메뉴 건너뛰기




Volumn 196, Issue , 2014, Pages 56-64

High-yield soluble expression of recombinant influenza virus antigens from Escherichia coli and their potential uses in diagnosis

Author keywords

Antibody library; Bacteria; ELISA; Fusion partner; Influenza viruses; Recombinant proteins

Indexed keywords

HYBRID PROTEIN; INFLUENZA VIRUS HEMAGGLUTININ; LYSINE TRANSFER RNA LIGASE; LYSRS HA PROTEIN; RECOMBINANT ANTIGEN; UNCLASSIFIED DRUG; VIRUS ANTIBODY; VIRUS ANTIGEN; VIRUS PROTEIN;

EID: 84888123350     PISSN: 01660934     EISSN: 18790984     Source Type: Journal    
DOI: 10.1016/j.jviromet.2013.10.035     Document Type: Article
Times cited : (9)

References (40)
  • 2
    • 0032884573 scopus 로고    scopus 로고
    • Recombinant protein expression in Escherichia coli
    • Baneyx F. Recombinant protein expression in Escherichia coli. Curr. Opin. Biotechnol. 1999, 10:411-421.
    • (1999) Curr. Opin. Biotechnol. , vol.10 , pp. 411-421
    • Baneyx, F.1
  • 5
    • 79953297743 scopus 로고    scopus 로고
    • Chaperoning roles of macromolecules interacting with proteins in vivo
    • Choi S.I., Lim K.H., Seong B.L. Chaperoning roles of macromolecules interacting with proteins in vivo. Int. J. Mol. Sci. 2011, 12:1979-1990.
    • (2011) Int. J. Mol. Sci. , vol.12 , pp. 1979-1990
    • Choi, S.I.1    Lim, K.H.2    Seong, B.L.3
  • 6
    • 62549125006 scopus 로고    scopus 로고
    • RNA-mediated chaperone type for de novo protein folding
    • Choi S.I., Ryu K., Seong B.L. RNA-mediated chaperone type for de novo protein folding. RNA Biol. 2009, 6:21-24.
    • (2009) RNA Biol. , vol.6 , pp. 21-24
    • Choi, S.I.1    Ryu, K.2    Seong, B.L.3
  • 8
    • 0019840585 scopus 로고
    • Expression of antigenic determinants of the hemagglutinin gene of a human influenza virus in Escherichia coli
    • Davis A.R., Nayak D.P., Ueda M., Hiti A.L., Dowbenko D., Kleid D.G. Expression of antigenic determinants of the hemagglutinin gene of a human influenza virus in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 1981, 78:5376-5380.
    • (1981) Proc. Natl. Acad. Sci. U.S.A. , vol.78 , pp. 5376-5380
    • Davis, A.R.1    Nayak, D.P.2    Ueda, M.3    Hiti, A.L.4    Dowbenko, D.5    Kleid, D.G.6
  • 9
    • 0033589826 scopus 로고    scopus 로고
    • New fusion protein systems designed to give soluble expression in Escherichia coli
    • Davis G.D., Elisee C., Newham D.M., Harrison R.G. New fusion protein systems designed to give soluble expression in Escherichia coli. Biotechnol. Bioeng. 1999, 65:328-382.
    • (1999) Biotechnol. Bioeng. , vol.65 , pp. 328-382
    • Davis, G.D.1    Elisee, C.2    Newham, D.M.3    Harrison, R.G.4
  • 11
    • 77955659571 scopus 로고    scopus 로고
    • Prokaryotic expression and characterization of avian influenza A virus M2 gene as a candidate for universal recombinant vaccine against influenza A subtypes; specially H5N1 and H9N2
    • Ebrahimi S.M., Tebianian M., Aghaiypour K., Nili H., Mirjalili A. Prokaryotic expression and characterization of avian influenza A virus M2 gene as a candidate for universal recombinant vaccine against influenza A subtypes; specially H5N1 and H9N2. Mol. Biol. Rep. 2010, 37:2909-2914.
    • (2010) Mol. Biol. Rep. , vol.37 , pp. 2909-2914
    • Ebrahimi, S.M.1    Tebianian, M.2    Aghaiypour, K.3    Nili, H.4    Mirjalili, A.5
  • 13
    • 33746744319 scopus 로고    scopus 로고
    • Enhancement of soluble protein expression through the use of fusion tags
    • Esposito D., Chatterjee D.K. Enhancement of soluble protein expression through the use of fusion tags. Curr. Opin. Biotechnol. 2006, 17:353-358.
    • (2006) Curr. Opin. Biotechnol. , vol.17 , pp. 353-358
    • Esposito, D.1    Chatterjee, D.K.2
  • 16
    • 0037208811 scopus 로고    scopus 로고
    • Maltose-binding protein as a solubility enhancer
    • Fox J.D., Waugh D.S. Maltose-binding protein as a solubility enhancer. Methods Mol. Biol. 2003, 205:99-117.
    • (2003) Methods Mol. Biol. , vol.205 , pp. 99-117
    • Fox, J.D.1    Waugh, D.S.2
  • 17
    • 0032559232 scopus 로고    scopus 로고
    • Induced folding in RNA-protein recognition: more than a simple molecular handshake
    • Frankel A.D., Smith C.A. Induced folding in RNA-protein recognition: more than a simple molecular handshake. Cell 1998, 92:149-151.
    • (1998) Cell , vol.92 , pp. 149-151
    • Frankel, A.D.1    Smith, C.A.2
  • 18
    • 84871574987 scopus 로고    scopus 로고
    • Influenza A virus nucleoprotein derived from Escherichia coli or recombinant vaccinia (Tiantan) virus elicits robust cross-protection in mice
    • Huang B., Wang W., Li R., Wang X., Jiang T., Qi X., Gao Y., Tan W., Ruan L. Influenza A virus nucleoprotein derived from Escherichia coli or recombinant vaccinia (Tiantan) virus elicits robust cross-protection in mice. Virol. J. 2012, 9:322.
    • (2012) Virol. J. , vol.9 , pp. 322
    • Huang, B.1    Wang, W.2    Li, R.3    Wang, X.4    Jiang, T.5    Qi, X.6    Gao, Y.7    Tan, W.8    Ruan, L.9
  • 20
    • 0022255630 scopus 로고
    • Differential expression of influenza N protein and neuraminidase antigenic determinants in Escherichia coli
    • Jones I.M., Brownlee G.G. Differential expression of influenza N protein and neuraminidase antigenic determinants in Escherichia coli. Gene 1985, 35:333-342.
    • (1985) Gene , vol.35 , pp. 333-342
    • Jones, I.M.1    Brownlee, G.G.2
  • 21
    • 77955411860 scopus 로고    scopus 로고
    • Properly folded bacterially expressed H1N1 hemagglutinin globular head and ectodomain vaccines protect ferrets against H1N1 pandemic influenza virus
    • Khurana S., Verma S., Verma N., Crevar C.J., Carter D.M., Manischewitz J., King L.R., Ross T.M., Golding H. Properly folded bacterially expressed H1N1 hemagglutinin globular head and ectodomain vaccines protect ferrets against H1N1 pandemic influenza virus. PLoS ONE 2010, 5:e11548.
    • (2010) PLoS ONE , vol.5
    • Khurana, S.1    Verma, S.2    Verma, N.3    Crevar, C.J.4    Carter, D.M.5    Manischewitz, J.6    King, L.R.7    Ross, T.M.8    Golding, H.9
  • 22
    • 78651396311 scopus 로고    scopus 로고
    • Bacterial HA1 vaccine against pandemic H5N1 influenza virus: evidence of oligomerization, hemagglutination, and cross-protective immunity in ferrets
    • Khurana S., Verma S., Verma N., Crevar C.J., Carter D.M., Manischewitz J., King L.R., Ross T.M., Golding H. Bacterial HA1 vaccine against pandemic H5N1 influenza virus: evidence of oligomerization, hemagglutination, and cross-protective immunity in ferrets. J. Virol. 2011, 85:1246-1256.
    • (2011) J. Virol. , vol.85 , pp. 1246-1256
    • Khurana, S.1    Verma, S.2    Verma, N.3    Crevar, C.J.4    Carter, D.M.5    Manischewitz, J.6    King, L.R.7    Ross, T.M.8    Golding, H.9
  • 23
    • 0023244108 scopus 로고
    • Immunologic response to the influenza virus neuraminidase is influenced by prior experience with the associated viral hemagglutinin. I. Studies in human vaccinees
    • Kilbourne E.D., Cerini C.P., Khan M.W., Mitchell J.W., Ogra P.L. Immunologic response to the influenza virus neuraminidase is influenced by prior experience with the associated viral hemagglutinin. I. Studies in human vaccinees. J. Immunol. 1987, 138:3010-3013.
    • (1987) J. Immunol. , vol.138 , pp. 3010-3013
    • Kilbourne, E.D.1    Cerini, C.P.2    Khan, M.W.3    Mitchell, J.W.4    Ogra, P.L.5
  • 24
    • 33947728505 scopus 로고    scopus 로고
    • N-terminal domains of native multidomain proteins have the potential to assist de novo folding of their downstream domains in vivo by acting as solubility enhancers
    • Kim C.W., Han K.S., Ryu K.S., Kim B.H., Kim K.H., Choi S.I., Seong B.L. N-terminal domains of native multidomain proteins have the potential to assist de novo folding of their downstream domains in vivo by acting as solubility enhancers. Protein Sci. 2007, 16:635-643.
    • (2007) Protein Sci. , vol.16 , pp. 635-643
    • Kim, C.W.1    Han, K.S.2    Ryu, K.S.3    Kim, B.H.4    Kim, K.H.5    Choi, S.I.6    Seong, B.L.7
  • 25
    • 0001178029 scopus 로고    scopus 로고
    • Orthomyxoviridae: the viruses and their replication
    • Lippincott Williams & Wilkins, Philadelphia, M. David, P.M.H. Knipe (Eds.)
    • Krug R.A.L.R.M. Orthomyxoviridae: the viruses and their replication. Fields Virology 2001, 1487-1532. Lippincott Williams & Wilkins, Philadelphia. M. David, P.M.H. Knipe (Eds.).
    • (2001) Fields Virology , pp. 1487-1532
    • Lamb, R.A.1    Krug, R.M.2
  • 26
    • 84871797768 scopus 로고    scopus 로고
    • Recombinant haemagglutinin protein of highly pathogenic avian influenza A (H5N1) virus expressed in Pichia pastoris elicits a neutralizing antibody response in mice
    • Murugan S., Ponsekaran S., Kannivel L., Mangamoori L.N., Chandran D., Villuppanoor Alwar S., Chakravarty C., Lal S.K. Recombinant haemagglutinin protein of highly pathogenic avian influenza A (H5N1) virus expressed in Pichia pastoris elicits a neutralizing antibody response in mice. J. Virol. Methods 2013, 187:20-25.
    • (2013) J. Virol. Methods , vol.187 , pp. 20-25
    • Murugan, S.1    Ponsekaran, S.2    Kannivel, L.3    Mangamoori, L.N.4    Chandran, D.5    Villuppanoor Alwar, S.6    Chakravarty, C.7    Lal, S.K.8
  • 27
    • 28844481147 scopus 로고    scopus 로고
    • Solubility-enhancing proteins MBP and NusA play a passive role in the folding of their fusion partners
    • Nallamsetty S., Waugh D.S. Solubility-enhancing proteins MBP and NusA play a passive role in the folding of their fusion partners. Protein Exp. Purif. 2006, 45:175-182.
    • (2006) Protein Exp. Purif. , vol.45 , pp. 175-182
    • Nallamsetty, S.1    Waugh, D.S.2
  • 28
    • 0032874490 scopus 로고    scopus 로고
    • A universal influenza A vaccine based on the extracellular domain of the M2 protein
    • Neirynck S., Deroo T., Saelens X., Vanlandschoot P., Jou W.M., Fiers W. A universal influenza A vaccine based on the extracellular domain of the M2 protein. Nat. Med. 1999, 5:1157-1163.
    • (1999) Nat. Med. , vol.5 , pp. 1157-1163
    • Neirynck, S.1    Deroo, T.2    Saelens, X.3    Vanlandschoot, P.4    Jou, W.M.5    Fiers, W.6
  • 29
    • 67649297821 scopus 로고    scopus 로고
    • Emergence and pandemic potential of swine-origin H1N1 influenza virus
    • Neumann G., Noda T., Kawaoka Y. Emergence and pandemic potential of swine-origin H1N1 influenza virus. Nature 2009, 459:931-939.
    • (2009) Nature , vol.459 , pp. 931-939
    • Neumann, G.1    Noda, T.2    Kawaoka, Y.3
  • 31
    • 0034796387 scopus 로고    scopus 로고
    • A history of influenza
    • Potter C.W. A history of influenza. J. Appl. Microbiol. 2001, 91:572-579.
    • (2001) J. Appl. Microbiol. , vol.91 , pp. 572-579
    • Potter, C.W.1
  • 32
    • 0032978995 scopus 로고    scopus 로고
    • Acceleration of the refolding of Arc repressor by nucleic acids and other polyanions
    • Rentzeperis D., Jonsson T., Sauer R.T. Acceleration of the refolding of Arc repressor by nucleic acids and other polyanions. Nat. Struct. Biol. 1999, 6:569-573.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 569-573
    • Rentzeperis, D.1    Jonsson, T.2    Sauer, R.T.3
  • 34
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith D.B., Johnson K.S. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene 1988, 67:31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 36
    • 0034669882 scopus 로고    scopus 로고
    • Why are natively unfolded proteins unstructured under physiologic conditions?
    • Uversky V.N., Gillespie J.R., Fink A.L. Why are natively unfolded proteins unstructured under physiologic conditions?. Proteins 2000, 41:415-427.
    • (2000) Proteins , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 37
    • 84877693578 scopus 로고    scopus 로고
    • Global concerns regarding novel influenza A (H7N9) virus infections
    • Uyeki T.M., Cox N.J. Global concerns regarding novel influenza A (H7N9) virus infections. New Engl. J. Med. 2013, 368:1862-1864.
    • (2013) New Engl. J. Med. , vol.368 , pp. 1862-1864
    • Uyeki, T.M.1    Cox, N.J.2
  • 40
    • 84860309632 scopus 로고    scopus 로고
    • Recombinant protein expression and purification: a comprehensive review of affinity tags and microbial applications
    • Young C.L., Britton Z.T., Robinson A.S. Recombinant protein expression and purification: a comprehensive review of affinity tags and microbial applications. Biotechnol. J. 2012, 7:620-634.
    • (2012) Biotechnol. J. , vol.7 , pp. 620-634
    • Young, C.L.1    Britton, Z.T.2    Robinson, A.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.