메뉴 건너뛰기




Volumn 411, Issue 1, 2011, Pages 22-31

In vivo biotinylated recombinant influenza A virus hemagglutinin for use in subtype-specific serodiagnostic assays

Author keywords

Hemagglutinin; In vivo biotinylation; Influenza A virus; Recombinant expression; Serodiagnosis

Indexed keywords

ACYLATION; ANTIGEN-ANTIBODY REACTIONS; COENZYMES; EPITOPES; MAMMALS; MONOCLONAL ANTIBODIES; VIRUSES;

EID: 79951576389     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2010.12.022     Document Type: Article
Times cited : (12)

References (29)
  • 2
    • 0020416123 scopus 로고
    • The antigenic structure of the influenza virus A/PR/8/34 hemagglutinin (H1 subtype)
    • A.J. Caton, G.G. Brownlee, J.W. Yewdell, and W. Gerhard The antigenic structure of the influenza virus A/PR/8/34 hemagglutinin (H1 subtype) Cell 31 1982 417 427 (Pubitemid 13178866)
    • (1982) Cell , vol.31 , Issue.2 , pp. 417-427
    • Caton, A.J.1    Brownlee, G.G.2    Yewdell, J.W.3    Gerhard, W.4
  • 4
    • 0025011303 scopus 로고
    • An ELISA for detection of antibodies against influenza A nucleoprotein in humans and various animal species
    • G.F. de Boer, W. Back, and A.D. Osterhaus An ELISA for detection of antibodies against influenza A nucleoprotein in humans and various animal species Arch. Virol. 115 1990 47 61 (Pubitemid 20381033)
    • (1990) Archives of Virology , vol.115 , Issue.1-2 , pp. 47-61
    • De Boer, G.F.1    Back, W.2    Osterhaus, A.D.M.E.3
  • 5
    • 57349110705 scopus 로고    scopus 로고
    • A multiplexed immunoassay for detection of antibodies against avian influenza virus
    • D.S. Watson, S.M. Reddy, V. Brahmakshatriya, and B. Lupiani A multiplexed immunoassay for detection of antibodies against avian influenza virus J. Immunol. Methods 340 2009 123 131
    • (2009) J. Immunol. Methods , vol.340 , pp. 123-131
    • Watson, D.S.1    Reddy, S.M.2    Brahmakshatriya, V.3    Lupiani, B.4
  • 7
  • 8
    • 0036178009 scopus 로고    scopus 로고
    • Domain organization, folding and stability of bacteriophage T4 fibritin, a segmented coiled-coil protein
    • DOI 10.1046/j.1432-1033.2002.02734.x
    • S.P. Boudko, Y.Y. Londer, A.V. Letarov, N.V. Sernova, J. Engel, and V.V. Mesyanzhinov Domain organization, folding, and stability of bacteriophage T4 fibritin, a segmented coiled-coil protein Eur. J. Biochem. 269 2002 833 841 (Pubitemid 34175403)
    • (2002) European Journal of Biochemistry , vol.269 , Issue.3 , pp. 833-841
    • Boudko, S.P.1    Londer, Y.Y.2    Letarov, A.V.3    Sernova, N.V.4    Engel, J.5    Mesyanzhinov, V.V.6
  • 9
    • 45749084541 scopus 로고    scopus 로고
    • Comparative efficacy of neutralizing antibodies elicited by recombinant hemagglutinin proteins from avian H5N1 influenza virus
    • DOI 10.1128/JVI.00187-08
    • C.J. Wei, L. Xu, W.P. Kong, W. Shi, K. Canis, J. Stevens, Z.Y. Yang, A. Dell, S.M. Haslam, I.A. Wilson, and G.J. Nabel Comparative efficacy of neutralizing antibodies elicited by recombinant hemagglutinin proteins from avian H5N1 influenza virus J. Virol. 82 2008 6200 6208 (Pubitemid 351875101)
    • (2008) Journal of Virology , vol.82 , Issue.13 , pp. 6200-6208
    • Wei, C.-J.1    Xu, L.2    Kong, W.-P.3    Shi, W.4    Canis, K.5    Stevens, J.6    Yang, Z.-Y.7    Dell, A.8    Haslam, S.M.9    Wilson, I.A.10    Nabel, G.J.11
  • 11
    • 0014944179 scopus 로고
    • A factor preventing the major head protein of bacteriophage T4 from random aggregation
    • U.K. Laemmli, F. Beguin, and G. Gujer-Kellenberger A factor preventing the major head protein of bacteriophage T4 from random aggregation J. Mol. Biol. 47 1970 69 85
    • (1970) J. Mol. Biol. , vol.47 , pp. 69-85
    • Laemmli, U.K.1    Beguin, F.2    Gujer-Kellenberger, G.3
  • 14
    • 0034810850 scopus 로고    scopus 로고
    • Metabolic biotinylation of secreted and cell surface proteins from mammalian cells
    • DOI 10.1006/bbrc.2001.4437
    • M.B. Parrott, and M.A. Barry Metabolic biotinylation of secreted and cell surface proteins from mammalian cells Biochem. Biophys. Res. Commun. 281 2001 993 1000 (Pubitemid 32917830)
    • (2001) Biochemical and Biophysical Research Communications , vol.281 , Issue.4 , pp. 993-1000
    • Parrott M.Brandon1    Barry, M.A.2
  • 15
    • 4043084175 scopus 로고    scopus 로고
    • In vivo biotinylation of the major histocompatibility complex (MHC) class II/peptide complex by coexpression of BirA enzyme for the generation of MHC class II/tetramers
    • DOI 10.1016/j.humimm.2004.04.001, PII S0198885904000837
    • J. Yang, A. Jaramillo, R. Shi, W.W. Kwok, and T. Mohanakumar In vivo biotinylation of the major histocompatibility complex (MHC) class II/peptide complex by coexpression of BirA enzyme for the generation of MHC class II/tetramers Hum. Immunol. 65 2004 692 699 (Pubitemid 39061165)
    • (2004) Human Immunology , vol.65 , Issue.7 , pp. 692-699
    • Yang, J.1    Jaramillo, A.2    Shi, R.3    Kwok, W.W.4    Mohanakumar, T.5
  • 16
    • 0032505105 scopus 로고    scopus 로고
    • Site-specific, enzymatic biotinylation of recombinant proteins in Spodoptera frugiperda cells using biotin acceptor peptides
    • DOI 10.1006/abio.1998.2770
    • S. Duffy, K.L. Tsao, and D.S. Waugh Site-specific, enzymatic biotinylation of recombinant proteins in Spodoptera frugiperda cells using biotin acceptor peptides Anal. Biochem. 262 1998 122 128 (Pubitemid 28452772)
    • (1998) Analytical Biochemistry , vol.262 , Issue.2 , pp. 122-128
    • Duffy, S.1    Tsao, K.-L.2    Waugh, D.S.3
  • 17
    • 0026527936 scopus 로고
    • Secretion of fowl plague virus haemagglutinin from insect cells requires elimination of both hydrophobic domains
    • E. Kretzschmar, M. Veit, S. Brunschon, K. Kuroda, and H.D. Klenk Secretion of fowl plague virus haemagglutinin from insect cells requires elimination of both hydrophobic domains J. Gen. Virol. 73 1992 839 848
    • (1992) J. Gen. Virol. , vol.73 , pp. 839-848
    • Kretzschmar, E.1    Veit, M.2    Brunschon, S.3    Kuroda, K.4    Klenk, H.D.5
  • 18
    • 0025815364 scopus 로고
    • Site-specific mutagenesis identifies three cysteine residues in the cytoplasmic tail as acylation sites of influenza virus hemagglutinin
    • M. Veit, E. Kretzschmar, K. Kuroda, W. Garten, M.F. Schmidt, H.D. Klenk, and R. Rott Site-specific mutagenesis identifies three cysteine residues in the cytoplasmic tail as acylation sites of influenza virus hemagglutinin J. Virol. 65 1991 2491 2500
    • (1991) J. Virol. , vol.65 , pp. 2491-2500
    • Veit, M.1    Kretzschmar, E.2    Kuroda, K.3    Garten, W.4    Schmidt, M.F.5    Klenk, H.D.6    Rott, R.7
  • 19
    • 18144395402 scopus 로고    scopus 로고
    • Acylation-mediated membrane anchoring of avian influenza virus hemagglutinin is essential for fusion pore formation and virus infectivity
    • DOI 10.1128/JVI.79.10.6449-6458.2005
    • R. Wagner, A. Herwig, N. Azzouz, and H.D. Klenk Acylation-mediated membrane anchoring of avian influenza virus hemagglutinin is essential for fusion pore formation and virus infectivity J. Virol. 79 2005 6449 6458 (Pubitemid 40617248)
    • (2005) Journal of Virology , vol.79 , Issue.10 , pp. 6449-6458
    • Wagner, R.1    Herwig, A.2    Azzouz, N.3    Klenk, H.D.4
  • 21
    • 0025291360 scopus 로고
    • Protein biotinylation
    • DOI 10.1016/0076-6879(90)84268-L
    • E.A. Bayer, and M. Wilchek Protein biotinylation Methods Enzymol. 184 1990 138 160 (Pubitemid 20219739)
    • (1990) Methods in Enzymology , vol.184 , pp. 138-160
    • Bayer, E.A.1    Wilchek, M.2
  • 22
    • 0025856887 scopus 로고
    • The biotin-(strept)avidin system: Principles and applications in biotechnology
    • E.P. Diamandis, and T.K. Christopoulos The biotin-(strept)avidin system: principles and applications in biotechnology Clin. Chem. 37 1991 625 636 (Pubitemid 21892699)
    • (1991) Clinical Chemistry , vol.37 , Issue.5 , pp. 625-636
    • Diamandis, E.P.1    Christopoulos, T.K.2
  • 23
    • 34548834691 scopus 로고    scopus 로고
    • Strategies for site-specific protein biotinylation using in vitro, in vivo, and cell-free systems: Toward functional protein arrays
    • S. Chattopadhaya, L.P. Tan, and S.Q. Yao Strategies for site-specific protein biotinylation using in vitro, in vivo, and cell-free systems: toward functional protein arrays Nat. Protoc. 1 2006 2386 2398
    • (2006) Nat. Protoc. , vol.1 , pp. 2386-2398
    • Chattopadhaya, S.1    Tan, L.P.2    Yao, S.Q.3
  • 24
    • 0033819031 scopus 로고    scopus 로고
    • Biotinylation of proteins in vivo and in vitro using small peptide tags
    • M.G. Cull, and P.J. Schatz Biotinylation of proteins in vivo and in vitro using small peptide tags Methods Enzymol. 326 2000 430 440
    • (2000) Methods Enzymol. , vol.326 , pp. 430-440
    • Cull, M.G.1    Schatz, P.J.2
  • 25
    • 0032924825 scopus 로고    scopus 로고
    • BirA enzyme: Production and application in the study of membrane receptor-ligand interactions by site-specific biotinylation
    • DOI 10.1006/abio.1998.2930
    • C.A. O'Callaghan, M.F. Byford, J.R. Wyer, B.E. Willcox, B.K. Jakobsen, A.J. McMichael, and J.I. Bell BirA enzyme: production and application in the study of membrane receptor-ligand interactions by site-specific biotinylation Anal. Biochem. 266 1999 9 15 (Pubitemid 29024603)
    • (1999) Analytical Biochemistry , vol.266 , Issue.1 , pp. 9-15
    • O'Callaghan, C.A.1    Byford, M.F.2    Wyer, J.R.3    Willcox, B.E.4    Jakobsen, B.K.5    McMichael, A.J.6    Bell, J.I.7
  • 26
    • 0033621510 scopus 로고    scopus 로고
    • In vivo enzymatic protein biotinylation
    • DOI 10.1016/S1050-3862(99)00046-7, PII S1050386299000467
    • A. Chapman-Smith, and J.E. Cronan Jr In vivo enzymatic protein biotinylation Biomol. Eng. 16 1999 119 125 (Pubitemid 30184848)
    • (1999) Biomolecular Engineering , vol.16 , Issue.1-4 , pp. 119-125
    • Chapman-Smith, A.1    Cronan Jr., J.E.2
  • 27
    • 33751420234 scopus 로고    scopus 로고
    • Method for generation of in vivo biotinylated recombinant antibodies by yeast mating
    • DOI 10.1016/j.jim.2006.10.003, PII S0022175906002894
    • N. Scholler, B. Garvik, T. Quarles, S. Jiang, and N. Urban Method for generation of in vivo biotinylated recombinant antibodies by yeast mating J. Immunol. Methods 317 2006 132 143 (Pubitemid 44816326)
    • (2006) Journal of Immunological Methods , vol.317 , Issue.1-2 , pp. 132-143
    • Scholler, N.1    Garvik, B.2    Quarles, T.3    Jiang, S.4    Urban, N.5
  • 28
    • 34548485309 scopus 로고    scopus 로고
    • Metabolic biotinylation of recombinant antibody by biotin ligase retained in the endoplasmic reticulum
    • DOI 10.1016/j.bioeng.2007.02.003, PII S1389034407000202, 6th Atlantic Symposium on Computational Biology
    • B. Barat, and A.M. Wu Metabolic biotinylation of recombinant antibody by biotin ligase retained in the endoplasmic reticulum Biomol. Eng. 24 2007 283 291 (Pubitemid 47380450)
    • (2007) Biomolecular Engineering , vol.24 , Issue.3 , pp. 283-291
    • Barat, B.1    Wu, A.M.2
  • 29
    • 43049102042 scopus 로고    scopus 로고
    • In vivo site-specific biotinylation of proteins within the secretory pathway using a single vector system
    • A. Predonzani, F. Arnoldi, A. Lopez-Requena, and O.R. Burrone In vivo site-specific biotinylation of proteins within the secretory pathway using a single vector system BMC Biotechnol. 8 2008 41
    • (2008) BMC Biotechnol. , vol.8 , pp. 41
    • Predonzani, A.1    Arnoldi, F.2    Lopez-Requena, A.3    Burrone, O.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.