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Volumn 136, Issue 1-2, 2006, Pages 283-288

Surface display of an internal His-tag on virus-like particles of Nudaurelia capensis ω virus (NωV) produced in a baculovirus expression system

Author keywords

Baculovirus expression; His tag; Nudaurelia capensis virus; Surface display; Tetravirus; Virus like particle

Indexed keywords

CAPSID PROTEIN; HISTIDINE; NANOPARTICLE; RNA;

EID: 33746082812     PISSN: 01660934     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jviromet.2006.05.014     Document Type: Article
Times cited : (9)

References (25)
  • 1
    • 0028906644 scopus 로고
    • Assembly of the T = 4 Nudaurelia capensis ω virus capsid protein, post-translational cleavage, and specific encapsidation of its mRNA in a baculovirus expression system
    • Agrawal D.K., and Johnson J.E. Assembly of the T = 4 Nudaurelia capensis ω virus capsid protein, post-translational cleavage, and specific encapsidation of its mRNA in a baculovirus expression system. Virology 207 (1995) 89-97
    • (1995) Virology , vol.207 , pp. 89-97
    • Agrawal, D.K.1    Johnson, J.E.2
  • 2
    • 0026688634 scopus 로고
    • Sequence and analysis of the capsid protein of Nudaurelia capensis ω virus with T = 4 icosahedral symmetry
    • Agrawal D.K., and Johnson J.E. Sequence and analysis of the capsid protein of Nudaurelia capensis ω virus with T = 4 icosahedral symmetry. Virology 190 (1992) 806-814
    • (1992) Virology , vol.190 , pp. 806-814
    • Agrawal, D.K.1    Johnson, J.E.2
  • 3
    • 0025730892 scopus 로고
    • Engineering metal-binding proteins: purification to protein folding
    • Arnold F.H., and Haymore B.L. Engineering metal-binding proteins: purification to protein folding. Science 252 (1991) 1796-1797
    • (1991) Science , vol.252 , pp. 1796-1797
    • Arnold, F.H.1    Haymore, B.L.2
  • 4
    • 0012176468 scopus 로고    scopus 로고
    • Family tetraviridae
    • Van Regenmortel M.H.V., Fauquet C.M., Bishop D.H.L., Carstens E.B., Estes M.K., Lemon S.M., Maniloff J., Mayo M.A., McGeoch D.J., Pringle C.R., and Wickner R.B. (Eds), Academic Press, San Diego
    • Ball L.A., Hendry D.A., Johnson J.E., Rueckert R.R., and Scotti P.D. Family tetraviridae. In: Van Regenmortel M.H.V., Fauquet C.M., Bishop D.H.L., Carstens E.B., Estes M.K., Lemon S.M., Maniloff J., Mayo M.A., McGeoch D.J., Pringle C.R., and Wickner R.B. (Eds). Virus Taxonomy, Seventh Report of the International Committee on Taxonomy of Viruses (2000), Academic Press, San Diego 757-764
    • (2000) Virus Taxonomy, Seventh Report of the International Committee on Taxonomy of Viruses , pp. 757-764
    • Ball, L.A.1    Hendry, D.A.2    Johnson, J.E.3    Rueckert, R.R.4    Scotti, P.D.5
  • 5
  • 6
    • 14644438331 scopus 로고    scopus 로고
    • Maturation of a tetravirus capsid alters the dynamic properties and creates a metastable complex
    • Bothner B., Taylor D., Jun B., Lee K.K., Suizdak G., Schultz C.P., and Johnson J.E. Maturation of a tetravirus capsid alters the dynamic properties and creates a metastable complex. Virology 334 (2005) 17-27
    • (2005) Virology , vol.334 , pp. 17-27
    • Bothner, B.1    Taylor, D.2    Jun, B.3    Lee, K.K.4    Suizdak, G.5    Schultz, C.P.6    Johnson, J.E.7
  • 7
    • 0034625320 scopus 로고    scopus 로고
    • Large conformational changes in the maturation of a simple RNA virus Nudaurelia capensis ω virus (NωV)
    • Canady M.A., Tihova M., Hanzlik T.N., Johnson J.E., and Yeager M. Large conformational changes in the maturation of a simple RNA virus Nudaurelia capensis ω virus (NωV). J. Mol. Biol. 299 (2000) 573-584
    • (2000) J. Mol. Biol. , vol.299 , pp. 573-584
    • Canady, M.A.1    Tihova, M.2    Hanzlik, T.N.3    Johnson, J.E.4    Yeager, M.5
  • 8
    • 26844463892 scopus 로고    scopus 로고
    • Revised RNA2 sequence of the tetravirus Nudaurelia capensis ω virus (NωV)
    • Du Plessis L., Hendry D.A., Dorrington R.A., Hanzlik T.N., and Appel M. Revised RNA2 sequence of the tetravirus Nudaurelia capensis ω virus (NωV). Arch. Virol. 150 (2005) 2397-2402
    • (2005) Arch. Virol. , vol.150 , pp. 2397-2402
    • Du Plessis, L.1    Hendry, D.A.2    Dorrington, R.A.3    Hanzlik, T.N.4    Appel, M.5
  • 9
    • 0031822853 scopus 로고    scopus 로고
    • An internal affinity-tag for purification and crystallization of the siderophore receptor FhuA, integral outer membrane protein from Escherichia coli K-12
    • Ferguson A.D., Breed J., Diederichs K., Welte W., and Coultoni J.W. An internal affinity-tag for purification and crystallization of the siderophore receptor FhuA, integral outer membrane protein from Escherichia coli K-12. Prot. Sci. 7 (1998) 1636-1638
    • (1998) Prot. Sci. , vol.7 , pp. 1636-1638
    • Ferguson, A.D.1    Breed, J.2    Diederichs, K.3    Welte, W.4    Coultoni, J.W.5
  • 11
    • 0034947940 scopus 로고    scopus 로고
    • Integration of PCR fragments at any specific site within cloning vectors without the use of restriction enzymes and DNA ligase
    • Geiser M., Cèbe R., Drewello D., and Schmitz R. Integration of PCR fragments at any specific site within cloning vectors without the use of restriction enzymes and DNA ligase. Biotechniques 31 (2001) 88-92
    • (2001) Biotechniques , vol.31 , pp. 88-92
    • Geiser, M.1    Cèbe, R.2    Drewello, D.3    Schmitz, R.4
  • 13
    • 0002703976 scopus 로고    scopus 로고
    • Tetraviruses (Tetraviridae)
    • Webster R.G., and Granoff R.G. (Eds), Harcourt Brace & Company, London
    • Hanzlik T.N., and Gordon K.H.J. Tetraviruses (Tetraviridae). In: Webster R.G., and Granoff R.G. (Eds). Encyclopedia of Virology. 2nd ed. (1999), Harcourt Brace & Company, London 1764-1773
    • (1999) Encyclopedia of Virology. 2nd ed. , pp. 1764-1773
    • Hanzlik, T.N.1    Gordon, K.H.J.2
  • 14
    • 1242319463 scopus 로고    scopus 로고
    • The refined structure of Nudaurelia capensis ω virus reveals control elements for a T = 4 capsid maturation
    • Helgstrand C., Munshi S., Johnson J.E., and Liljas L. The refined structure of Nudaurelia capensis ω virus reveals control elements for a T = 4 capsid maturation. Virology 318 (2004) 192-203
    • (2004) Virology , vol.318 , pp. 192-203
    • Helgstrand, C.1    Munshi, S.2    Johnson, J.E.3    Liljas, L.4
  • 15
    • 2942691397 scopus 로고    scopus 로고
    • Small compounds targeted to subunit interfaces arrest maturation in a nonenveloped, icosahedral animal virus
    • Lee K.K., Tang J., Taylor D., Bothner B., and Johnson J.E. Small compounds targeted to subunit interfaces arrest maturation in a nonenveloped, icosahedral animal virus. J. Virol. 78 (2004) 7208-7216
    • (2004) J. Virol. , vol.78 , pp. 7208-7216
    • Lee, K.K.1    Tang, J.2    Taylor, D.3    Bothner, B.4    Johnson, J.E.5
  • 16
    • 0030576341 scopus 로고    scopus 로고
    • The 28 Å structure of a T = 4 animal virus and its implications for membrane translocation of RNA
    • Munshi S., Liljas L., Cavarelli J., Bomu W.U., McKinney B., Reddy V., and Johnson J.E. The 28 Å structure of a T = 4 animal virus and its implications for membrane translocation of RNA. J. Mol. Biol. 261 (1996) 1-10
    • (1996) J. Mol. Biol. , vol.261 , pp. 1-10
    • Munshi, S.1    Liljas, L.2    Cavarelli, J.3    Bomu, W.U.4    McKinney, B.5    Reddy, V.6    Johnson, J.E.7
  • 18
    • 0037440765 scopus 로고    scopus 로고
    • Providence virus: a new member of the Tetraviridae that infects cultured insect cells
    • Pringle F.M., Johnson K.N., Goodman C.L., McIntosh A.H., and Ball A.L. Providence virus: a new member of the Tetraviridae that infects cultured insect cells. Virology 306 (2003) 359-370
    • (2003) Virology , vol.306 , pp. 359-370
    • Pringle, F.M.1    Johnson, K.N.2    Goodman, C.L.3    McIntosh, A.H.4    Ball, A.L.5
  • 20
    • 0036776532 scopus 로고    scopus 로고
    • Large-scale, pH-dependent, quaternary structure changes in an RNA virus capsid are reversible in the absence of subunit autoproteolysis
    • Taylor D.J., Canady M.A., Schneemann A., and Johnson J.E. Large-scale, pH-dependent, quaternary structure changes in an RNA virus capsid are reversible in the absence of subunit autoproteolysis. J. Virol. 76 (2002) 9972-9980
    • (2002) J. Virol. , vol.76 , pp. 9972-9980
    • Taylor, D.J.1    Canady, M.A.2    Schneemann, A.3    Johnson, J.E.4
  • 21
    • 0344099412 scopus 로고    scopus 로고
    • Correlation of chemical reactivity of Nudaurelia capensis ω virus with a pH-induced conformational change
    • Taylor D.J., Wang Q., Bothner B., Natarajan P., Finn M.G., and Johnson J.E. Correlation of chemical reactivity of Nudaurelia capensis ω virus with a pH-induced conformational change. Chem. Commun. (Camb.) 22 (2003) 2770-2771
    • (2003) Chem. Commun. (Camb.) , vol.22 , pp. 2770-2771
    • Taylor, D.J.1    Wang, Q.2    Bothner, B.3    Natarajan, P.4    Finn, M.G.5    Johnson, J.E.6
  • 22
    • 13244259151 scopus 로고    scopus 로고
    • Folding and particle assembly are disrupted by single point mutations near the autocatalytic cleavage site of Nudaurelia capensis ω virus capsid protein
    • Taylor D.J., and Johnson J.E. Folding and particle assembly are disrupted by single point mutations near the autocatalytic cleavage site of Nudaurelia capensis ω virus capsid protein. Prot. Sci. 14 (2005) 401-408
    • (2005) Prot. Sci. , vol.14 , pp. 401-408
    • Taylor, D.J.1    Johnson, J.E.2
  • 23
    • 0037255597 scopus 로고    scopus 로고
    • Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems
    • Terpe K. Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems. Appl. Microbiol. Biotechnol. 60 (2003) 523-533
    • (2003) Appl. Microbiol. Biotechnol. , vol.60 , pp. 523-533
    • Terpe, K.1
  • 24
    • 0011127735 scopus 로고
    • Negative staining electron microscopy of protein at pH below their isoelectric points: its application to hemocyanin
    • Van Bruggen E.F.S., Wiebenger E.H., and Gruber M. Negative staining electron microscopy of protein at pH below their isoelectric points: its application to hemocyanin. Biochim. Biophys. Acta 42 (1960) 171-172
    • (1960) Biochim. Biophys. Acta , vol.42 , pp. 171-172
    • Van Bruggen, E.F.S.1    Wiebenger, E.H.2    Gruber, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.