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Volumn 178, Issue 1-2, 2011, Pages 44-51

Enhanced expression of secretable influenza virus neuraminidase in suspension mammalian cells by influenza virus nonstructural protein 1

Author keywords

Influenza virus; Mammalian cell culture; Neuraminidase; Nonstructural protein 1; Transient gene expression

Indexed keywords

MYC PROTEIN; NONSTRUCTURAL PROTEIN 1; VIRUS SIALIDASE;

EID: 80955144158     PISSN: 01660934     EISSN: 18790984     Source Type: Journal    
DOI: 10.1016/j.jviromet.2011.08.010     Document Type: Article
Times cited : (11)

References (41)
  • 1
    • 56649099058 scopus 로고    scopus 로고
    • Coexpression of acidic fibroblast growth factor enhances specific productivity and antibody titers in transiently transfected HEK293 cells
    • Backliwal G., Hildinger M., Chenuet S., Dejesus M., Wurm F.M. Coexpression of acidic fibroblast growth factor enhances specific productivity and antibody titers in transiently transfected HEK293 cells. N. Biotechnol. 2008, 25:162-166.
    • (2008) N. Biotechnol. , vol.25 , pp. 162-166
    • Backliwal, G.1    Hildinger, M.2    Chenuet, S.3    Dejesus, M.4    Wurm, F.M.5
  • 2
    • 80955144512 scopus 로고    scopus 로고
    • Validation of different systems for tumstatin expression and its in-vitro and in-vivo activities
    • Boosani C.S., Varma A.K., Sudhakar A. Validation of different systems for tumstatin expression and its in-vitro and in-vivo activities. J. Cancer Sci. Ther. 2009, 8-18.
    • (2009) J. Cancer Sci. Ther. , pp. 8-18
    • Boosani, C.S.1    Varma, A.K.2    Sudhakar, A.3
  • 4
    • 0346121589 scopus 로고    scopus 로고
    • PABP1 and eIF4GI associate with influenza virus NS1 protein in viral mRNA translation initiation complexes
    • Burgui I., Aragon T., Ortin J., Nieto A. PABP1 and eIF4GI associate with influenza virus NS1 protein in viral mRNA translation initiation complexes. J. Gen. Virol. 2003, 84:3263-3274.
    • (2003) J. Gen. Virol. , vol.84 , pp. 3263-3274
    • Burgui, I.1    Aragon, T.2    Ortin, J.3    Nieto, A.4
  • 6
    • 0014594355 scopus 로고
    • Effect of antibody to neuraminidase on the maturation and hemagglutinating activity of an influenza A2 virus
    • Compans R.W., Dimmock N.J., Meier-Ewert H. Effect of antibody to neuraminidase on the maturation and hemagglutinating activity of an influenza A2 virus. J. Virol. 1969, 4(4):528-534.
    • (1969) J. Virol. , vol.4 , Issue.4 , pp. 528-534
    • Compans, R.W.1    Dimmock, N.J.2    Meier-Ewert, H.3
  • 7
    • 33751009658 scopus 로고    scopus 로고
    • Development of recombinant protein-based influenza vaccine. Expression and affinity purification of H1N1 influenza virus neuraminidase
    • Dalakouras T., Smith B.J., Platis D., Cox M.M., Labrou N.E. Development of recombinant protein-based influenza vaccine. Expression and affinity purification of H1N1 influenza virus neuraminidase. J. Chromatogr. A 2006, 1136:48-56.
    • (2006) J. Chromatogr. A , vol.1136 , pp. 48-56
    • Dalakouras, T.1    Smith, B.J.2    Platis, D.3    Cox, M.M.4    Labrou, N.E.5
  • 8
    • 0015977897 scopus 로고
    • Inhibition of virus release by antibodies to surface antigens of influenza viruses
    • Dowdle W.R., Downie J.C., Laver W.G. Inhibition of virus release by antibodies to surface antigens of influenza viruses. J. Virol. 1974, 13(2):269-275.
    • (1974) J. Virol. , vol.13 , Issue.2 , pp. 269-275
    • Dowdle, W.R.1    Downie, J.C.2    Laver, W.G.3
  • 10
    • 0028923921 scopus 로고
    • Influenza virus NS1 protein enhances the rate of translation initiation of viral mRNAs
    • de la Luna S., Fortes P., Beloso A., Ortin J. Influenza virus NS1 protein enhances the rate of translation initiation of viral mRNAs. J. Virol. 1995, 69:2427-2433.
    • (1995) J. Virol. , vol.69 , pp. 2427-2433
    • de la Luna, S.1    Fortes, P.2    Beloso, A.3    Ortin, J.4
  • 11
    • 0037082158 scopus 로고    scopus 로고
    • High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cells
    • Durocher Y., Perret S., Kamen A. High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cells. Nucleic Acids Res. 2002, 30:E9.
    • (2002) Nucleic Acids Res. , vol.30
    • Durocher, Y.1    Perret, S.2    Kamen, A.3
  • 12
    • 58749101153 scopus 로고    scopus 로고
    • Reflections on more than 10 years of TGE approaches
    • Geisse S. Reflections on more than 10 years of TGE approaches. Protein Expr. Purif. 2009, 64:99-107.
    • (2009) Protein Expr. Purif. , vol.64 , pp. 99-107
    • Geisse, S.1
  • 15
    • 0037135677 scopus 로고    scopus 로고
    • Eight-plasmid system for rapid generation of influenza virus vaccines
    • Hoffmann E., Krauss S., Perez D., Webby R., Webster R.G. Eight-plasmid system for rapid generation of influenza virus vaccines. Vaccine 2002, 20:3165-3170.
    • (2002) Vaccine , vol.20 , pp. 3165-3170
    • Hoffmann, E.1    Krauss, S.2    Perez, D.3    Webby, R.4    Webster, R.G.5
  • 17
    • 0028218512 scopus 로고
    • Deletion mutation in the signal anchor domain activates cleavage of the influenza virus neuraminidase, a type II transmembrane protein
    • Hogue B.G., Nayak D.P. Deletion mutation in the signal anchor domain activates cleavage of the influenza virus neuraminidase, a type II transmembrane protein. J. Gen. Virol. 1994, 75:1015-1022.
    • (1994) J. Gen. Virol. , vol.75 , pp. 1015-1022
    • Hogue, B.G.1    Nayak, D.P.2
  • 18
    • 0032535452 scopus 로고    scopus 로고
    • A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation
    • Imataka H., Gradi A., Sonenberg N. A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation. EMBO J. 1998, 17:7480-7489.
    • (1998) EMBO J. , vol.17 , pp. 7480-7489
    • Imataka, H.1    Gradi, A.2    Sonenberg, N.3
  • 19
    • 70349329466 scopus 로고    scopus 로고
    • The generation of stable, high MAb expressing CHO cell lines based on the artificial chromosome expression (ACE) technology
    • Kennard M.L., Goosney D.L., Monteith D., Zhang L., Moffat M., Fischer D., Mott J. The generation of stable, high MAb expressing CHO cell lines based on the artificial chromosome expression (ACE) technology. Biotechnol. Bioeng. 2009, 104:540-553.
    • (2009) Biotechnol. Bioeng. , vol.104 , pp. 540-553
    • Kennard, M.L.1    Goosney, D.L.2    Monteith, D.3    Zhang, L.4    Moffat, M.5    Fischer, D.6    Mott, J.7
  • 20
    • 0031048319 scopus 로고    scopus 로고
    • Influenza neuraminidase inhibitors possessing a novel hydrophobic interaction in the enzyme active site: design, synthesis, and structural analysis of carbocyclic sialic acid analogues with potent anti-influenza activity
    • Kim C.U., Lew W., Williams M.A., Liu H., Zhang L., Swaminathan S., Bischofberger N., Chen M.S., Mendel D.B., Tai C.Y., Laver W.G., Stevens R.C. Influenza neuraminidase inhibitors possessing a novel hydrophobic interaction in the enzyme active site: design, synthesis, and structural analysis of carbocyclic sialic acid analogues with potent anti-influenza activity. J. Am. Chem. Soc. 1997, 119:681-690.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 681-690
    • Kim, C.U.1    Lew, W.2    Williams, M.A.3    Liu, H.4    Zhang, L.5    Swaminathan, S.6    Bischofberger, N.7    Chen, M.S.8    Mendel, D.B.9    Tai, C.Y.10    Laver, W.G.11    Stevens, R.C.12
  • 23
    • 72049092943 scopus 로고    scopus 로고
    • Detection of an oseltamivir-resistant pandemic influenza A/H1N1 virus in Hong Kong
    • Leung T.W., Tai A.L., Cheng P.K., Kong M.S., Lim W. Detection of an oseltamivir-resistant pandemic influenza A/H1N1 virus in Hong Kong. J. Clin. Virol. 2009, 46:298-299.
    • (2009) J. Clin. Virol. , vol.46 , pp. 298-299
    • Leung, T.W.1    Tai, A.L.2    Cheng, P.K.3    Kong, M.S.4    Lim, W.5
  • 24
    • 53549124125 scopus 로고    scopus 로고
    • Enhancement of transient gene expression and culture viability using Chinese hamster ovary cells overexpressing Bcl-x(L)
    • Majors B.S., Betenbaugh M.J., Pederson N.E., Chiang G.G. Enhancement of transient gene expression and culture viability using Chinese hamster ovary cells overexpressing Bcl-x(L). Biotechnol. Bioeng. 2008, 101:567-578.
    • (2008) Biotechnol. Bioeng. , vol.101 , pp. 567-578
    • Majors, B.S.1    Betenbaugh, M.J.2    Pederson, N.E.3    Chiang, G.G.4
  • 25
    • 0030694071 scopus 로고    scopus 로고
    • The N-terminal half of the influenza virus NS1 protein is sufficient for nuclear retention of mRNA and enhancement of viral mRNA translation
    • Marion R.M., Aragon T., Beloso A., Nieto A., Ortin J. The N-terminal half of the influenza virus NS1 protein is sufficient for nuclear retention of mRNA and enhancement of viral mRNA translation. Nucleic Acids Res. 1997, 25:4271-4277.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4271-4277
    • Marion, R.M.1    Aragon, T.2    Beloso, A.3    Nieto, A.4    Ortin, J.5
  • 26
    • 0030843878 scopus 로고    scopus 로고
    • Protection of mice against a lethal influenza challenge by immunization with yeast-derived recombinant influenza neuraminidase
    • Martinet W., Saelens X., Deroo T., Neirynck S., Contreras R., Min Jou W., Fiers W. Protection of mice against a lethal influenza challenge by immunization with yeast-derived recombinant influenza neuraminidase. Eur. J. Biochem. 1997, 247:332-338.
    • (1997) Eur. J. Biochem. , vol.247 , pp. 332-338
    • Martinet, W.1    Saelens, X.2    Deroo, T.3    Neirynck, S.4    Contreras, R.5    Min Jou, W.6    Fiers, W.7
  • 28
    • 0018421350 scopus 로고
    • Fluorometric assay of neuraminidase with a sodium (4-methylumbelliferyl-alpha-d-N-acetylneuraminate) substrate
    • Potier M., Mameli L., Belisle M., Dallaire L., Melancon S.B. Fluorometric assay of neuraminidase with a sodium (4-methylumbelliferyl-alpha-d-N-acetylneuraminate) substrate. Anal. Biochem. 1979, 94:287-296.
    • (1979) Anal. Biochem. , vol.94 , pp. 287-296
    • Potier, M.1    Mameli, L.2    Belisle, M.3    Dallaire, L.4    Melancon, S.B.5
  • 30
    • 0036147256 scopus 로고    scopus 로고
    • Effects of influenza A virus NS1 protein on protein expression: the NS1 protein enhances translation and is not required for shutoff of host protein synthesis
    • Salvatore M., Basler C.F., Parisien J.P., Horvath C.M., Bourmakina S., Zheng H., Muster T., Palese P., Garcia-Sastre A. Effects of influenza A virus NS1 protein on protein expression: the NS1 protein enhances translation and is not required for shutoff of host protein synthesis. J. Virol. 2002, 76:1206-1212.
    • (2002) J. Virol. , vol.76 , pp. 1206-1212
    • Salvatore, M.1    Basler, C.F.2    Parisien, J.P.3    Horvath, C.M.4    Bourmakina, S.5    Zheng, H.6    Muster, T.7    Palese, P.8    Garcia-Sastre, A.9
  • 31
    • 79951521237 scopus 로고    scopus 로고
    • A generic system for the expression and purification of soluble and stable influenza neuraminidase
    • Schmidt P.M., Attwood R.M., Mohr P.G., Barrett S.A., McKimm-Breschkim J.L. A generic system for the expression and purification of soluble and stable influenza neuraminidase. PLoS One 2011, 6(2):e16284.
    • (2011) PLoS One , vol.6 , Issue.2
    • Schmidt, P.M.1    Attwood, R.M.2    Mohr, P.G.3    Barrett, S.A.4    McKimm-Breschkim, J.L.5
  • 32
    • 0001131495 scopus 로고
    • Behavior and analysis of steady-state and rapid equilibrium enzyme system
    • Wiley-Interscience, New York, I.H. Segal (Ed.)
    • Segal I.H. Behavior and analysis of steady-state and rapid equilibrium enzyme system. Enzyme Kinetics 1975, 100-160. Wiley-Interscience, New York. I.H. Segal (Ed.).
    • (1975) Enzyme Kinetics , pp. 100-160
    • Segal, I.H.1
  • 34
    • 0348003908 scopus 로고    scopus 로고
    • Comparison of seven different heterologous protein expression systems for the production of the serotonin transporter
    • Tate C.G., Hasse J., Baker C., Boorsma M., Magnani F., Vallis Y., Williams D.C. Comparison of seven different heterologous protein expression systems for the production of the serotonin transporter. Biochim. Biophys. Acta 2003, 1610:141-153.
    • (2003) Biochim. Biophys. Acta , vol.1610 , pp. 141-153
    • Tate, C.G.1    Hasse, J.2    Baker, C.3    Boorsma, M.4    Magnani, F.5    Vallis, Y.6    Williams, D.C.7
  • 38
    • 70649104597 scopus 로고    scopus 로고
    • Extraction of catalytically active neuraminidase of H5N1 influenza virus using thrombin proteolytic cleavage
    • Wanitchang A., Wongwisarnsri S., Yongkiettrakul S., Jongkaewwattana A. Extraction of catalytically active neuraminidase of H5N1 influenza virus using thrombin proteolytic cleavage. J. Virol. Methods 2010, 163:137-143.
    • (2010) J. Virol. Methods , vol.163 , pp. 137-143
    • Wanitchang, A.1    Wongwisarnsri, S.2    Yongkiettrakul, S.3    Jongkaewwattana, A.4
  • 40
    • 36048996081 scopus 로고    scopus 로고
    • Neuraminidase inhibitor-resistant recombinant A/Vietnam/1203/04 (H5N1) influenza viruses retain their replication efficiency and pathogenicity in vitro and in vivo
    • Yen H.L., Ilyushina N.A., Salomon R., Hoffmann E., Webster R.G., Govorkova E.A. Neuraminidase inhibitor-resistant recombinant A/Vietnam/1203/04 (H5N1) influenza viruses retain their replication efficiency and pathogenicity in vitro and in vivo. J. Virol. 2007, 81:12418-12426.
    • (2007) J. Virol. , vol.81 , pp. 12418-12426
    • Yen, H.L.1    Ilyushina, N.A.2    Salomon, R.3    Hoffmann, E.4    Webster, R.G.5    Govorkova, E.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.