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Volumn 100, Issue 1, 2008, Pages 28-37

Escherichia coli-based cell-free synthesis of virus-like particles

Author keywords

Cell free protein synthesis; Hepatitis B; MS2; Virus like particles; VLP

Indexed keywords

CELLS; DRUG DELIVERY; PROTEINS; VACCINES; VIRUSES;

EID: 42549090557     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.21716     Document Type: Article
Times cited : (153)

References (48)
  • 5
    • 33744829027 scopus 로고    scopus 로고
    • Virus-like particles: Combining innate and adaptive immunity for effective vaccination
    • Kaufmann SHE, editor, Weinheim: WILEY-VCH Verlag GmbH & Co. KGaA, pp
    • Bachmann MF, Jennings GT. 2004. Virus-like particles: Combining innate and adaptive immunity for effective vaccination. In: Kaufmann SHE, editor. Novel vaccination strategies. Weinheim: WILEY-VCH Verlag GmbH & Co. KGaA, pp. 415-430.
    • (2004) Novel vaccination strategies , pp. 415-430
    • Bachmann, M.F.1    Jennings, G.T.2
  • 7
    • 0016261362 scopus 로고
    • Intermediates of bacteriophage-Ms2 assembly in vivo
    • Bonner PH. 1974. Intermediates of bacteriophage-Ms2 assembly in vivo. J Virol 14(5):1152-1168.
    • (1974) J Virol , vol.14 , Issue.5 , pp. 1152-1168
    • Bonner, P.H.1
  • 9
    • 23244440886 scopus 로고    scopus 로고
    • An economical method for cell-free protein synthesis using glucose and nucleoside monophosphates
    • Calhoun KA, Swartz JR. 2005. An economical method for cell-free protein synthesis using glucose and nucleoside monophosphates. Biotechnol Progr 21(4):1146-1153.
    • (2005) Biotechnol Progr , vol.21 , Issue.4 , pp. 1146-1153
    • Calhoun, K.A.1    Swartz, J.R.2
  • 10
    • 0036786867 scopus 로고    scopus 로고
    • Weak protein-protein interactions are sufficient to drive assembly of hepatitis B virus capsids
    • Ceres P, Zlotnick A. 2002. Weak protein-protein interactions are sufficient to drive assembly of hepatitis B virus capsids. Biochemistry 41(39):11525-11531.
    • (2002) Biochemistry , vol.41 , Issue.39 , pp. 11525-11531
    • Ceres, P.1    Zlotnick, A.2
  • 11
    • 33646578826 scopus 로고    scopus 로고
    • Viruses: Making friends with old foes
    • Douglas T, Young M. 2006. Viruses: Making friends with old foes. Science 312(5775):873-875.
    • (2006) Science , vol.312 , Issue.5775 , pp. 873-875
    • Douglas, T.1    Young, M.2
  • 12
    • 0023840230 scopus 로고
    • Ompt encodes the Escherichia-coli outer-membrane protease that cleaves T7-RNA polymerase during purification
    • Grodberg J, Dunn JJ. 1988. Ompt encodes the Escherichia-coli outer-membrane protease that cleaves T7-RNA polymerase during purification. J Bacteriol 170(3):1245-1253.
    • (1988) J Bacteriol , vol.170 , Issue.3 , pp. 1245-1253
    • Grodberg, J.1    Dunn, J.J.2
  • 13
    • 1642314171 scopus 로고    scopus 로고
    • Interior surface modification of bacteriophage MS2
    • Hooker JM, Kovacs EW, Francis MB. 2004. Interior surface modification of bacteriophage MS2. J Am Chem Soc 126(12):3718-3719.
    • (2004) J Am Chem Soc , vol.126 , Issue.12 , pp. 3718-3719
    • Hooker, J.M.1    Kovacs, E.W.2    Francis, M.B.3
  • 14
    • 0037095730 scopus 로고    scopus 로고
    • DNAWorks: An automated method for designing oligonucleotides for PCR-based gene synthesis
    • Hoover DM, Lubkowski J. 2002. DNAWorks: An automated method for designing oligonucleotides for PCR-based gene synthesis. Nucleic Acids Res 30(10):E43.
    • (2002) Nucleic Acids Res , vol.30 , Issue.10
    • Hoover, D.M.1    Lubkowski, J.2
  • 16
    • 1542720448 scopus 로고    scopus 로고
    • Mimicking the Escherichia coli cytoplasmic environment activates long-lived and efficient cell-free protein synthesis
    • Jewett MC, Swartz JR. 2004a. Mimicking the Escherichia coli cytoplasmic environment activates long-lived and efficient cell-free protein synthesis. Biotechnol Bioeng 86(1):19-26.
    • (2004) Biotechnol Bioeng , vol.86 , Issue.1 , pp. 19-26
    • Jewett, M.C.1    Swartz, J.R.2
  • 17
    • 1142269592 scopus 로고    scopus 로고
    • Rapid expression and purification of 100 nmol quantities of active protein using cell-free protein synthesis
    • Jewett MC, Swartz JR. 2004b. Rapid expression and purification of 100 nmol quantities of active protein using cell-free protein synthesis. Biotechnol Progr 20(1):102-109.
    • (2004) Biotechnol Progr , vol.20 , Issue.1 , pp. 102-109
    • Jewett, M.C.1    Swartz, J.R.2
  • 18
    • 0037162453 scopus 로고    scopus 로고
    • An engineered Escherichia coli tyrosyl-tRNA synthetase for site-specific incorporation of an unnatural amino acid into proteins in eukaryotic translation and its application in a wheat germ cell-free system
    • Kiga D, Sakamoto K, Kodama K, Kigawa T, Matsuda T, Yabuki T, Shirouzu M, Harada Y, Nakayama H, Takio K, et al. 2002. An engineered Escherichia coli tyrosyl-tRNA synthetase for site-specific incorporation of an unnatural amino acid into proteins in eukaryotic translation and its application in a wheat germ cell-free system. Proc Natl Acad Sci USA 99(15):9715-9720.
    • (2002) Proc Natl Acad Sci USA , vol.99 , Issue.15 , pp. 9715-9720
    • Kiga, D.1    Sakamoto, K.2    Kodama, K.3    Kigawa, T.4    Matsuda, T.5    Yabuki, T.6    Shirouzu, M.7    Harada, Y.8    Nakayama, H.9    Takio, K.10
  • 20
    • 0033514992 scopus 로고    scopus 로고
    • Native display of complete foreign protein domains on the surface of hepatitis B virus capsids
    • Kratz PA, Bottcher B, Nassal M. 1999. Native display of complete foreign protein domains on the surface of hepatitis B virus capsids. Proc Natl Acad Sci USA 96(5):1915-1920.
    • (1999) Proc Natl Acad Sci USA , vol.96 , Issue.5 , pp. 1915-1920
    • Kratz, P.A.1    Bottcher, B.2    Nassal, M.3
  • 22
    • 16844382807 scopus 로고    scopus 로고
    • Production in Saccharomyces cerevisiae of MS2 virus-like particles packaging functional heterologous mRNAs
    • Legendre D, Fastrez J. 2005. Production in Saccharomyces cerevisiae of MS2 virus-like particles packaging functional heterologous mRNAs. J Biotechnol 117(2):183-194.
    • (2005) J Biotechnol , vol.117 , Issue.2 , pp. 183-194
    • Legendre, D.1    Fastrez, J.2
  • 23
    • 13544270914 scopus 로고    scopus 로고
    • Comparing capsid assembly of primate lentiviruses and hepatitis B virus using cell-free systems
    • Lingappa JR, Newman MA, Klein KC, Dooher JE. 2005. Comparing capsid assembly of primate lentiviruses and hepatitis B virus using cell-free systems. Virology 333(1):114-123.
    • (2005) Virology , vol.333 , Issue.1 , pp. 114-123
    • Lingappa, J.R.1    Newman, M.A.2    Klein, K.C.3    Dooher, J.E.4
  • 24
    • 16344377955 scopus 로고    scopus 로고
    • Streamlining Escherichia coli S30 extract preparation for economical cell-free protein synthesis
    • Liu DV, Zawada JF, Swartz JR. 2005. Streamlining Escherichia coli S30 extract preparation for economical cell-free protein synthesis. Biotechnol Progr 21(2):460-465.
    • (2005) Biotechnol Progr , vol.21 , Issue.2 , pp. 460-465
    • Liu, D.V.1    Zawada, J.F.2    Swartz, J.R.3
  • 25
    • 0027407913 scopus 로고
    • Multiple presentation of foreign peptides on the surface of an RNA-free spherical bacteriophage capsid
    • Mastico RA, Talbot SJ, Stockley PG. 1993. Multiple presentation of foreign peptides on the surface of an RNA-free spherical bacteriophage capsid. J Gen Virol 74:541-548.
    • (1993) J Gen Virol , vol.74 , pp. 541-548
    • Mastico, R.A.1    Talbot, S.J.2    Stockley, P.G.3
  • 26
    • 32544457847 scopus 로고    scopus 로고
    • Therapeutic vaccines for nicotine dependence
    • Maurer P, Bachmann MF. 2006. Therapeutic vaccines for nicotine dependence. Curr Opin Mol Ther 8(1):11-16.
    • (2006) Curr Opin Mol Ther , vol.8 , Issue.1 , pp. 11-16
    • Maurer, P.1    Bachmann, M.F.2
  • 29
    • 24944552040 scopus 로고    scopus 로고
    • Towards the preparative and large-scale precision manufacture of virus-like particles
    • Pattenden LK, Middelberg APJ, Niebert M, Lipin DI. 2005. Towards the preparative and large-scale precision manufacture of virus-like particles. Trends Biotechnol 23(10):523-529.
    • (2005) Trends Biotechnol , vol.23 , Issue.10 , pp. 523-529
    • Pattenden, L.K.1    Middelberg, A.P.J.2    Niebert, M.3    Lipin, D.I.4
  • 30
    • 0030968219 scopus 로고    scopus 로고
    • Role of the coat protein-RNA interaction in the life cycle of bacteriophage MS2
    • Peabody DS. 1997. Role of the coat protein-RNA interaction in the life cycle of bacteriophage MS2. Mol Gen Genet 254(4):358-364.
    • (1997) Mol Gen Genet , vol.254 , Issue.4 , pp. 358-364
    • Peabody, D.S.1
  • 31
    • 2942572809 scopus 로고    scopus 로고
    • A viral platform for chemical modification and multivalent display
    • Peabody DS. 2003. A viral platform for chemical modification and multivalent display. J Nanobiotechnol 1 5.
    • (2003) J Nanobiotechnol 1 , vol.5
    • Peabody, D.S.1
  • 32
    • 0027486046 scopus 로고
    • Encapsidation of heterologous RNAs by bacteriophage-MS2 coat protein
    • Pickett GG, Peabody DS. 1993. Encapsidation of heterologous RNAs by bacteriophage-MS2 coat protein. Nucleic Acids Res 21(19):4621-4626.
    • (1993) Nucleic Acids Res , vol.21 , Issue.19 , pp. 4621-4626
    • Pickett, G.G.1    Peabody, D.S.2
  • 33
    • 0034889864 scopus 로고    scopus 로고
    • HBV core particles as a carrier for B cell/T cell epitopes
    • Pumpens P, Grens E. 2001. HBV core particles as a carrier for B cell/T cell epitopes. Intervirology 44(2-3):98-114.
    • (2001) Intervirology , vol.44 , Issue.2-3 , pp. 98-114
    • Pumpens, P.1    Grens, E.2
  • 34
    • 33750728433 scopus 로고    scopus 로고
    • Targeting dendritic cells with biomaterials: Developing the next generation of vaccines
    • Reddy ST, Swartz MA, Hubbell JA. 2006. Targeting dendritic cells with biomaterials: Developing the next generation of vaccines. Trends Immunol 27(12):573-579.
    • (2006) Trends Immunol , vol.27 , Issue.12 , pp. 573-579
    • Reddy, S.T.1    Swartz, M.A.2    Hubbell, J.A.3
  • 35
    • 0014840905 scopus 로고
    • Physical, biochemical, and immunological properties of coliphage MS-2 particles
    • Rohrmann GF, Krueger RG. 1970. Physical, biochemical, and immunological properties of coliphage MS-2 particles. J Virol 6(3):269-279.
    • (1970) J Virol , vol.6 , Issue.3 , pp. 269-279
    • Rohrmann, G.F.1    Krueger, R.G.2
  • 36
    • 33847399192 scopus 로고    scopus 로고
    • Advocating for the quadravalent HPV vaccination, Gardasil, by Merck
    • Rothengass BE. 2007. Advocating for the quadravalent HPV vaccination, Gardasil, by Merck. Int J Pediatr Otorhi 71(4):671-672.
    • (2007) Int J Pediatr Otorhi , vol.71 , Issue.4 , pp. 671-672
    • Rothengass, B.E.1
  • 37
    • 0033076481 scopus 로고    scopus 로고
    • Inorganic-organic nanotube composites from template mineralization of tobacco mosaic virus
    • Shenton W, Douglas T, Young M, Stubbs G, Mann S. 1999. Inorganic-organic nanotube composites from template mineralization of tobacco mosaic virus. Adv Mater 11(3):253-256.
    • (1999) Adv Mater , vol.11 , Issue.3 , pp. 253-256
    • Shenton, W.1    Douglas, T.2    Young, M.3    Stubbs, G.4    Mann, S.5
  • 39
    • 0029152885 scopus 로고
    • The potentials of the in vitro protein biosynthesis system
    • Stiege W, Erdmann VA. 1995. The potentials of the in vitro protein biosynthesis system. J Biotechnol 41(2-3):81-90.
    • (1995) J Biotechnol , vol.41 , Issue.2-3 , pp. 81-90
    • Stiege, W.1    Erdmann, V.A.2
  • 40
    • 25144506135 scopus 로고    scopus 로고
    • Viruses in the sea
    • Suttle CA. 2005. Viruses in the sea. Nature 437(7057):356-361.
    • (2005) Nature , vol.437 , Issue.7057 , pp. 356-361
    • Suttle, C.A.1
  • 41
    • 23244446620 scopus 로고    scopus 로고
    • Quantitative polysome analysis identifies limitations in bacterial cell-free protein synthesis
    • Underwood KA, Swartz JR, Puglisi JD. 2005. Quantitative polysome analysis identifies limitations in bacterial cell-free protein synthesis. Biotechnol Bioeng 91(4):425-435.
    • (2005) Biotechnol Bioeng , vol.91 , Issue.4 , pp. 425-435
    • Underwood, K.A.1    Swartz, J.R.2    Puglisi, J.D.3
  • 43
    • 23244462601 scopus 로고    scopus 로고
    • Efficient and scalable method for scaling up cell free protein synthesis in batch mode
    • Voloshin AM, Swartz JR. 2005. Efficient and scalable method for scaling up cell free protein synthesis in batch mode. Biotechnol Bioeng 91(4):516-521.
    • (2005) Biotechnol Bioeng , vol.91 , Issue.4 , pp. 516-521
    • Voloshin, A.M.1    Swartz, J.R.2
  • 44
    • 84889282595 scopus 로고    scopus 로고
    • Large-scale batch reactions for cell-free protein synthesis
    • Spirin AS, Swartz JR, editors, Weinheim: Wiley-VCH Verlag GmbH & Co. KGaA. p
    • Voloshin AM, Swartz JR. 2007. Large-scale batch reactions for cell-free protein synthesis. In: Spirin AS, Swartz JR, editors. Cell-free protein synthesis: methods and protocols. Weinheim: Wiley-VCH Verlag GmbH & Co. KGaA. p. 207-235.
    • (2007) Cell-free protein synthesis: Methods and protocols , pp. 207-235
    • Voloshin, A.M.1    Swartz, J.R.2
  • 45
    • 0028953769 scopus 로고
    • Hepatitis core antigen produced in Escherichia-coli - Subunit composition, conformational- analysis, and in-vitro capsid assembly
    • Wingfield PT, Stahl SJ, Williams RW, Steven AC. 1995. Hepatitis core antigen produced in Escherichia-coli - Subunit composition, conformational- analysis, and in-vitro capsid assembly. Biochemistry 34(15):4919-4932.
    • (1995) Biochemistry , vol.34 , Issue.15 , pp. 4919-4932
    • Wingfield, P.T.1    Stahl, S.J.2    Williams, R.W.3    Steven, A.C.4
  • 46
    • 33845454189 scopus 로고    scopus 로고
    • Rapid expression of functional genomic libraries
    • Woodrow KA, Airen IO, Swartz JR. 2006. Rapid expression of functional genomic libraries. J Proteome Res 5(12):3288-3300.
    • (2006) J Proteome Res , vol.5 , Issue.12 , pp. 3288-3300
    • Woodrow, K.A.1    Airen, I.O.2    Swartz, J.R.3
  • 47
    • 0029366201 scopus 로고
    • Cell-specific delivery of bacteriophage-encapsidated Ricin A Chain
    • Wu M, Brown WL, Stockley PG. 1995. Cell-specific delivery of bacteriophage-encapsidated Ricin A Chain. Bioconjugate Chem 6:587-595.
    • (1995) Bioconjugate Chem , vol.6 , pp. 587-595
    • Wu, M.1    Brown, W.L.2    Stockley, P.G.3
  • 48
    • 0029950758 scopus 로고    scopus 로고
    • Dimorphism of hepatitis B virus capsids is strongly influenced by the c-terminus of the capsid protein
    • Zlotnick A, Cheng N, Conway JF, Booy FP, Steven AC, Stahl SJ, Wingfield PT. 1996. Dimorphism of hepatitis B virus capsids is strongly influenced by the c-terminus of the capsid protein. Biochemistry 35(23):7412-7421.
    • (1996) Biochemistry , vol.35 , Issue.23 , pp. 7412-7421
    • Zlotnick, A.1    Cheng, N.2    Conway, J.F.3    Booy, F.P.4    Steven, A.C.5    Stahl, S.J.6    Wingfield, P.T.7


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