메뉴 건너뛰기




Volumn 8, Issue 2, 2013, Pages

A Novel Synthetic Receptor-Based Immunoassay for Influenza Vaccine Quantification

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA 2,3 SIALYLLACTOSIDE RECEPTOR; ALPHA 2,3 SIALYLTRANSFERASE; ALPHA 2,6 SIALYLLACTOSIDE RECEPTOR; ALPHA 2,6 SIALYLTRANSFERASE; AZIDE; INFLUENZA VACCINE; N ACETYLNEURAMINIC ACID 2,3 LACTOSE; N ACETYLNEURAMINIC ACID 2,6 LACTOSE; N ACETYLNEURAMINIC ACID DERIVATIVE; SERUM ALBUMIN; SIALIC ACID; SIALYLTRANSFERASE; UNCLASSIFIED DRUG; VIRUS HEMAGGLUTININ; VIRUS RECEPTOR;

EID: 84873720921     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0055428     Document Type: Article
Times cited : (23)

References (61)
  • 1
    • 0032712272 scopus 로고    scopus 로고
    • Epidemiology and pathogenesis of influenza
    • Zambon MC, (1999) Epidemiology and pathogenesis of influenza. J Antimicrob Chemother 44: 3-9.
    • (1999) J Antimicrob Chemother , vol.44 , pp. 3-9
    • Zambon, M.C.1
  • 2
    • 0035925678 scopus 로고    scopus 로고
    • Influenza vaccines: a review and rationale for use in developed and underdeveloped countries
    • doi:101016/S0264-410X(00)00448-5
    • Poland GA, Rottinghaus ST, Jacobson RM, (2001) Influenza vaccines: a review and rationale for use in developed and underdeveloped countries. Vaccine 19(17-19): 2216-2220 doi:10.1016/S0264-410X(00)00448-5.
    • (2001) Vaccine , vol.19 , Issue.17-19 , pp. 2216-2220
    • Poland, G.A.1    Rottinghaus, S.T.2    Jacobson, R.M.3
  • 3
    • 33746724834 scopus 로고    scopus 로고
    • Prevention and Control of Influenza: recommendations of the Advisory Committee on Immunization Practices (ACIP)
    • Smith NM, Bresee JS, Shay DK, Uyeki TM, Cox NJ, et al. (2006) Prevention and Control of Influenza: recommendations of the Advisory Committee on Immunization Practices (ACIP). MMWR Recomm Rep 55: 1-42.
    • (2006) MMWR Recomm Rep , vol.55 , pp. 1-42
    • Smith, N.M.1    Bresee, J.S.2    Shay, D.K.3    Uyeki, T.M.4    Cox, N.J.5
  • 4
    • 77649274431 scopus 로고    scopus 로고
    • Research and development of universal influenza vaccines
    • doi:101016/j.micinf.2010.01.001
    • Du L, Zhou Y, Jiang S, (2010) Research and development of universal influenza vaccines. Microbes Infect 12(4): 280-286 doi:10.1016/j.micinf.2010.01.001.
    • (2010) Microbes Infect , vol.12 , Issue.4 , pp. 280-286
    • Du, L.1    Zhou, Y.2    Jiang, S.3
  • 5
    • 0014316281 scopus 로고
    • Protective effects of specific immunity to viral neuraminidase on influenza virus infection of mice
    • Schulman JL, Khakpour M, Kilbourne ED, (1986) Protective effects of specific immunity to viral neuraminidase on influenza virus infection of mice. J Virol 2(8): 778-786.
    • (1986) J Virol , vol.2 , Issue.8 , pp. 778-786
    • Schulman, J.L.1    Khakpour, M.2    Kilbourne, E.D.3
  • 6
    • 0015969911 scopus 로고
    • The significance of influenza virus neuraminidase in immunity
    • Rott R, Becht H, Orlich M, (1974) The significance of influenza virus neuraminidase in immunity. J Gen Virol 22(1): 35-41.
    • (1974) J Gen Virol , vol.22 , Issue.1 , pp. 35-41
    • Rott, R.1    Becht, H.2    Orlich, M.3
  • 7
    • 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(10): 1037-1039.
    • (1993) Vaccine , vol.11 , Issue.10 , pp. 1037-1039
    • Johansson, B.E.1    Grajower, B.2    Kilbourne, E.D.3
  • 8
    • 33847610733 scopus 로고    scopus 로고
    • Cross-reactive neuraminidase antibodies afford partial protection against H5N1 in mice and are present in unexposed humans
    • doi:101371/journal.pmed.0040059
    • Sandbulte MR, Jimenez GS, Boon AC, Smith LR, Treanor JJ, (2007) Cross-reactive neuraminidase antibodies afford partial protection against H5N1 in mice and are present in unexposed humans. PLoS Med 4(2): e59 doi:10.1371/journal.pmed.0040059.
    • (2007) PLoS Med , vol.4 , Issue.2
    • Sandbulte, M.R.1    Jimenez, G.S.2    Boon, A.C.3    Smith, L.R.4    Treanor, J.J.5
  • 9
    • 67650679858 scopus 로고    scopus 로고
    • Protective immunity afforded by inactivated H5N1 (NIBRG-14) vaccine requires antibodies against both hemagglutinin and neuraminidase in mice
    • doi:101086/598954
    • Takahashi Y, Hasegawa H, Hara Y, Ato M, Ninomiya A, et al. (2009) Protective immunity afforded by inactivated H5N1 (NIBRG-14) vaccine requires antibodies against both hemagglutinin and neuraminidase in mice. J Infect Dis 199(11): 1629-1637 doi:10.1086/598954.
    • (2009) J Infect Dis , vol.199 , Issue.11 , pp. 1629-1637
    • Takahashi, Y.1    Hasegawa, H.2    Hara, Y.3    Ato, M.4    Ninomiya, A.5
  • 10
    • 77955553259 scopus 로고    scopus 로고
    • Qualitative and quantitative analyses of virtually all subtypes of influenza A and B viral neuraminidases using antibodies targeting the universally conserved sequences
    • doi:101016/j.vaccine.2010.06.075
    • Gravel C, Li C, Wang J, Hashem AM, Jaentschke B, et al. (2010) Qualitative and quantitative analyses of virtually all subtypes of influenza A and B viral neuraminidases using antibodies targeting the universally conserved sequences. Vaccine 28(36): 5774-5784 doi:10.1016/j.vaccine.2010.06.075.
    • (2010) Vaccine , vol.28 , Issue.36 , pp. 5774-5784
    • Gravel, C.1    Li, C.2    Wang, J.3    Hashem, A.M.4    Jaentschke, B.5
  • 11
    • 85081777687 scopus 로고    scopus 로고
    • A contributing role for anti-neuraminidase antibodies
    • doi:10.1371/journal.pone.0026335
    • Marcelin G, DuBois R, Rubrum A, Russell C, McElhaney J, et al. (2010) A contributing role for anti-neuraminidase antibodies. PloS one 6(10): e26335. doi:10.1371/journal.pone.0026335.
    • (2010) PloS one , vol.6 , Issue.10
    • Marcelin, G.1    DuBois, R.2    Rubrum, A.3    Russell, C.4    McElhaney, J.5
  • 12
    • 33645981586 scopus 로고    scopus 로고
    • Structure and receptor specificity of the hemagglutinin from an H5N1 influenza virus
    • doi:101126/science.1124513
    • Stevens J, Blixt O, Tumpey TM, Taubenberger JK, Paulson JC, et al. (2006) Structure and receptor specificity of the hemagglutinin from an H5N1 influenza virus. Science 312(5772): 404-410 doi:10.1126/science.1124513.
    • (2006) Science , vol.312 , Issue.5772 , pp. 404-410
    • Stevens, J.1    Blixt, O.2    Tumpey, T.M.3    Taubenberger, J.K.4    Paulson, J.C.5
  • 13
    • 0032899505 scopus 로고    scopus 로고
    • Comparative analysis of evolutionary mechanisms of the hemagglutinin and three internal protein genes of influenza B virus: multiple cocirculating lineages and frequent reassortment of the NP, M, and NS genes
    • Lindstrom SE, Hiromoto Y, Nishimura H, Saito T, Nerome R, et al. (1999) Comparative analysis of evolutionary mechanisms of the hemagglutinin and three internal protein genes of influenza B virus: multiple cocirculating lineages and frequent reassortment of the NP, M, and NS genes. J Virol 73(5): 4413-4426.
    • (1999) J Virol , vol.73 , Issue.5 , pp. 4413-4426
    • Lindstrom, S.E.1    Hiromoto, Y.2    Nishimura, H.3    Saito, T.4    Nerome, R.5
  • 15
    • 0027988832 scopus 로고
    • Receptor specificity in human, avian, and equine H2 and H3 influenza virus isolates
    • Connor RJ, Kawaoka Y, Webster RG, Paulson JC, (1994) Receptor specificity in human, avian, and equine H2 and H3 influenza virus isolates. Virology 205: 17-23.
    • (1994) Virology , vol.205 , pp. 17-23
    • Connor, R.J.1    Kawaoka, Y.2    Webster, R.G.3    Paulson, J.C.4
  • 16
    • 2442440593 scopus 로고    scopus 로고
    • Immunogenicity and protective efficacy of influenza vaccination
    • Hannoun C, Megas F, Piercy J, (2004) Immunogenicity and protective efficacy of influenza vaccination. Virus Res 103(1-2): 133-138.
    • (2004) Virus Res , vol.103 , Issue.1-2 , pp. 133-138
    • Hannoun, C.1    Megas, F.2    Piercy, J.3
  • 17
    • 48949089658 scopus 로고    scopus 로고
    • Prevention and control of influenza: recommendations of the Advisory Committee on Immunization Practices (ACIP)
    • Fiore AE, Shay DK, Broder K, Iskander JK, Uyeki TM, et al. (2008) Prevention and control of influenza: recommendations of the Advisory Committee on Immunization Practices (ACIP). MMWR Recomm Rep 57: 1-60.
    • (2008) MMWR Recomm Rep , vol.57 , pp. 1-60
    • Fiore, A.E.1    Shay, D.K.2    Broder, K.3    Iskander, J.K.4    Uyeki, T.M.5
  • 18
    • 0017640515 scopus 로고
    • An improved single radial-immunodiffusion technique for the assay of influenza haemagglutinin antigen: application for potency determinations of inactivated whole virus and subunit vaccines
    • Wood JM, Schild GC, Neuman RW, Seagroatt V, (1977) An improved single radial-immunodiffusion technique for the assay of influenza haemagglutinin antigen: application for potency determinations of inactivated whole virus and subunit vaccines. J Biol Stand 5(3): 237-247.
    • (1977) J Biol Stand , vol.5 , Issue.3 , pp. 237-247
    • Wood, J.M.1    Schild, G.C.2    Neuman, R.W.3    Seagroatt, V.4
  • 19
    • 80054777680 scopus 로고    scopus 로고
    • Confronting the next pandemic - Workshop on lessons learned from potency testing of pandemic (H1N1) 2009 influenza vaccines and considerations for future potency tests, Ottawa, Canada, July 27-29, 2010
    • doi:101111/j.1750-2659.2011.00250.x
    • Hardy S, Eichelberger M, Griffiths E, Weir JP, Wood D, et al. (2011) Confronting the next pandemic - Workshop on lessons learned from potency testing of pandemic (H1N1) 2009 influenza vaccines and considerations for future potency tests, Ottawa, Canada, July 27-29, 2010. Influenza Other Respi Viruses 5(6): 438-442 doi:10.1111/j.1750-2659.2011.00250.x.
    • (2011) Influenza Other Respi Viruses , vol.5 , Issue.6 , pp. 438-442
    • Hardy, S.1    Eichelberger, M.2    Griffiths, E.3    Weir, J.P.4    Wood, D.5
  • 20
    • 0027142970 scopus 로고
    • Single radial immunodiffusion as an in vitro potency assay for human inactivated viral vaccines
    • Williams MS, (1993) Single radial immunodiffusion as an in vitro potency assay for human inactivated viral vaccines. Vet Microbiol 37(3-4): 253-262.
    • (1993) Vet Microbiol , vol.37 , Issue.3-4 , pp. 253-262
    • Williams, M.S.1
  • 21
    • 0032610870 scopus 로고    scopus 로고
    • The influence of the host cell on standardisation of influenza vaccine potency
    • Wood JM, Dunleavy U, Newman RW, Riley AM, Robertson JS, et al. (1999) The influence of the host cell on standardisation of influenza vaccine potency. Dev Biol Stand 98: 183-188.
    • (1999) Dev Biol Stand , vol.98 , pp. 183-188
    • Wood, J.M.1    Dunleavy, U.2    Newman, R.W.3    Riley, A.M.4    Robertson, J.S.5
  • 23
    • 0020793305 scopus 로고
    • Reactogenicity, immunogenicity, and antibody persistence in adults given inactivated influenza virus vaccines - 1978
    • Cate TR, Couch RB, Parker D, Baxter B, (1983) Reactogenicity, immunogenicity, and antibody persistence in adults given inactivated influenza virus vaccines- 1978. Rev Infect Dis 5(4): 737-747.
    • (1983) Rev Infect Dis , vol.5 , Issue.4 , pp. 737-747
    • Cate, T.R.1    Couch, R.B.2    Parker, D.3    Baxter, B.4
  • 24
    • 0020794609 scopus 로고
    • Antigenicity and reactogenicity of influenza A/USSR/77 virus vaccine in children - a multicentered evaluation of dosage and safety
    • Wright PF, Cherry JD, Foy HM, Glezen WP, Hall CB, et al. (1983) Antigenicity and reactogenicity of influenza A/USSR/77 virus vaccine in children - a multicentered evaluation of dosage and safety. Rev Infect Dis 5(4): 758-764.
    • (1983) Rev Infect Dis , vol.5 , Issue.4 , pp. 758-764
    • Wright, P.F.1    Cherry, J.D.2    Foy, H.M.3    Glezen, W.P.4    Hall, C.B.5
  • 25
    • 0017124998 scopus 로고
    • Chromatographic isolation of the hemagglutinin polypeptides from influenza virus vaccine and determination of their amino-terminal sequences
    • Bucher DJ, Li SSL, Kehoe JM, Kilbourne ED, (1976) Chromatographic isolation of the hemagglutinin polypeptides from influenza virus vaccine and determination of their amino-terminal sequences. Proc Nat Acad Sci U S A 73(1): 238-242.
    • (1976) Proc Nat Acad Sci U S A , vol.73 , Issue.1 , pp. 238-242
    • Bucher, D.J.1    Li, S.S.L.2    Kehoe, J.M.3    Kilbourne, E.D.4
  • 26
    • 0020643099 scopus 로고
    • Gradient optimization principles in reversed-phase high-performance liquid chromatography and the separation of influenza virus components
    • Phelan MA, Cohen KA, (1983) Gradient optimization principles in reversed-phase high-performance liquid chromatography and the separation of influenza virus components. J Chromatogr 266: 55-66.
    • (1983) J Chromatogr , vol.266 , pp. 55-66
    • Phelan, M.A.1    Cohen, K.A.2
  • 27
    • 33746648119 scopus 로고    scopus 로고
    • Rapid and selective characterization of influenza virus constituents in monovalent and multivalent preparations using non-porous reversed-phase high performance liquid chromatography columns
    • doi:101016/j.chroma.2006.04.003
    • García-Cañas V, Lorbetskie B, Girard M, (2006) Rapid and selective characterization of influenza virus constituents in monovalent and multivalent preparations using non-porous reversed-phase high performance liquid chromatography columns. J Chromatogr A 1123(2): 225-232 doi:10.1016/j.chroma.2006.04.003.
    • (2006) J Chromatogr A , vol.1123 , Issue.2 , pp. 225-232
    • García-Cañas, V.1    Lorbetskie, B.2    Girard, M.3
  • 28
    • 33645061494 scopus 로고    scopus 로고
    • Haemagglutinin quantification and identification of influenza A&B strains propagated in PER.C6 cells: a novel RP-HPLC method
    • doi:101016/j.vaccine.2006.01.046
    • Kapteyn JC, Saidi MD, Dijkstra R, Kars C, Tjon JC, et al. (2006) Haemagglutinin quantification and identification of influenza A&B strains propagated in PER.C6 cells: a novel RP-HPLC method. Vaccine 24(16): 3137-3144 doi:10.1016/j.vaccine.2006.01.046.
    • (2006) Vaccine , vol.24 , Issue.16 , pp. 3137-3144
    • Kapteyn, J.C.1    Saidi, M.D.2    Dijkstra, R.3    Kars, C.4    Tjon, J.C.5
  • 29
    • 59649112550 scopus 로고    scopus 로고
    • HPLC-based quantification of haemagglutinin in the production of egg- and MDCK cell-derived influenza virus seasonal and pandemic vaccines
    • doi:101016/j.vaccine.2008.11.113
    • Kapteyn JC, Porre AM, de Rond EJ, Hessels WB, Tijms MA, et al. (2009) HPLC-based quantification of haemagglutinin in the production of egg- and MDCK cell-derived influenza virus seasonal and pandemic vaccines. Vaccine 27(9): 1468-1477 doi:10.1016/j.vaccine.2008.11.113.
    • (2009) Vaccine , vol.27 , Issue.9 , pp. 1468-1477
    • Kapteyn, J.C.1    Porre, A.M.2    de Rond, E.J.3    Hessels, W.B.4    Tijms, M.A.5
  • 30
    • 34247333472 scopus 로고    scopus 로고
    • Selective and quantitative detection of influenza virus proteins in commercial vaccines using two-dimensional high-performance liquid chromatography and fluorescence detection
    • doi:101021/ac0621120
    • García-Cañas V, Lorbetskie B, Bertrand D, Cyr TD, Girard M, (2007) Selective and quantitative detection of influenza virus proteins in commercial vaccines using two-dimensional high-performance liquid chromatography and fluorescence detection. Anal Chem 79(8): 3164-3172 doi:10.1021/ac0621120.
    • (2007) Anal Chem , vol.79 , Issue.8 , pp. 3164-3172
    • García-Cañas, V.1    Lorbetskie, B.2    Bertrand, D.3    Cyr, T.D.4    Girard, M.5
  • 31
    • 42349094160 scopus 로고    scopus 로고
    • Ultra performance liquid chromatography isotope dilution tandem mass spectrometry for the absolute quantification of proteins and peptides
    • doi:101021/ac701945h
    • Luna LG, Williams TL, Pirkle JL, Barr JR, (2008) Ultra performance liquid chromatography isotope dilution tandem mass spectrometry for the absolute quantification of proteins and peptides. Anal Chem 80(8): 2688-2693 doi:10.1021/ac701945h.
    • (2008) Anal Chem , vol.80 , Issue.8 , pp. 2688-2693
    • Luna, L.G.1    Williams, T.L.2    Pirkle, J.L.3    Barr, J.R.4
  • 32
    • 42649130016 scopus 로고    scopus 로고
    • Quantification of influenza virus hemagglutinins in complex mixtures using isotope dilution tandem mass spectrometry
    • doi:101016/j.vaccine.2008.03.014
    • Williams TL, Luna L, Guo Z, Cox NJ, Pirkle JL, et al. (2008) Quantification of influenza virus hemagglutinins in complex mixtures using isotope dilution tandem mass spectrometry. Vaccine 26(2): 2510-2520 doi:10.1016/j.vaccine.2008.03.014.
    • (2008) Vaccine , vol.26 , Issue.2 , pp. 2510-2520
    • Williams, T.L.1    Luna, L.2    Guo, Z.3    Cox, N.J.4    Pirkle, J.L.5
  • 33
    • 70350238279 scopus 로고    scopus 로고
    • Proteomics based characterization of hemagglutinins in different strains of influenza virus
    • doi:101002/prca.200800219
    • Getie-Kebtie M, Chen D, Eichelberger M, Alterman M, (2009) Proteomics based characterization of hemagglutinins in different strains of influenza virus. Proteomics Clin Appl 3(8): 979-988 doi:10.1002/prca.200800219.
    • (2009) Proteomics Clin Appl , vol.3 , Issue.8 , pp. 979-988
    • Getie-Kebtie, M.1    Chen, D.2    Eichelberger, M.3    Alterman, M.4
  • 34
    • 77956231586 scopus 로고    scopus 로고
    • Strain identification of commercial influenza vaccines by mass spectrometry
    • doi:101016/j.ab.2010.07.016
    • Creskey MC, Smith DG, Cyr TD, (2010) Strain identification of commercial influenza vaccines by mass spectrometry. Anal Biochem 406(2): 193-203 doi:10.1016/j.ab.2010.07.016.
    • (2010) Anal Biochem , vol.406 , Issue.2 , pp. 193-203
    • Creskey, M.C.1    Smith, D.G.2    Cyr, T.D.3
  • 35
    • 77950689751 scopus 로고    scopus 로고
    • Application of deglycosylation and electrophoresis to the quantification of influenza viral hemagglutinins facilitating the production of 2009 pandemic influenza (H1N1) vaccines at multiple manufacturing sites in China
    • doi:101016/j.biologicals.2009.12.004
    • Li C, Shao M, Cui X, Song Y, Li J, et al. (2010) Application of deglycosylation and electrophoresis to the quantification of influenza viral hemagglutinins facilitating the production of 2009 pandemic influenza (H1N1) vaccines at multiple manufacturing sites in China. Biologicals 38(2): 284-289 doi:10.1016/j.biologicals.2009.12.004.
    • (2010) Biologicals , vol.38 , Issue.2 , pp. 284-289
    • Li, C.1    Shao, M.2    Cui, X.3    Song, Y.4    Li, J.5
  • 36
    • 79952698089 scopus 로고    scopus 로고
    • Influenza A (H1N1) 2009 two-dose immunization of US children: An observer-blinded, randomized, placebo-controlled trial
    • doi:101016/j.vaccine.2010.12.116
    • Plennevaux E, Blatter M, Cornish MJ, Go K, Kirby D, et al. (2011) Influenza A (H1N1) 2009 two-dose immunization of US children: An observer-blinded, randomized, placebo-controlled trial. Vaccine 29(8): 1569-1575 doi:10.1016/j.vaccine.2010.12.116.
    • (2011) Vaccine , vol.29 , Issue.8 , pp. 1569-1575
    • Plennevaux, E.1    Blatter, M.2    Cornish, M.J.3    Go, K.4    Kirby, D.5
  • 37
    • 55049102432 scopus 로고    scopus 로고
    • Universal antibodies and their applications to the quantitative determination of virtually all subtypes of the influenza A viral hemagglutinins
    • doi:101016/j.vaccine.2008.09.015
    • Chun S, Li C, Van Domselaar G, Wang J, Farnsworth A, et al. (2008) Universal antibodies and their applications to the quantitative determination of virtually all subtypes of the influenza A viral hemagglutinins. Vaccine 26(48): 6068-6076 doi:10.1016/j.vaccine.2008.09.015.
    • (2008) Vaccine , vol.26 , Issue.48 , pp. 6068-6076
    • Chun, S.1    Li, C.2    Van Domselaar, G.3    Wang, J.4    Farnsworth, A.5
  • 38
    • 78649958318 scopus 로고    scopus 로고
    • Universal antibodies against the highly conserved influenza fusion peptide cross-neutralize several subtypes of influenza A virus
    • 10.1016/j.bbrc.2010.11.030
    • Hashem AM, Van Domselaar G, Li C, Wang J, She YM, et al. (2010) Universal antibodies against the highly conserved influenza fusion peptide cross-neutralize several subtypes of influenza A virus. Biochem Biophys Res Commun 403(2): 247-251 10.1016/j.bbrc.2010.11.030.
    • (2010) Biochem Biophys Res Commun , vol.403 , Issue.2 , pp. 247-251
    • Hashem, A.M.1    van Domselaar, G.2    Li, C.3    Wang, J.4    She, Y.M.5
  • 39
    • 81155124042 scopus 로고    scopus 로고
    • Recent Developments in Bioinformatics Analyses of Influenza A Virus Surface Glycoproteins and their Biological Relevance
    • Hashem AM, Doyle TM, Van Domselaar G, Farnsworth A, Li C, et al. (2011) Recent Developments in Bioinformatics Analyses of Influenza A Virus Surface Glycoproteins and their Biological Relevance. Current Bioinformatics 6(4): 415-426.
    • (2011) Current Bioinformatics , vol.6 , Issue.4 , pp. 415-426
    • Hashem, A.M.1    Doyle, T.M.2    Van Domselaar, G.3    Farnsworth, A.4    Li, C.5
  • 40
    • 75149127241 scopus 로고    scopus 로고
    • A simple slot blot for the detection of virtually all subtypes of the influenza A viral hemagglutinins using universal antibodies targeting the fusion peptide
    • doi:101038/nprot.2009.200
    • Li C, Jaentschke B, Song Y, Wang J, Cyr TD, et al. (2010) A simple slot blot for the detection of virtually all subtypes of the influenza A viral hemagglutinins using universal antibodies targeting the fusion peptide. Nat Protoc 5(1): 14-19 doi:10.1038/nprot.2009.200.
    • (2010) Nat Protoc , vol.5 , Issue.1 , pp. 14-19
    • Li, C.1    Jaentschke, B.2    Song, Y.3    Wang, J.4    Cyr, T.D.5
  • 41
    • 80355149121 scopus 로고    scopus 로고
    • Quantitative analyses of all influenza type a viral hemagglutinins and neuraminidases using universal antibodies in simple slot blot assays
    • doi:10.3791/2784
    • Gravel C, Li C, Wang J, Hashem AM, Jaentschke B, et al. (2011) Quantitative analyses of all influenza type a viral hemagglutinins and neuraminidases using universal antibodies in simple slot blot assays. J Vis Exp 50 doi:10.3791/2784. Available: http://www.jove.com/details.php?id=2784.
    • (2011) J Vis Exp , vol.50
    • Gravel, C.1    Li, C.2    Wang, J.3    Hashem, A.M.4    Jaentschke, B.5
  • 42
    • 80955158477 scopus 로고    scopus 로고
    • Avian glycan-specific IgM monoclonal antibodies for the detection and quantitation of type A and B haemagglutinins in egg-derived influenza vaccines
    • doi:101016/j.jviromet.2011.08.027
    • Legastelois I, Chevalier M, Bernard MC, de Montfort A, Fouque M, et al. (2011) Avian glycan-specific IgM monoclonal antibodies for the detection and quantitation of type A and B haemagglutinins in egg-derived influenza vaccines. J Virol Methods 178: 129-136 doi:10.1016/j.jviromet.2011.08.027.
    • (2011) J Virol Methods , vol.178 , pp. 129-136
    • Legastelois, I.1    Chevalier, M.2    Bernard, M.C.3    de Montfort, A.4    Fouque, M.5
  • 43
    • 0026698245 scopus 로고
    • A solid-phase enzyme-linked assay for influenza virus receptor-binding activity
    • Gambaryan AS, Matrosovich MN, (1992) A solid-phase enzyme-linked assay for influenza virus receptor-binding activity. J Virol Methods 39: 111-123.
    • (1992) J Virol Methods , vol.39 , pp. 111-123
    • Gambaryan, A.S.1    Matrosovich, M.N.2
  • 44
    • 8444250949 scopus 로고    scopus 로고
    • Physicochemical studies on the stability of influenza haemagglutinin in vaccine bulk material
    • Luykx DM, Casteleijn MG, Jiskoot W, Westdijk D, Jongen PM, (2004) Physicochemical studies on the stability of influenza haemagglutinin in vaccine bulk material. Eur J Pharm Sci 23(1): 65-75.
    • (2004) Eur J Pharm Sci , vol.23 , Issue.1 , pp. 65-75
    • Luykx, D.M.1    Casteleijn, M.G.2    Jiskoot, W.3    Westdijk, D.4    Jongen, P.M.5
  • 45
    • 77958572922 scopus 로고    scopus 로고
    • Enhanced Immunogenicity of Stabilized Trimeric Soluble Influenza Hemagglutinin
    • doi:101371/journal.pone.0012466
    • Weldon WC, Wang BZ, Martin MP, Koutsonanos DG, Skountzou I, et al. (2010) Enhanced Immunogenicity of Stabilized Trimeric Soluble Influenza Hemagglutinin. PLoS ONE 5(9): e12466 doi:10.1371/journal.pone.0012466.
    • (2010) PLoS ONE , vol.5 , Issue.9
    • Weldon, W.C.1    Wang, B.Z.2    Martin, M.P.3    Koutsonanos, D.G.4    Skountzou, I.5
  • 46
    • 79952702297 scopus 로고    scopus 로고
    • Antigenic stability of H1N1 pandemic vaccines correlates with vaccine strain
    • doi:101016/j.vaccine.2010.12.120
    • Farnsworth A, Cyr TD, Li C, Wang J, Li X, (2011) Antigenic stability of H1N1 pandemic vaccines correlates with vaccine strain. Vaccine 29(8): 1529-1533 doi:10.1016/j.vaccine.2010.12.120.
    • (2011) Vaccine , vol.29 , Issue.8 , pp. 1529-1533
    • Farnsworth, A.1    Cyr, T.D.2    Li, C.3    Wang, J.4    Li, X.5
  • 47
    • 79960943055 scopus 로고    scopus 로고
    • Immunogenicity of low-pH treated whole viral influenza vaccine
    • doi:101016/j.virol.2011.05.014
    • Quan FS, Li ZN, Kim MC, Yang D, Compans RW, et al. (2011) Immunogenicity of low-pH treated whole viral influenza vaccine. Virology 417(1): 196-202 doi:10.1016/j.virol.2011.05.014.
    • (2011) Virology , vol.417 , Issue.1 , pp. 196-202
    • Quan, F.S.1    Li, Z.N.2    Kim, M.C.3    Yang, D.4    Compans, R.W.5
  • 48
    • 84864310550 scopus 로고    scopus 로고
    • Modifying the thermostability of inactivated influenza vaccines
    • doi:101016/j.vaccine.2012.06.051
    • Bliu A, Lemieux M, Li C, Li X, Wang J, et al. (2012) Modifying the thermostability of inactivated influenza vaccines. Vaccine 30: 5506-5511 doi:10.1016/j.vaccine.2012.06.051.
    • (2012) Vaccine , vol.30 , pp. 5506-5511
    • Bliu, A.1    Lemieux, M.2    Li, C.3    Li, X.4    Wang, J.5
  • 49
    • 39649119640 scopus 로고    scopus 로고
    • GM3, GM2 and GM1 mimics designed for biosensing: chemoenzymatic synthesis, target affinities and 900 MHz NMR analysis
    • doi:101016/j.carres.2008.01.007
    • Pukin AV, Weijers CA, van Lagen B, Wechselberger R, Sun B, et al. (2008) GM3, GM2 and GM1 mimics designed for biosensing: chemoenzymatic synthesis, target affinities and 900 MHz NMR analysis. Carbohydr Res 343(4): 636-650 doi:10.1016/j.carres.2008.01.007.
    • (2008) Carbohydr Res , vol.343 , Issue.4 , pp. 636-650
    • Pukin, A.V.1    Weijers, C.A.2    van Lagen, B.3    Wechselberger, R.4    Sun, B.5
  • 50
    • 37549044252 scopus 로고    scopus 로고
    • Crystal structure of Vibrionaceae Photobacterium sp. JT-ISH-224 alpha2,6-sialyltransferase in a ternary complex with donor product CMP and acceptor substrate lactose: catalytic mechanism and substrate recognition
    • doi:101093/glycob/cwm119
    • Kakuta Y, Okino N, Kajiwara H, Ichikawa M, Takakura Y, et al. (2008) Crystal structure of Vibrionaceae Photobacterium sp. JT-ISH-224 alpha2,6-sialyltransferase in a ternary complex with donor product CMP and acceptor substrate lactose: catalytic mechanism and substrate recognition. Glycobiology 18(1): 66-73 doi:10.1093/glycob/cwm119.
    • (2008) Glycobiology , vol.18 , Issue.1 , pp. 66-73
    • Kakuta, Y.1    Okino, N.2    Kajiwara, H.3    Ichikawa, M.4    Takakura, Y.5
  • 51
    • 39049097535 scopus 로고    scopus 로고
    • Photobacterium sp. JT-ISH-224 produces two sialyltransferases, alpha-/beta-galactoside alpha2,3-sialyltransferase and beta-galactoside alpha2,6-sialyltransferase
    • doi:101093/jb/mvm208
    • Tsukamoto H, Takakura Y, Mine T, Yamamoto T, (2008) Photobacterium sp. JT-ISH-224 produces two sialyltransferases, alpha-/beta-galactoside alpha2,3-sialyltransferase and beta-galactoside alpha2,6-sialyltransferase. J Biochem 143(2): 187-197 doi:10.1093/jb/mvm208.
    • (2008) J Biochem , vol.143 , Issue.2 , pp. 187-197
    • Tsukamoto, H.1    Takakura, Y.2    Mine, T.3    Yamamoto, T.4
  • 52
    • 77952543565 scopus 로고    scopus 로고
    • A direct NMR method for the measurement of competitive kinetic isotope effects
    • doi:101038/nchembio.352
    • Chan J, Lewis AR, Gilbert M, Karwaski MF, Bennet AJ, (2010) A direct NMR method for the measurement of competitive kinetic isotope effects. Nat Chem Biol 6(6): 405-407 doi:10.1038/nchembio.352.
    • (2010) Nat Chem Biol , vol.6 , Issue.6 , pp. 405-407
    • Chan, J.1    Lewis, A.R.2    Gilbert, M.3    Karwaski, M.F.4    Bennet, A.J.5
  • 53
    • 2942593754 scopus 로고    scopus 로고
    • Bioengineering of surface GD3 ganglioside for immunotargeting human melanoma cells
    • doi:101074/jbc.M402787200
    • Zou W, Borrelli S, Gilbert M, Liu T, Pon RA, et al. (2004) Bioengineering of surface GD3 ganglioside for immunotargeting human melanoma cells. J Biol Chem 279(24): 25390-25399 doi:10.1074/jbc.M402787200.
    • (2004) J Biol Chem , vol.279 , Issue.24 , pp. 25390-25399
    • Zou, W.1    Borrelli, S.2    Gilbert, M.3    Liu, T.4    Pon, R.A.5
  • 54
    • 0041113516 scopus 로고    scopus 로고
    • Mimics of the structural elements of Type III Group B Streptococcus capsular polysaccharide. Part II: Synthesis of a carboxylate-containing hexasaccharide with a short spacer
    • doi:101080/07328309608005653
    • Zou W, Jennings HJ, (1996) Mimics of the structural elements of Type III Group B Streptococcus capsular polysaccharide. Part II: Synthesis of a carboxylate-containing hexasaccharide with a short spacer. J Carbohydr Chem 15: 279-295 doi:10.1080/07328309608005653.
    • (1996) J Carbohydr Chem , vol.15 , pp. 279-295
    • Zou, W.1    Jennings, H.J.2
  • 55
    • 84860715168 scopus 로고    scopus 로고
    • Subcutaneous immunization with recombinant adenovirus expressing influenza A nucleoprotein protects mice against lethal viral challenge
    • Hashem AM, Jaentschke B, Gravel C, Tocchi M, Doyle TM, et al. (2012) Subcutaneous immunization with recombinant adenovirus expressing influenza A nucleoprotein protects mice against lethal viral challenge. Hum Vaccin Immunother 8(4): 425-430.
    • (2012) Hum Vaccin Immunother , vol.8 , Issue.4 , pp. 425-430
    • Hashem, A.M.1    Jaentschke, B.2    Gravel, C.3    Tocchi, M.4    Doyle, T.M.5
  • 56
    • 0022931059 scopus 로고
    • Single-radial-immunodiffusion potency tests of inactivated influenza vaccines for use in man and animals
    • Wood JM, Mumford J, Schild GC, Webster RG, Nicholson KG, (1986) Single-radial-immunodiffusion potency tests of inactivated influenza vaccines for use in man and animals. Dev Biol Stand 64: 169-177.
    • (1986) Dev Biol Stand , vol.64 , pp. 169-177
    • Wood, J.M.1    Mumford, J.2    Schild, G.C.3    Webster, R.G.4    Nicholson, K.G.5
  • 57
    • 0029962092 scopus 로고    scopus 로고
    • Use of diethyl squarate for the coupling of oligosaccharide amines to carrier proteins and characterization of the resulting neoglycoproteins by MALDI-TOF mass spectrometry
    • Vivekanand PK, Diedrich P, Hindsgaul O, (1996) Use of diethyl squarate for the coupling of oligosaccharide amines to carrier proteins and characterization of the resulting neoglycoproteins by MALDI-TOF mass spectrometry. Glycoconj J 13(2): 315-319.
    • (1996) Glycoconj J , vol.13 , Issue.2 , pp. 315-319
    • Vivekanand, P.K.1    Diedrich, P.2    Hindsgaul, O.3
  • 58
    • 84863129288 scopus 로고    scopus 로고
    • Characterization of glycan binding specificities of influenza B viruses with correlation with hemagglutinin genotypes and clinical features
    • doi:101002/jmv.23219
    • Wang YF, Chang CF, Chi CY, Wang HC, Wang JR, et al. (2012) Characterization of glycan binding specificities of influenza B viruses with correlation with hemagglutinin genotypes and clinical features. J Med Virol 84(4): 679-685 doi:10.1002/jmv.23219.
    • (2012) J Med Virol , vol.84 , Issue.4 , pp. 679-685
    • Wang, Y.F.1    Chang, C.F.2    Chi, C.Y.3    Wang, H.C.4    Wang, J.R.5
  • 59
    • 0023574003 scopus 로고
    • Anti-peptide antibodies detect steps in a protein conformational change: low-pH activation of the influenza virus hemagglutinin
    • White JM, Wilson IA, (1987) Anti-peptide antibodies detect steps in a protein conformational change: low-pH activation of the influenza virus hemagglutinin. J Cell Biol 105(6 Pt 2): 2887-2896.
    • (1987) J Cell Biol , vol.105 , Issue.6 Pt 2 , pp. 2887-2896
    • White, J.M.1    Wilson, I.A.2
  • 60
    • 18844470928 scopus 로고    scopus 로고
    • Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation
    • doi:101016/S0092-8674(00)81771-7
    • Chen J, Lee KH, Steinhauer DA, Stevens DJ, Skehel JJ, et al. (1998) Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation. Cell 95: 409-417 doi:10.1016/S0092-8674(00)81771-7.
    • (1998) Cell , vol.95 , pp. 409-417
    • Chen, J.1    Lee, K.H.2    Steinhauer, D.A.3    Stevens, D.J.4    Skehel, J.J.5
  • 61
    • 0027210034 scopus 로고
    • Probing of the receptor-binding sites of the H1 and H3 influenza A and influenza B virus hemagglutinins by synthetic and natural sialosides
    • Matrosovich MN, Gambaryan AS, Tuzikov AB, Byramova NE, Mochalova LV, et al. (1993) Probing of the receptor-binding sites of the H1 and H3 influenza A and influenza B virus hemagglutinins by synthetic and natural sialosides. Virology 195: 111-121.
    • (1993) Virology , vol.195 , pp. 111-121
    • Matrosovich, M.N.1    Gambaryan, A.S.2    Tuzikov, A.B.3    Byramova, N.E.4    Mochalova, L.V.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.