메뉴 건너뛰기




Volumn 12, Issue 8, 2013, Pages 3707-3720

Comparative glycomics analysis of influenza hemagglutinin (H5N1) produced in vaccine relevant cell platforms

Author keywords

cell substrate; glycosylation; hemagglutinin; influenza; mass spectrometry; MSE; NetNGlyc; permethylation

Indexed keywords

HEMAGGLUTININ; INFLUENZA VACCINE;

EID: 84881141968     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr400329k     Document Type: Article
Times cited : (55)

References (81)
  • 1
    • 84881173099 scopus 로고    scopus 로고
    • WHO. Influenza(Seasonal)
    • WHO. Influenza(Seasonal). http://www.who.int/mediacentre/factsheets/ fs211/en/.
  • 3
    • 84881180945 scopus 로고    scopus 로고
    • WHO
    • WHO, http://www.who.int/influenza/vaccines/virus/ avianinfluenzastrains2006/en/.
  • 4
    • 84858700318 scopus 로고    scopus 로고
    • Regulatory, biosafety and safety challenges for novel cells as substrates for human vaccines
    • Hess, R. D.; Weber, F.; Watson, K.; Schmitt, S. Regulatory, biosafety and safety challenges for novel cells as substrates for human vaccines Vaccine 2012, 30 (17) 2715-27
    • (2012) Vaccine , vol.30 , Issue.17 , pp. 2715-2727
    • Hess, R.D.1    Weber, F.2    Watson, K.3    Schmitt, S.4
  • 7
    • 77954951040 scopus 로고    scopus 로고
    • Trichoplusia ni cells (High Five) are highly efficient for the production of influenza A virus-like particles: A comparison of two insect cell lines as production platforms for influenza vaccines
    • Krammer, F.; Schinko, T.; Palmberger, D.; Tauer, C.; Messner, P.; Grabherr, R. Trichoplusia ni cells (High Five) are highly efficient for the production of influenza A virus-like particles: a comparison of two insect cell lines as production platforms for influenza vaccines Mol. Biotechnol. 2010, 45 (3) 226-234
    • (2010) Mol. Biotechnol. , vol.45 , Issue.3 , pp. 226-234
    • Krammer, F.1    Schinko, T.2    Palmberger, D.3    Tauer, C.4    Messner, P.5    Grabherr, R.6
  • 8
    • 38649140512 scopus 로고    scopus 로고
    • Progress on baculovirus-derived influenza vaccines
    • Cox, M. M. Progress on baculovirus-derived influenza vaccines Curr. Opin. Mol. Ther. 2008, 10 (1) 56-61
    • (2008) Curr. Opin. Mol. Ther. , vol.10 , Issue.1 , pp. 56-61
    • Cox, M.M.1
  • 9
    • 32844456405 scopus 로고    scopus 로고
    • Expression and purification of an influenza hemagglutinin - One step closer to a recombinant protein-based influenza vaccine
    • Wang, K.; Holtz, K. M.; Anderson, K.; Chubet, R.; Mahmoud, W.; Cox, M. M. Expression and purification of an influenza hemagglutinin - one step closer to a recombinant protein-based influenza vaccine Vaccine 2006, 24 (12) 2176-2185
    • (2006) Vaccine , vol.24 , Issue.12 , pp. 2176-2185
    • Wang, K.1    Holtz, K.M.2    Anderson, K.3    Chubet, R.4    Mahmoud, W.5    Cox, M.M.6
  • 10
    • 4444376554 scopus 로고    scopus 로고
    • Effect of the addition of oligosaccharides on the biological activities and antigenicity of influenza A/H3N2 virus hemagglutinin
    • Abe, Y.; Takashita, E.; Sugawara, K.; Matsuzaki, Y.; Muraki, Y.; Hongo, S. Effect of the addition of oligosaccharides on the biological activities and antigenicity of influenza A/H3N2 virus hemagglutinin J. Virol. 2004, 78 (18) 9605-9611
    • (2004) J. Virol. , vol.78 , Issue.18 , pp. 9605-9611
    • Abe, Y.1    Takashita, E.2    Sugawara, K.3    Matsuzaki, Y.4    Muraki, Y.5    Hongo, S.6
  • 11
    • 0020579632 scopus 로고
    • Studies on the role of glycosylation in the functions and antigenic properties of influenza virus glycoproteins
    • Basak, S.; Compans, R. W. Studies on the role of glycosylation in the functions and antigenic properties of influenza virus glycoproteins Virology 1983, 128 (1) 77-91
    • (1983) Virology , vol.128 , Issue.1 , pp. 77-91
    • Basak, S.1    Compans, R.W.2
  • 12
    • 0344406204 scopus 로고    scopus 로고
    • Impact of glycosylation on the immunogenicity of a DNA-based influenza H5 HA vaccine
    • Bright, R. A.; Ross, T. M.; Subbarao, K.; Robinson, H. L.; Katz, J. M. Impact of glycosylation on the immunogenicity of a DNA-based influenza H5 HA vaccine Virology 2003, 308 (2) 270-278
    • (2003) Virology , vol.308 , Issue.2 , pp. 270-278
    • Bright, R.A.1    Ross, T.M.2    Subbarao, K.3    Robinson, H.L.4    Katz, J.M.5
  • 14
    • 84857072874 scopus 로고    scopus 로고
    • Prediction of Biological Functions on Glycosylation Site Migrations in Human Influenza H1N1 Viruses
    • Sun, S. S.; Wang, Q. Z.; Zhao, F.; Chen, W. T.; Li, Z. Prediction of Biological Functions on Glycosylation Site Migrations in Human Influenza H1N1 Viruses PLoS One 2012, 7, 2
    • (2012) PLoS One , vol.7 , pp. 2
    • Sun, S.S.1    Wang, Q.Z.2    Zhao, F.3    Chen, W.T.4    Li, Z.5
  • 15
    • 0022931080 scopus 로고
    • Use of the single radial immunodiffusion test as a replacement for the NIH mouse potency test for rabies vaccine
    • Fitzgerald, E. A.; Needy, C. F. Use of the single radial immunodiffusion test as a replacement for the NIH mouse potency test for rabies vaccine Dev. Biol. Stand. 1986, 64, 73-79
    • (1986) Dev. Biol. Stand. , vol.64 , pp. 73-79
    • Fitzgerald, E.A.1    Needy, C.F.2
  • 16
    • 0027142970 scopus 로고
    • Single-radial-immunodiffusion as an in vitro potency assay for human inactivated viral vaccines
    • Williams, M. S. Single-radial-immunodiffusion as an in vitro potency assay for human inactivated viral vaccines Vet. Microbiol. 1993, 37 (3-4) 253-262
    • (1993) Vet. Microbiol. , vol.37 , Issue.34 , pp. 253-262
    • Williams, M.S.1
  • 17
    • 84867898126 scopus 로고    scopus 로고
    • Pandemic influenza vaccine: Characterization of A/California/07/2009 (H1N1) recombinant hemagglutinin protein and insights into H1N1 antigen stability
    • Feshchenko, E.; Rhodes, D. G.; Felberbaum, R.; McPherson, C.; Rininger, J. A.; Post, P.; Cox, M. M. Pandemic influenza vaccine: characterization of A/California/07/2009 (H1N1) recombinant hemagglutinin protein and insights into H1N1 antigen stability BMC Biotechnol. 2012, 12, 77
    • (2012) BMC Biotechnol. , vol.12 , pp. 77
    • Feshchenko, E.1    Rhodes, D.G.2    Felberbaum, R.3    McPherson, C.4    Rininger, J.A.5    Post, P.6    Cox, M.M.7
  • 18
    • 33846187538 scopus 로고    scopus 로고
    • The role of protein glycosylation in allergy
    • Altmann, F. The role of protein glycosylation in allergy Int. Arch. Allergy Immunol. 2007, 142 (2) 99-115
    • (2007) Int. Arch. Allergy Immunol. , vol.142 , Issue.2 , pp. 99-115
    • Altmann, F.1
  • 20
    • 33645572819 scopus 로고    scopus 로고
    • Construction of eukaryotic expressing plasmids for HA and HA1 of influenza A virus and their transient expression in HEK293 cells
    • Zhang, W. D.; Ca, K.; Li, M. Y.; Shi, Q. F.; Wang, B. N.; Jiang, Z. H.; Li, H. [Construction of eukaryotic expressing plasmids for HA and HA1 of influenza A virus and their transient expression in HEK293 cells] Sichuan Da Xue Xue Bao Yi Xue Ban 2006, 37 (2) 176-179
    • (2006) Sichuan da Xue Xue Bao Yi Xue Ban , vol.37 , Issue.2 , pp. 176-179
    • Zhang, W.D.1    Ca, K.2    Li, M.Y.3    Shi, Q.F.4    Wang, B.N.5    Jiang, Z.H.6    Li, H.7
  • 21
    • 14244249300 scopus 로고    scopus 로고
    • Cell-based protein vaccines for influenza
    • Cox, M. M. Cell-based protein vaccines for influenza Curr. Opin. Mol. Ther. 2005, 7 (1) 24-29
    • (2005) Curr. Opin. Mol. Ther. , vol.7 , Issue.1 , pp. 24-29
    • Cox, M.M.1
  • 22
    • 79960652218 scopus 로고    scopus 로고
    • A fast track influenza virus vaccine produced in insect cells
    • Cox, M. M.; Hashimoto, Y. A fast track influenza virus vaccine produced in insect cells J. Invertebr. Pathol. 2011, 107 (Suppl) S31-S41
    • (2011) J. Invertebr. Pathol. , vol.107 , Issue.SUPPL.
    • Cox, M.M.1    Hashimoto, Y.2
  • 23
    • 80053537874 scopus 로고    scopus 로고
    • Characterization of a recombinant influenza vaccine candidate using complementary LC-MS methods
    • Xie, H.; Doneanu, C.; Chen, W.; Rininger, J.; Mazzeo, J. R. Characterization of a recombinant influenza vaccine candidate using complementary LC-MS methods Curr. Pharm. Biotechnol. 2011, 12 (10) 1568-1579
    • (2011) Curr. Pharm. Biotechnol. , vol.12 , Issue.10 , pp. 1568-1579
    • Xie, H.1    Doneanu, C.2    Chen, W.3    Rininger, J.4    Mazzeo, J.R.5
  • 24
    • 0035886994 scopus 로고    scopus 로고
    • Qualitative and quantitative analysis of the glycosylation pattern of recombinant proteins
    • Viseux, N.; Hronowski, X.; Delaney, J.; Domon, B. Qualitative and quantitative analysis of the glycosylation pattern of recombinant proteins Anal. Chem. 2001, 73 (20) 4755-4762
    • (2001) Anal. Chem. , vol.73 , Issue.20 , pp. 4755-4762
    • Viseux, N.1    Hronowski, X.2    Delaney, J.3    Domon, B.4
  • 25
    • 33846874141 scopus 로고    scopus 로고
    • Construction and characterization of new piggyBac vectors for constitutive or inducible expression of heterologous gene pairs and the identification of a previously unrecognized activator sequence in piggyBac
    • Shi, X.; Harrison, R. L.; Hollister, J. R.; Mohammed, A.; Fraser, M. J., Jr.; Jarvis, D. L. Construction and characterization of new piggyBac vectors for constitutive or inducible expression of heterologous gene pairs and the identification of a previously unrecognized activator sequence in piggyBac BMC Biotechnol. 2007, 7, 5
    • (2007) BMC Biotechnol. , vol.7 , pp. 5
    • Shi, X.1    Harrison, R.L.2    Hollister, J.R.3    Mohammed, A.4    Fraser Jr., M.J.5    Jarvis, D.L.6
  • 26
    • 36048982078 scopus 로고    scopus 로고
    • Transforming lepidopteran insect cells for improved protein processing
    • Harrison, R. L.; Jarvis, D. L. Transforming lepidopteran insect cells for improved protein processing Methods Mol. Biol. 2007, 388, 341-356
    • (2007) Methods Mol. Biol. , vol.388 , pp. 341-356
    • Harrison, R.L.1    Jarvis, D.L.2
  • 27
    • 36049050599 scopus 로고    scopus 로고
    • Transforming lepidopteran insect cells for continuous recombinant protein expression
    • Harrison, R. L.; Jarvis, D. L. Transforming lepidopteran insect cells for continuous recombinant protein expression Methods Mol. Biol. 2007, 388, 299-316
    • (2007) Methods Mol. Biol. , vol.388 , pp. 299-316
    • Harrison, R.L.1    Jarvis, D.L.2
  • 28
    • 0029769504 scopus 로고    scopus 로고
    • Modifying the insect cell N -glycosylation pathway with immediate early baculovirus expression vectors
    • Jarvis, D. L.; Finn, E. E. Modifying the insect cell N -glycosylation pathway with immediate early baculovirus expression vectors Nat. Biotechnol. 1996, 14 (10) 1288-1292
    • (1996) Nat. Biotechnol. , vol.14 , Issue.10 , pp. 1288-1292
    • Jarvis, D.L.1    Finn, E.E.2
  • 29
    • 79957740403 scopus 로고    scopus 로고
    • An unbiased approach for analysis of protein glycosylation and application to influenza vaccine hemagglutinin
    • An, Y.; Cipollo, J. F. An unbiased approach for analysis of protein glycosylation and application to influenza vaccine hemagglutinin Anal. Biochem. 2011, 415 (1) 67-80
    • (2011) Anal. Biochem. , vol.415 , Issue.1 , pp. 67-80
    • An, Y.1    Cipollo, J.F.2
  • 30
    • 69549088131 scopus 로고    scopus 로고
    • Structural analysis of sulfated glycans by sequential double-permethylation using methyl iodide and deuteromethyl iodide
    • Lei, M.; Mechref, Y.; Novotny, M. V. Structural analysis of sulfated glycans by sequential double-permethylation using methyl iodide and deuteromethyl iodide J. Am. Soc. Mass Spectrom. 2009, 20 (9) 1660-1671
    • (2009) J. Am. Soc. Mass Spectrom. , vol.20 , Issue.9 , pp. 1660-1671
    • Lei, M.1    Mechref, Y.2    Novotny, M.V.3
  • 31
    • 39749147631 scopus 로고    scopus 로고
    • Separation efficiencies in hydrophilic interaction chromatography
    • Ikegami, T.; Tomomatsu, K.; Takubo, H.; Horie, K.; Tanaka, N. Separation efficiencies in hydrophilic interaction chromatography J. Chromatogr., A 2008, 1184 (1-2) 474-503
    • (2008) J. Chromatogr., A , vol.1184 , Issue.12 , pp. 474-503
    • Ikegami, T.1    Tomomatsu, K.2    Takubo, H.3    Horie, K.4    Tanaka, N.5
  • 32
    • 83755205441 scopus 로고    scopus 로고
    • Recent advances in hydrophilic interaction liquid chromatography (HILIC) for structural glycomics
    • Zauner, G.; Deelder, A. M.; Wuhrer, M. Recent advances in hydrophilic interaction liquid chromatography (HILIC) for structural glycomics Electrophoresis 2011, 32 (24) 3456-3466
    • (2011) Electrophoresis , vol.32 , Issue.24 , pp. 3456-3466
    • Zauner, G.1    Deelder, A.M.2    Wuhrer, M.3
  • 33
    • 48849109894 scopus 로고    scopus 로고
    • Assessment of lectin and HILIC based enrichment protocols for characterization of serum glycoproteins by mass spectrometry
    • Calvano, C. D.; Zambonin, C. G.; Jensen, O. N. Assessment of lectin and HILIC based enrichment protocols for characterization of serum glycoproteins by mass spectrometry J. Proteomics 2008, 71 (3) 304-17
    • (2008) J. Proteomics , vol.71 , Issue.3 , pp. 304-317
    • Calvano, C.D.1    Zambonin, C.G.2    Jensen, O.N.3
  • 34
    • 8644240243 scopus 로고    scopus 로고
    • Hydrophilic affinity isolation and MALDI multiple-stage tandem mass spectrometry of glycopeptides for glycoproteomics
    • Wada, Y.; Tajiri, M.; Yoshida, S. Hydrophilic affinity isolation and MALDI multiple-stage tandem mass spectrometry of glycopeptides for glycoproteomics Anal. Chem. 2004, 76 (22) 6560-6565
    • (2004) Anal. Chem. , vol.76 , Issue.22 , pp. 6560-6565
    • Wada, Y.1    Tajiri, M.2    Yoshida, S.3
  • 35
    • 84864128566 scopus 로고    scopus 로고
    • Fully automatable two-dimensional hydrophilic interaction liquid chromatography-reversed phase liquid chromatography with online tandem mass spectrometry for shotgun proteomics
    • Zhao, Y.; Kong, R. P.; Li, G.; Lam, M. P.; Law, C. H.; Lee, S. M.; Lam, H. C.; Chu, I. K. Fully automatable two-dimensional hydrophilic interaction liquid chromatography-reversed phase liquid chromatography with online tandem mass spectrometry for shotgun proteomics J. Sep. Sci. 2012, 35 (14) 1755-1763
    • (2012) J. Sep. Sci. , vol.35 , Issue.14 , pp. 1755-1763
    • Zhao, Y.1    Kong, R.P.2    Li, G.3    Lam, M.P.4    Law, C.H.5    Lee, S.M.6    Lam, H.C.7    Chu, I.K.8
  • 36
    • 63049138916 scopus 로고    scopus 로고
    • Database searching and accounting of multiplexed precursor and product ion spectra from the data independent analysis of simple and complex peptide mixtures
    • Li, G. Z.; Vissers, J. P.; Silva, J. C.; Golick, D.; Gorenstein, M. V.; Geromanos, S. J. Database searching and accounting of multiplexed precursor and product ion spectra from the data independent analysis of simple and complex peptide mixtures Proteomics 2009, 9 (6) 1696-1719
    • (2009) Proteomics , vol.9 , Issue.6 , pp. 1696-1719
    • Li, G.Z.1    Vissers, J.P.2    Silva, J.C.3    Golick, D.4    Gorenstein, M.V.5    Geromanos, S.J.6
  • 37
    • 63049084861 scopus 로고    scopus 로고
    • The detection, correlation, and comparison of peptide precursor and product ions from data independent LC-MS with data dependant LC-MS/MS
    • Geromanos, S. J.; Vissers, J. P.; Silva, J. C.; Dorschel, C. A.; Li, G. Z.; Gorenstein, M. V.; Bateman, R. H.; Langridge, J. I. The detection, correlation, and comparison of peptide precursor and product ions from data independent LC-MS with data dependant LC-MS/MS Proteomics 2009, 9 (6) 1683-1695
    • (2009) Proteomics , vol.9 , Issue.6 , pp. 1683-1695
    • Geromanos, S.J.1    Vissers, J.P.2    Silva, J.C.3    Dorschel, C.A.4    Li, G.Z.5    Gorenstein, M.V.6    Bateman, R.H.7    Langridge, J.I.8
  • 38
    • 0035170507 scopus 로고    scopus 로고
    • GlycoSuiteDB: A new curated relational database of glycoprotein glycan structures and their biological sources
    • Cooper, C. A.; Harrison, M. J.; Wilkins, M. R.; Packer, N. H. GlycoSuiteDB: a new curated relational database of glycoprotein glycan structures and their biological sources Nucleic Acids Res. 2001, 29 (1) 332-335
    • (2001) Nucleic Acids Res. , vol.29 , Issue.1 , pp. 332-335
    • Cooper, C.A.1    Harrison, M.J.2    Wilkins, M.R.3    Packer, N.H.4
  • 39
    • 0037250530 scopus 로고    scopus 로고
    • GlycoSuiteDB: A curated relational database of glycoprotein glycan structures and their biological sources. 2003 update
    • Cooper, C. A.; Joshi, H. J.; Harrison, M. J.; Wilkins, M. R.; Packer, N. H. GlycoSuiteDB: a curated relational database of glycoprotein glycan structures and their biological sources. 2003 update Nucleic Acids Res. 2003, 31 (1) 511-513
    • (2003) Nucleic Acids Res. , vol.31 , Issue.1 , pp. 511-513
    • Cooper, C.A.1    Joshi, H.J.2    Harrison, M.J.3    Wilkins, M.R.4    Packer, N.H.5
  • 42
    • 22544463401 scopus 로고    scopus 로고
    • N-Glycans of Caenorhabditis elegans are specific to developmental stages
    • Cipollo, J. F.; Awad, A. M.; Costello, C. E.; Hirschberg, C. B. N-Glycans of Caenorhabditis elegans are specific to developmental stages J. Biol. Chem. 2005, 280 (28) 26063-26072
    • (2005) J. Biol. Chem. , vol.280 , Issue.28 , pp. 26063-26072
    • Cipollo, J.F.1    Awad, A.M.2    Costello, C.E.3    Hirschberg, C.B.4
  • 43
    • 34548681626 scopus 로고    scopus 로고
    • A glycomics platform for the analysis of permethylated oligosaccharide alditols
    • Costello, C. E.; Contado-Miller, J. M.; Cipollo, J. F. A glycomics platform for the analysis of permethylated oligosaccharide alditols J. Am. Soc. Mass Spectrom. 2007, 18 (10) 1799-1812
    • (2007) J. Am. Soc. Mass Spectrom. , vol.18 , Issue.10 , pp. 1799-1812
    • Costello, C.E.1    Contado-Miller, J.M.2    Cipollo, J.F.3
  • 44
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • Kornfeld, R.; Kornfeld, S. Assembly of asparagine-linked oligosaccharides Annu. Rev. Biochem. 1985, 54, 631-664
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 46
    • 0142135856 scopus 로고    scopus 로고
    • Determination of N-glycosylation sites and site heterogeneity in glycoproteins
    • An, H. J.; Peavy, T. R.; Hedrick, J. L.; Lebrilla, C. B. Determination of N-glycosylation sites and site heterogeneity in glycoproteins Anal. Chem. 2003, 75 (20) 5628-5637
    • (2003) Anal. Chem. , vol.75 , Issue.20 , pp. 5628-5637
    • An, H.J.1    Peavy, T.R.2    Hedrick, J.L.3    Lebrilla, C.B.4
  • 47
    • 0023878299 scopus 로고
    • The covalent structure of individual N-linked glycopeptides from ovomucoid and asialofetuin
    • Yet, M. G.; Chin, C. C.; Wold, F. The covalent structure of individual N-linked glycopeptides from ovomucoid and asialofetuin J. Biol. Chem. 1988, 263 (1) 111-117
    • (1988) J. Biol. Chem. , vol.263 , Issue.1 , pp. 111-117
    • Yet, M.G.1    Chin, C.C.2    Wold, F.3
  • 48
    • 84868243289 scopus 로고    scopus 로고
    • Unexpected mucin-type O-glycosylation and host-specific N-glycosylation of human recombinant interleukin-17A expressed in a human kidney cell line
    • Geoghegan, K. F.; Song, X.; Hoth, L. R.; Feng, X.; Shanker, S.; Quazi, A.; Luxenberg, D. P.; Wright, J. F.; Griffor, M. C. Unexpected mucin-type O-glycosylation and host-specific N-glycosylation of human recombinant interleukin-17A expressed in a human kidney cell line Protein Expression Purif. 2013, 87 (1) 27-34
    • (2013) Protein Expression Purif. , vol.87 , Issue.1 , pp. 27-34
    • Geoghegan, K.F.1    Song, X.2    Hoth, L.R.3    Feng, X.4    Shanker, S.5    Quazi, A.6    Luxenberg, D.P.7    Wright, J.F.8    Griffor, M.C.9
  • 49
    • 84865058631 scopus 로고    scopus 로고
    • Structures and biosynthesis of the N- and O-glycans of recombinant human oviduct-specific glycoprotein expressed in human embryonic kidney cells
    • Yang, X.; Tao, S.; Orlando, R.; Brockhausen, I.; Kan, F. W. Structures and biosynthesis of the N- and O-glycans of recombinant human oviduct-specific glycoprotein expressed in human embryonic kidney cells Carbohydr. Res. 2012, 358, 47-55
    • (2012) Carbohydr. Res. , vol.358 , pp. 47-55
    • Yang, X.1    Tao, S.2    Orlando, R.3    Brockhausen, I.4    Kan, F.W.5
  • 50
    • 0020713174 scopus 로고
    • Structural requirements of N-glycosylation of proteins. Studies with proline peptides as conformational probes
    • Bause, E. Structural requirements of N-glycosylation of proteins. Studies with proline peptides as conformational probes Biochem. J. 1983, 209 (2) 331-336
    • (1983) Biochem. J. , vol.209 , Issue.2 , pp. 331-336
    • Bause, E.1
  • 51
    • 79956357741 scopus 로고    scopus 로고
    • Do N-glycoproteins have preference for specific sequons?
    • Rao, R. S.; Bernd, W. Do N-glycoproteins have preference for specific sequons? Bioinformation 2010, 5 (5) 208-212
    • (2010) Bioinformation , vol.5 , Issue.5 , pp. 208-212
    • Rao, R.S.1    Bernd, W.2
  • 52
    • 0035261661 scopus 로고    scopus 로고
    • GlycoMod - A software tool for determining glycosylation compositions from mass spectrometric data
    • Cooper, C. A.; Gasteiger, E.; Packer, N. H. GlycoMod - a software tool for determining glycosylation compositions from mass spectrometric data Proteomics 2001, 1 (2) 340-349
    • (2001) Proteomics , vol.1 , Issue.2 , pp. 340-349
    • Cooper, C.A.1    Gasteiger, E.2    Packer, N.H.3
  • 53
    • 69449094891 scopus 로고    scopus 로고
    • Darwinian selection for sites of Asn-linked glycosylation in phylogenetically disparate eukaryotes and viruses
    • Cui, J.; Smith, T.; Robbins, P. W.; Samuelson, J. Darwinian selection for sites of Asn-linked glycosylation in phylogenetically disparate eukaryotes and viruses Proc. Natl. Acad. Sci. U.S.A. 2009, 106 (32) 13421-13426
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , Issue.32 , pp. 13421-13426
    • Cui, J.1    Smith, T.2    Robbins, P.W.3    Samuelson, J.4
  • 54
  • 55
    • 34447250320 scopus 로고    scopus 로고
    • Direct ex vivo analyses of HLA-DR1 transgenic mice reveal an exceptionally broad pattern of immunodominance in the primary HLA-DR1-restricted CD4 T-cell response to influenza virus hemagglutinin
    • Richards, K. A.; Chaves, F. A.; Krafcik, F. R.; Topham, D. J.; Lazarski, C. A.; Sant, A. J. Direct ex vivo analyses of HLA-DR1 transgenic mice reveal an exceptionally broad pattern of immunodominance in the primary HLA-DR1-restricted CD4 T-cell response to influenza virus hemagglutinin J. Virol. 2007, 81 (14) 7608-7619
    • (2007) J. Virol. , vol.81 , Issue.14 , pp. 7608-7619
    • Richards, K.A.1    Chaves, F.A.2    Krafcik, F.R.3    Topham, D.J.4    Lazarski, C.A.5    Sant, A.J.6
  • 58
    • 9744280420 scopus 로고    scopus 로고
    • Tracking global patterns of N-linked glycosylation site variation in highly variable viral glycoproteins: HIV, SIV, and HCV envelopes and influenza hemagglutinin
    • Zhang, M.; Gaschen, B.; Blay, W.; Foley, B.; Haigwood, N.; Kuiken, C.; Korber, B. Tracking global patterns of N-linked glycosylation site variation in highly variable viral glycoproteins: HIV, SIV, and HCV envelopes and influenza hemagglutinin Glycobiology 2004, 14 (12) 1229-1246
    • (2004) Glycobiology , vol.14 , Issue.12 , pp. 1229-1246
    • Zhang, M.1    Gaschen, B.2    Blay, W.3    Foley, B.4    Haigwood, N.5    Kuiken, C.6    Korber, B.7
  • 61
    • 80052284394 scopus 로고    scopus 로고
    • The ferret as a model organism to study influenza A virus infection
    • Belser, J. A.; Katz, J. M.; Tumpey, T. M. The ferret as a model organism to study influenza A virus infection Dis. Models Mech. 2011, 4 (5) 575-579
    • (2011) Dis. Models Mech. , vol.4 , Issue.5 , pp. 575-579
    • Belser, J.A.1    Katz, J.M.2    Tumpey, T.M.3
  • 62
    • 35648962553 scopus 로고    scopus 로고
    • The influenza viruses
    • Hampson, A. W.; Mackenzie, J. S. The influenza viruses Med. J. Aust. 2006, 185 (10 Suppl) S39-S43
    • (2006) Med. J. Aust. , vol.185 , Issue.10 SUPPL.
    • Hampson, A.W.1    Mackenzie, J.S.2
  • 64
    • 84862260858 scopus 로고    scopus 로고
    • Two Glycosylation Sites in H5N1 Influenza Virus Hemagglutinin That Affect Binding Preference by Computer-Based Analysis
    • Chen, W. T.; Sun, S. S.; Li, Z. Two Glycosylation Sites in H5N1 Influenza Virus Hemagglutinin That Affect Binding Preference by Computer-Based Analysis PLoS One 2012, 7 (6) e38794
    • (2012) PLoS One , vol.7 , Issue.6 , pp. 38794
    • Chen, W.T.1    Sun, S.S.2    Li, Z.3
  • 65
    • 77953290115 scopus 로고    scopus 로고
    • The influenza A virus hemagglutinin glycosylation state affects receptor-binding specificity
    • de Vries, R. P.; de Vries, E.; Bosch, B. J.; de Groot, R. J.; Rottier, P. J.; de Haan, C. A. The influenza A virus hemagglutinin glycosylation state affects receptor-binding specificity Virology 2010, 403 (1) 17-25
    • (2010) Virology , vol.403 , Issue.1 , pp. 17-25
    • De Vries, R.P.1    De Vries, E.2    Bosch, B.J.3    De Groot, R.J.4    Rottier, P.J.5    De Haan, C.A.6
  • 67
    • 79251480393 scopus 로고    scopus 로고
    • Glycosylation focuses sequence variation in the influenza A virus H1 hemagglutinin globular domain
    • Das, S. R.; Puigbo, P.; Hensley, S. E.; Hurt, D. E.; Bennink, J. R.; Yewdell, J. W. Glycosylation focuses sequence variation in the influenza A virus H1 hemagglutinin globular domain PLoS Pathog. 2010, 6 (11) e1001211
    • (2010) PLoS Pathog. , vol.6 , Issue.11 , pp. 1001211
    • Das, S.R.1    Puigbo, P.2    Hensley, S.E.3    Hurt, D.E.4    Bennink, J.R.5    Yewdell, J.W.6
  • 68
    • 84857072874 scopus 로고    scopus 로고
    • Prediction of biological functions on glycosylation site migrations in human influenza H1N1 viruses
    • Sun, S.; Wang, Q.; Zhao, F.; Chen, W.; Li, Z. Prediction of biological functions on glycosylation site migrations in human influenza H1N1 viruses PLoS One 2012, 7 (2) e32119
    • (2012) PLoS One , vol.7 , Issue.2 , pp. 32119
    • Sun, S.1    Wang, Q.2    Zhao, F.3    Chen, W.4    Li, Z.5
  • 69
    • 79952713119 scopus 로고    scopus 로고
    • Glycan shielding of the influenza virus hemagglutinin contributes to immunopathology in mice
    • Wanzeck, K.; Boyd, K. L.; McCullers, J. A. Glycan shielding of the influenza virus hemagglutinin contributes to immunopathology in mice Am. J. Respir. Crit. Care Med. 2011, 183 (6) 767-773
    • (2011) Am. J. Respir. Crit. Care Med. , vol.183 , Issue.6 , pp. 767-773
    • Wanzeck, K.1    Boyd, K.L.2    McCullers, J.A.3
  • 70
    • 0018177170 scopus 로고
    • Effects of sialylation of influenza virions on their interactions with host cells and erythrocytes
    • Lakshmi, M. V.; Schulze, I. T. Effects of sialylation of influenza virions on their interactions with host cells and erythrocytes Virology 1978, 88 (2) 314-324
    • (1978) Virology , vol.88 , Issue.2 , pp. 314-324
    • Lakshmi, M.V.1    Schulze, I.T.2
  • 71
    • 7644241814 scopus 로고    scopus 로고
    • Neuraminidase is important for the initiation of influenza virus infection in human airway epithelium
    • Matrosovich, M. N.; Matrosovich, T. Y.; Gray, T.; Roberts, N. A.; Klenk, H. D. Neuraminidase is important for the initiation of influenza virus infection in human airway epithelium J. Virol. 2004, 78 (22) 12665-12667
    • (2004) J. Virol. , vol.78 , Issue.22 , pp. 12665-12667
    • Matrosovich, M.N.1    Matrosovich, T.Y.2    Gray, T.3    Roberts, N.A.4    Klenk, H.D.5
  • 72
    • 0036224388 scopus 로고    scopus 로고
    • Influenza virus carrying neuraminidase with reduced sensitivity to oseltamivir carboxylate has altered properties in vitro and is compromised for infectivity and replicative ability in vivo
    • Carr, J.; Ives, J.; Kelly, L.; Lambkin, R.; Oxford, J.; Mendel, D.; Tai, L.; Roberts, N. Influenza virus carrying neuraminidase with reduced sensitivity to oseltamivir carboxylate has altered properties in vitro and is compromised for infectivity and replicative ability in vivo Antiviral Res. 2002, 54 (2) 79-88
    • (2002) Antiviral Res. , vol.54 , Issue.2 , pp. 79-88
    • Carr, J.1    Ives, J.2    Kelly, L.3    Lambkin, R.4    Oxford, J.5    Mendel, D.6    Tai, L.7    Roberts, N.8
  • 73
    • 0036842048 scopus 로고    scopus 로고
    • A release-competent influenza A virus mutant lacking the coding capacity for the neuraminidase active site
    • Gubareva, L. V.; Nedyalkova, M. S.; Novikov, D. V.; Murti, K. G.; Hoffmann, E.; Hayden, F. G. A release-competent influenza A virus mutant lacking the coding capacity for the neuraminidase active site J. Gen. Virol. 2002, 83 (Pt 11) 2683-2692
    • (2002) J. Gen. Virol. , vol.83 , Issue.PART 11 , pp. 2683-2692
    • Gubareva, L.V.1    Nedyalkova, M.S.2    Novikov, D.V.3    Murti, K.G.4    Hoffmann, E.5    Hayden, F.G.6
  • 74
    • 79551501860 scopus 로고    scopus 로고
    • Synthesis of cross-reactive carbohydrate determinants fragments as tools for in vitro allergy diagnosis
    • Collot, M.; Wilson, I. B.; Bublin, M.; Hoffmann-Sommergruber, K.; Mallet, J. M. Synthesis of cross-reactive carbohydrate determinants fragments as tools for in vitro allergy diagnosis Bioorg. Med. Chem. 2011, 19 (3) 1306-1320
    • (2011) Bioorg. Med. Chem. , vol.19 , Issue.3 , pp. 1306-1320
    • Collot, M.1    Wilson, I.B.2    Bublin, M.3    Hoffmann-Sommergruber, K.4    Mallet, J.M.5
  • 75
    • 68149091435 scopus 로고    scopus 로고
    • Immunoglobulin-E reactivity to a glycosylated food allergen (peanuts) due to interference with cross-reactive carbohydrate determinants in heavy drinkers
    • Vidal, C.; Vizcaino, L.; Diaz-Peromingo, J. A.; Garrido, M.; Gomez-Rial, J.; Linneberg, A.; Gonzalez-Quintela, A. Immunoglobulin-E reactivity to a glycosylated food allergen (peanuts) due to interference with cross-reactive carbohydrate determinants in heavy drinkers Alcohol.: Clin. Exp. Res. 2009, 33 (8) 1322-1328
    • (2009) Alcohol.: Clin. Exp. Res. , vol.33 , Issue.8 , pp. 1322-1328
    • Vidal, C.1    Vizcaino, L.2    Diaz-Peromingo, J.A.3    Garrido, M.4    Gomez-Rial, J.5    Linneberg, A.6    Gonzalez-Quintela, A.7
  • 76
    • 84855586936 scopus 로고    scopus 로고
    • Formation of the immunogenic alpha1,3-fucose epitope: Elucidation of substrate specificity and of enzyme mechanism of core fucosyltransferase A
    • Kotzler, M. P.; Blank, S.; Behnken, H. N.; Alpers, D.; Bantleon, F. I.; Spillner, E.; Meyer, B. Formation of the immunogenic alpha1,3-fucose epitope: elucidation of substrate specificity and of enzyme mechanism of core fucosyltransferase A Insect Biochem. Mol. Biol. 2012, 42 (2) 116-125
    • (2012) Insect Biochem. Mol. Biol. , vol.42 , Issue.2 , pp. 116-125
    • Kotzler, M.P.1    Blank, S.2    Behnken, H.N.3    Alpers, D.4    Bantleon, F.I.5    Spillner, E.6    Meyer, B.7
  • 77
    • 80054681971 scopus 로고    scopus 로고
    • Distantly related plant and nematode core alpha1,3-fucosyltransferases display similar trends in structure-function relationships
    • Both, P.; Sobczak, L.; Breton, C.; Hann, S.; Nobauer, K.; Paschinger, K.; Kozmon, S.; Mucha, J.; Wilson, I. B. Distantly related plant and nematode core alpha1,3-fucosyltransferases display similar trends in structure-function relationships Glycobiology 2011, 21 (11) 1401-1415
    • (2011) Glycobiology , vol.21 , Issue.11 , pp. 1401-1415
    • Both, P.1    Sobczak, L.2    Breton, C.3    Hann, S.4    Nobauer, K.5    Paschinger, K.6    Kozmon, S.7    Mucha, J.8    Wilson, I.B.9
  • 80
    • 33750934617 scopus 로고    scopus 로고
    • Dendritic cells: Translating innate to adaptive immunity
    • Steinman, R. M.; Hemmi, H. Dendritic cells: translating innate to adaptive immunity Curr. Top. Microbiol. Immunol. 2006, 311, 17-58
    • (2006) Curr. Top. Microbiol. Immunol. , vol.311 , pp. 17-58
    • Steinman, R.M.1    Hemmi, H.2
  • 81
    • 77149123171 scopus 로고    scopus 로고
    • Does Glycosylation as a modifier of Original Antigenic Sin explain the case age distribution and unusual toxicity in pandemic novel H1N1 influenza?
    • Reichert, T.; Chowell, G.; Nishiura, H.; Christensen, R. A.; McCullers, J. A. Does Glycosylation as a modifier of Original Antigenic Sin explain the case age distribution and unusual toxicity in pandemic novel H1N1 influenza? BMC Infect. Dis. 2010, 10, 5
    • (2010) BMC Infect. Dis. , vol.10 , pp. 5
    • Reichert, T.1    Chowell, G.2    Nishiura, H.3    Christensen, R.A.4    McCullers, J.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.