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Volumn 14, Issue 9, 2015, Pages 3957-3969

Glycosylation analysis of engineered H3N2 influenza A virus hemagglutinins with sequentially added historically relevant glycosylation sites

Author keywords

antigenic site; glycan; glycopeptide; glycoprotein; H3N2; hemagglutinin; influenza; LC MS; mass spectrometry; SP D

Indexed keywords

INFLUENZA VIRUS HEMAGGLUTININ;

EID: 84941137376     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/acs.jproteome.5b00416     Document Type: Article
Times cited : (59)

References (42)
  • 1
    • 84941092692 scopus 로고    scopus 로고
    • WHO Influenza (Seasonal).
    • WHO Influenza (Seasonal). http://www.who.int/mediacentre/factsheets/fs211/en/.
  • 2
    • 0032712272 scopus 로고    scopus 로고
    • Epidemiology and pathogenesis of influenza
    • Zambon, M. C. Epidemiology and pathogenesis of influenza J. Antimicrob. Chemother. 1999, 44 (Suppl B) 3-9 10.1093/jac/44.suppl-2.3
    • (1999) J. Antimicrob. Chemother. , vol.44 , pp. 3-9
    • Zambon, M.C.1
  • 4
    • 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 10.1016/j.virol.2010.03.047
    • (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
  • 6
    • 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 10.1371/journal.pone.0038794
    • (2012) PLoS One , vol.7 , Issue.6 , pp. 38794
    • Chen, W.T.1    Sun, S.S.2    Li, Z.3
  • 7
    • 0036255966 scopus 로고    scopus 로고
    • Effect of addition of new oligosaccharide chains to the globular head of influenza A/H2N2 virus haemagglutinin on the intracellular transport and biological activities of the molecule
    • Tsuchiya, E.; Sugawara, K.; Hongo, S.; Matsuzaki, Y.; Muraki, Y.; Li, Z. N.; Nakamura, K. Effect of addition of new oligosaccharide chains to the globular head of influenza A/H2N2 virus haemagglutinin on the intracellular transport and biological activities of the molecule J. Gen. Virol. 2002, 83 (Pt 5) 1137-1146
    • (2002) J. Gen. Virol. , vol.83 , pp. 1137-1146
    • Tsuchiya, E.1    Sugawara, K.2    Hongo, S.3    Matsuzaki, Y.4    Muraki, Y.5    Li, Z.N.6    Nakamura, K.7
  • 8
    • 0003746861 scopus 로고
    • A carbohydrate side chain on hemagglutinins of Hong Kong influenza viruses inhibits recognition by a monoclonal antibody
    • Skehel, J. J.; Stevens, D. J.; Daniels, R. S.; Douglas, A. R.; Knossow, M.; Wilson, I. A.; Wiley, D. C. A carbohydrate side chain on hemagglutinins of Hong Kong influenza viruses inhibits recognition by a monoclonal antibody Proc. Natl. Acad. Sci. U. S. A. 1984, 81 (6) 1779-83 10.1073/pnas.81.6.1779
    • (1984) Proc. Natl. Acad. Sci. U. S. A. , vol.81 , Issue.6 , pp. 1779-1783
    • Skehel, J.J.1    Stevens, D.J.2    Daniels, R.S.3    Douglas, A.R.4    Knossow, M.5    Wilson, I.A.6    Wiley, D.C.7
  • 9
    • 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 10.1371/journal.ppat.1001211
    • (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
  • 10
    • 77952969448 scopus 로고    scopus 로고
    • Cross-neutralization of 1918 and 2009 influenza viruses: Role of glycans in viral evolution and vaccine design
    • Wei, C. J.; Boyington, J. C.; Dai, K.; Houser, K. V.; Pearce, M. B.; Kong, W. P.; Yang, Z. Y.; Tumpey, T. M.; Nabel, G. J. Cross-neutralization of 1918 and 2009 influenza viruses: role of glycans in viral evolution and vaccine design Sci. Transl. Med. 2010, 2 (24) 24ra21 10.1126/scitranslmed.3000799
    • (2010) Sci. Transl. Med. , vol.2 , Issue.24 , pp. 24ra21
    • Wei, C.J.1    Boyington, J.C.2    Dai, K.3    Houser, K.V.4    Pearce, M.B.5    Kong, W.P.6    Yang, Z.Y.7    Tumpey, T.M.8    Nabel, G.J.9
  • 11
    • 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) 767-73 10.1164/rccm.201007-1184OC
    • (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
  • 12
    • 0037245727 scopus 로고    scopus 로고
    • N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin
    • Daniels, R.; Kurowski, B.; Johnson, A. E.; Hebert, D. N. N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin Mol. Cell 2003, 11 (1) 79-90 10.1016/S1097-2765(02)00821-3
    • (2003) Mol. Cell , vol.11 , Issue.1 , pp. 79-90
    • Daniels, R.1    Kurowski, B.2    Johnson, A.E.3    Hebert, D.N.4
  • 13
    • 79251508720 scopus 로고    scopus 로고
    • Evolutionary dynamics of N-glycosylation sites of influenza virus hemagglutinin
    • Cherry, J. L.; Lipman, D. J.; Nikolskaya, A.; Wolf, Y. I. Evolutionary dynamics of N-glycosylation sites of influenza virus hemagglutinin PLoS Curr. 2009, 1, RRN1001 10.1371/currents.RRN1001
    • (2009) PLoS Curr. , vol.1 , pp. 1001
    • Cherry, J.L.1    Lipman, D.J.2    Nikolskaya, A.3    Wolf, Y.I.4
  • 14
    • 79960872741 scopus 로고    scopus 로고
    • Glycosylation site alteration in the evolution of influenza A (H1N1) viruses
    • Sun, S.; Wang, Q.; Zhao, F.; Chen, W.; Li, Z. Glycosylation site alteration in the evolution of influenza A (H1N1) viruses PLoS One 2011, 6 (7) e22844 10.1371/journal.pone.0022844
    • (2011) PLoS One , vol.6 , Issue.7 , pp. 22844
    • Sun, S.1    Wang, Q.2    Zhao, F.3    Chen, W.4    Li, Z.5
  • 15
    • 84861302846 scopus 로고    scopus 로고
    • Evidence for N-glycan shielding of antigenic sites during evolution of human influenza A virus hemagglutinin
    • Kobayashi, Y.; Suzuki, Y. Evidence for N-glycan shielding of antigenic sites during evolution of human influenza A virus hemagglutinin J. Virol 2012, 86 (7) 3446-51 10.1128/JVI.06147-11
    • (2012) J. Virol , vol.86 , Issue.7 , pp. 3446-3451
    • Kobayashi, Y.1    Suzuki, Y.2
  • 16
    • 0004257938 scopus 로고    scopus 로고
    • 6 th ed. Lippincott Williams and Wilkins.
    • Paul, W. E. Fundamental Immunology, 6 th ed.; Lippincott Williams and Wilkins, 2008.
    • (2008) Fundamental Immunology
    • Paul, W.E.1
  • 17
    • 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) 9605-11 10.1128/JVI.78.18.9605-9611.2004
    • (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
  • 18
    • 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 10.1186/1471-2334-10-5
    • (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
  • 19
    • 0030879806 scopus 로고    scopus 로고
    • Collectin-mediated antiviral host defense of the lung: Evidence from influenza virus infection of mice
    • Reading, P. C.; Morey, L. S.; Crouch, E. C.; Anders, E. M. Collectin-mediated antiviral host defense of the lung: evidence from influenza virus infection of mice J. Virol. 1997, 71 (11) 8204-8212
    • (1997) J. Virol. , vol.71 , Issue.11 , pp. 8204-8212
    • Reading, P.C.1    Morey, L.S.2    Crouch, E.C.3    Anders, E.M.4
  • 20
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution
    • Wilson, I. A.; Skehel, J. J.; Wiley, D. C. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution Nature 1981, 289 (5796) 366-73 10.1038/289366a0
    • (1981) Nature , vol.289 , Issue.5796 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 21
    • 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 10.1016/j.ab.2011.04.018
    • (2011) Anal. Biochem. , vol.415 , Issue.1 , pp. 67-80
    • An, Y.1    Cipollo, J.F.2
  • 22
    • 66149089569 scopus 로고    scopus 로고
    • Solid-phase permethylation for glycomic analysis
    • Mechref, Y.; Kang, P.; Novotny, M. V. Solid-phase permethylation for glycomic analysis Methods Mol. Biol. 2009, 534, 53-64 10.1007/978-1-59745-022-5-4
    • (2009) Methods Mol. Biol. , vol.534 , pp. 53-64
    • Mechref, Y.1    Kang, P.2    Novotny, M.V.3
  • 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 10.2174/138920111798357447
    • (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
    • 84881141968 scopus 로고    scopus 로고
    • Comparative glycomics analysis of influenza Hemagglutinin (H5N1) produced in vaccine relevant cell platforms
    • An, Y.; Rininger, J. A.; Jarvis, D. L.; Jing, X.; Ye, Z.; Aumiller, J. J.; Eichelberger, M.; Cipollo, J. F. Comparative glycomics analysis of influenza Hemagglutinin (H5N1) produced in vaccine relevant cell platforms J. Proteome Res. 2013, 12 (8) 3707-20 10.1021/pr400329k
    • (2013) J. Proteome Res. , vol.12 , Issue.8 , pp. 3707-3720
    • An, Y.1    Rininger, J.A.2    Jarvis, D.L.3    Jing, X.4    Ye, Z.5    Aumiller, J.J.6    Eichelberger, M.7    Cipollo, J.F.8
  • 26
    • 39449115394 scopus 로고    scopus 로고
    • I-TASSER server for protein 3D structure prediction
    • Zhang, Y. I-TASSER server for protein 3D structure prediction BMC Bioinf. 2008, 9, 40 10.1186/1471-2105-9-40
    • (2008) BMC Bioinf. , vol.9 , pp. 40
    • Zhang, Y.1
  • 27
    • 84925156346 scopus 로고    scopus 로고
    • The I-TASSER Suite: Protein structure and function prediction
    • Yang, J.; Yan, R.; Roy, A.; Xu, D.; Poisson, J.; Zhang, Y. The I-TASSER Suite: protein structure and function prediction Nat. Methods 2014, 12 (1) 7-8 10.1038/nmeth.3213
    • (2014) Nat. Methods , vol.12 , Issue.1 , pp. 7-8
    • Yang, J.1    Yan, R.2    Roy, A.3    Xu, D.4    Poisson, J.5    Zhang, Y.6
  • 28
  • 30
    • 0019065845 scopus 로고
    • Carbohydrate composition of the oligosaccharide units of the haemagglutinin from the Hong Kong influenza virus A/Memphis/102/72
    • Ward, C. W.; Gleeson, P. A.; Dopheide, T. A. Carbohydrate composition of the oligosaccharide units of the haemagglutinin from the Hong Kong influenza virus A/Memphis/102/72 Biochem. J. 1980, 189 (3) 649-652
    • (1980) Biochem. J. , vol.189 , Issue.3 , pp. 649-652
    • Ward, C.W.1    Gleeson, P.A.2    Dopheide, T.A.3
  • 31
    • 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 10.1016/j.jasms.2007.07.016
    • (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
  • 32
    • 11144231261 scopus 로고    scopus 로고
    • Srf-3, a mutant of Caenorhabditis elegans, resistant to bacterial infection and to biofilm binding, is deficient in glycoconjugates
    • Cipollo, J. F.; Awad, A. M.; Costello, C. E.; Hirschberg, C. B. srf-3, a mutant of Caenorhabditis elegans, resistant to bacterial infection and to biofilm binding, is deficient in glycoconjugates J. Biol. Chem. 2004, 279 (51) 52893-903 10.1074/jbc.M409557200
    • (2004) J. Biol. Chem. , vol.279 , Issue.51 , pp. 52893-52903
    • Cipollo, J.F.1    Awad, A.M.2    Costello, C.E.3    Hirschberg, C.B.4
  • 33
    • 8444220853 scopus 로고    scopus 로고
    • Three-dimensional window analysis for detecting positive selection at structural regions of proteins
    • Suzuki, Y. Three-dimensional window analysis for detecting positive selection at structural regions of proteins Mol. Biol. Evol. 2004, 21 (12) 2352-9 10.1093/molbev/msh249
    • (2004) Mol. Biol. Evol. , vol.21 , Issue.12 , pp. 2352-2359
    • Suzuki, Y.1
  • 34
    • 0020371209 scopus 로고
    • Mapping of antigenic changes in the haemagglutinin of Hong Kong influenza (H3N2) strains using a large panel of monoclonal antibodies
    • Underwood, P. A. Mapping of antigenic changes in the haemagglutinin of Hong Kong influenza (H3N2) strains using a large panel of monoclonal antibodies J. Gen. Virol. 1982, 62 (1) 153-169 10.1099/0022-1317-62-1-153
    • (1982) J. Gen. Virol. , vol.62 , Issue.1 , pp. 153-169
    • Underwood, P.A.1
  • 35
    • 0019432165 scopus 로고
    • Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation
    • Wiley, D. C.; Wilson, I. A.; Skehel, J. J. Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation Nature 1981, 289 (5796) 373-8 10.1038/289373a0
    • (1981) Nature , vol.289 , Issue.5796 , pp. 373-378
    • Wiley, D.C.1    Wilson, I.A.2    Skehel, J.J.3
  • 36
    • 0025298243 scopus 로고
    • Bovine and mouse serum beta inhibitors of influenza A viruses are mannose-binding lectins
    • Anders, E. M.; Hartley, C. A.; Jackson, D. C. Bovine and mouse serum beta inhibitors of influenza A viruses are mannose-binding lectins Proc. Natl. Acad. Sci. U. S. A. 1990, 87 (12) 4485-9 10.1073/pnas.87.12.4485
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , Issue.12 , pp. 4485-4489
    • Anders, E.M.1    Hartley, C.A.2    Jackson, D.C.3
  • 37
    • 79953117247 scopus 로고    scopus 로고
    • Glycosylation of the hemagglutinin modulates the sensitivity of H3N2 influenza viruses to innate proteins in airway secretions and virulence in mice
    • Tate, M. D.; Job, E. R.; Brooks, A. G.; Reading, P. C. Glycosylation of the hemagglutinin modulates the sensitivity of H3N2 influenza viruses to innate proteins in airway secretions and virulence in mice Virology 2011, 413 (1) 84-92 10.1016/j.virol.2011.01.036
    • (2011) Virology , vol.413 , Issue.1 , pp. 84-92
    • Tate, M.D.1    Job, E.R.2    Brooks, A.G.3    Reading, P.C.4
  • 39
    • 0020416123 scopus 로고
    • The antigenic structure of the influenza virus A/PR/8/34 hemagglutinin (H1 subtype)
    • Caton, A. J.; Brownlee, G. G.; Yewdell, J. W.; Gerhard, W. The antigenic structure of the influenza virus A/PR/8/34 hemagglutinin (H1 subtype) Cell 1982, 31 (2) 417-427 10.1016/0092-8674(82)90135-0
    • (1982) Cell , vol.31 , Issue.2 , pp. 417-427
    • Caton, A.J.1    Brownlee, G.G.2    Yewdell, J.W.3    Gerhard, W.4
  • 41
    • 84934437867 scopus 로고    scopus 로고
    • Glycosylation as a target for recognition of influenza viruses by the innate immune system
    • Reading, P. C.; Tate, M. D.; Pickett, D. L.; Brooks, A. G. Glycosylation as a target for recognition of influenza viruses by the innate immune system Adv. Exp. Med. Biol. 2007, 598, 279-292 10.1007/978-0-387-71767-8-20
    • (2007) Adv. Exp. Med. Biol. , vol.598 , pp. 279-292
    • Reading, P.C.1    Tate, M.D.2    Pickett, D.L.3    Brooks, A.G.4


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