6    Cox, R.J.7    Palese, P.8    Krammer, F.9
  • 21
    • 0021273164 scopus 로고
    • Antigenic and biological characterization of influenza virus neuraminidase (N2) with monoclonal antibodies
    • Webster RG, Brown LE, Laver WG. 1984. Antigenic and biological characterization of influenza virus neuraminidase (N2) with monoclonal antibodies. Virology 135:30-42. http://dx.doi.org/10.1016/0042-6822(84)90114-4.
    • (1984) Virology , vol.135 , pp. 30-42
    • Webster, R.G.1    Brown, L.E.2    Laver, W.G.3
  • 22
    • 84862777184 scopus 로고    scopus 로고
    • The 2009 pandemic H1N1 virus induces anti-neuraminidase (NA) antibodies that cross-react with the NA of H5N1 viruses in ferrets
    • Chen Z, Kim L, Subbarao K, Jin H. 2012. The 2009 pandemic H1N1 virus induces anti-neuraminidase (NA) antibodies that cross-react with the NA of H5N1 viruses in ferrets. Vaccine 30:2516-2522. http://dx.doi.org/10.1016/j.vaccine.2012.01.090.
    • (2012) Vaccine , vol.30 , pp. 2516-2522
    • Chen, Z.1    Kim, L.2    Subbarao, K.3    Jin, H.4
  • 23
    • 84864013012 scopus 로고    scopus 로고
    • Protection against a lethal H5N1 influenza challenge by intranasal immunization with virus-like particles containing 2009 pandemic H1N1 neuraminidase in mice
    • Easterbrook JD, Schwartzman LM, Gao J, Kash JC, Morens DM, Couzens L, Wan H, Eichelberger MC, Taubenberger JK. 2012. Protection against a lethal H5N1 influenza challenge by intranasal immunization with virus-like particles containing 2009 pandemic H1N1 neuraminidase in mice. Virology 432:39-44. http://dx.doi.org/10.1016/j.virol.2012.06.003.
    • (2012) Virology , vol.432 , pp. 39-44
    • Easterbrook, J.D.1    Schwartzman, L.M.2    Gao, J.3    Kash, J.C.4    Morens, D.M.5    Couzens, L.6    Wan, H.7    Eichelberger, M.C.8    Taubenberger, J.K.9
  • 24
    • 84863541193 scopus 로고    scopus 로고
    • Contribution of antibody production against neuraminidase to the protection afforded by influenza vaccines
    • Marcelin G, Sandbulte MR, Webby RJ. 2012. Contribution of antibody production against neuraminidase to the protection afforded by influenza vaccines. Rev Med Virol 22:267-279. http://dx.doi.org/10.1002/rmv.1713.
    • (2012) Rev Med Virol , vol.22 , pp. 267-279
    • Marcelin, G.1    Sandbulte, M.R.2    Webby, R.J.3
  • 29
    • 77954476468 scopus 로고    scopus 로고
    • Cross-reactive neutralizing antibodies directed against pandemic H1N1 2009 virus are protective in a highly sensitive DBA/2 mouse influenza model
    • Boon AC, deBeauchamp J, Krauss S, Rubrum A, Webb AD, Webster RG, McElhaney J, Webby RJ. 2010. Cross-reactive neutralizing antibodies directed against pandemic H1N1 2009 virus are protective in a highly sensitive DBA/2 mouse influenza model. J Virol 84:7662-7667. http://dx.doi.org/10.1128/JVI.02444-09.
    • (2010) J Virol , vol.84 , pp. 7662-7667
    • Boon, A.C.1    deBeauchamp, J.2    Krauss, S.3    Rubrum, A.4    Webb, A.D.5    Webster, R.G.6    McElhaney, J.7    Webby, R.J.8
  • 32
    • 84925003752 scopus 로고    scopus 로고
    • Chimeric neuraminidase and mutant PB1 gene constellation improves growth and yield of H5N1 vaccine candidate virus
    • Plant EP, Ye Z. 2015. Chimeric neuraminidase and mutant PB1 gene constellation improves growth and yield of H5N1 vaccine candidate virus. J Gen Virol 96:752-755. http://dx.doi.org/10.1099/jgv.0.000025.
    • (2015) J Gen Virol , vol.96 , pp. 752-755
    • Plant, E.P.1    Ye, Z.2
  • 33
    • 84908173790 scopus 로고    scopus 로고
    • An optimized enzyme-linked lectin assay to measure influenza A virus neuraminidase inhibition antibody titers in human sera
    • Couzens L, Gao J, Westgeest K, Sandbulte M, Lugovtsev V, Fouchier R, Eichelberger M. 2014. An optimized enzyme-linked lectin assay to measure influenza A virus neuraminidase inhibition antibody titers in human sera. J Virol Methods 210C:7-14. http://dx.doi.org/10.1016/j.jviromet.2014.09.003.
    • (2014) J Virol Methods , vol.210C , pp. 7-14
    • Couzens, L.1    Gao, J.2    Westgeest, K.3    Sandbulte, M.4    Lugovtsev, V.5    Fouchier, R.6    Eichelberger, M.7
  • 34
    • 0035559445 scopus 로고    scopus 로고
    • Universal primer set for the full-length amplification of all influenza A viruses
    • Hoffmann E, Stech J, Guan Y, Webster RG, Perez DR. 2001. Universal primer set for the full-length amplification of all influenza A viruses. Arch Virol 146:2275-2289. http://dx.doi.org/10.1007/s007050170002.
    • (2001) Arch Virol , vol.146 , pp. 2275-2289
    • Hoffmann, E.1    Stech, J.2    Guan, Y.3    Webster, R.G.4    Perez, D.R.5
  • 35
    • 0022257421 scopus 로고
    • Location of antigenic sites on the three-dimensional structure of the influenza N2 virus neuraminidase
    • Air GM, Els MC, Brown LE, Laver WG, Webster RG. 1985. Location of antigenic sites on the three-dimensional structure of the influenza N2 virus neuraminidase. Virology 145:237-248. http://dx.doi.org/10.1016/0042-6822(85)90157-6.
    • (1985) Virology , vol.145 , pp. 237-248
    • Air, G.M.1    Els, M.C.2    Brown, L.E.3    Laver, W.G.4    Webster, R.G.5
  • 36
    • 0020629047 scopus 로고
    • Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 Å resolution
    • Varghese JN, Laver WG, Colman PM. 1983. Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 Å resolution. Nature 303: 35-40. http://dx.doi.org/10.1038/303035a0.
    • (1983) Nature , vol.303 , pp. 35-40
    • Varghese, J.N.1    Laver, W.G.2    Colman, P.M.3
  • 37
    • 84892146370 scopus 로고    scopus 로고
    • A community cluster of influenza A(H1N1)pdm09 virus exhibiting cross-resistance to oseltamivir and peramivir in Japan, November to December 2013
    • Takashita E, Ejima M, Itoh R, Miura M, Ohnishi A, Nishimura H, Odagiri T, Tashiro M. 2014. A community cluster of influenza A(H1N1)pdm09 virus exhibiting cross-resistance to oseltamivir and peramivir in Japan, November to December 2013. Euro Surveill 19(1): pii=20666. http://dx.doi.org/10.2807/1560-7917.ES2014.19.1.20666.
    • (2014) Euro Surveill , vol.19 , Issue.1
    • Takashita, E.1    Ejima, M.2    Itoh, R.3    Miura, M.4    Ohnishi, A.5    Nishimura, H.6    Odagiri, T.7    Tashiro, M.8
  • 38
    • 84931291764 scopus 로고    scopus 로고
    • Characterization of a large cluster of influenza A(H1N1)pdm09 viruses cross-resistant to oseltamivir and peramivir during the 2013-2014 influenza season in Japan
    • Takashita E, Kiso M, Fujisaki S, Yokoyama M, Nakamura K, Shirakura M, Sato H, Odagiri T, Kawaoka Y, Tashiro M. 2015. Characterization of a large cluster of influenza A(H1N1)pdm09 viruses cross-resistant to oseltamivir and peramivir during the 2013-2014 influenza season in Japan. Antimicrob Agents Chemother 59:2607-2617. http://dx.doi.org/10.1128/AAC.04836-14.
    • (2015) Antimicrob Agents Chemother , vol.59 , pp. 2607-2617
    • Takashita, E.1    Kiso, M.2    Fujisaki, S.3    Yokoyama, M.4    Nakamura, K.5    Shirakura, M.6    Sato, H.7    Odagiri, T.8    Kawaoka, Y.9    Tashiro, M.10
  • 39
    • 0025260109 scopus 로고
    • Mechanism of antigenic variation in an individual epitope on influenza virus N9 neuraminidase
    • Air GM, Laver WG, Webster RG. 1990. Mechanism of antigenic variation in an individual epitope on influenza virus N9 neuraminidase. J Virol 64:5797-5803.
    • (1990) J Virol , vol.64 , pp. 5797-5803
    • Air, G.M.1    Laver, W.G.2    Webster, R.G.3


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