메뉴 건너뛰기




Volumn 309, Issue 3, 2003, Pages 672-678

Blocking the dengue virus 2 infections on BHK-21 cells with purified recombinant dengue virus 2 E protein expressed in Escherichia coli

Author keywords

Dengue virus; Envelope (E) protein expression; Functional assay; In vivo expression tag

Indexed keywords

RECOMBINANT PROTEIN; VIRUS ENVELOPE PROTEIN;

EID: 0041328862     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2003.08.053     Document Type: Article
Times cited : (25)

References (22)
  • 1
    • 0035051804 scopus 로고    scopus 로고
    • Mutational evidence for an internal fusion peptide in flavivirus envelope protein E
    • Allison S.L., Schalich J., Stiasny K., Mandl C.W., Heinz F.X. Mutational evidence for an internal fusion peptide in flavivirus envelope protein E. J. Virol. 75:2001;4268-4275.
    • (2001) J. Virol. , vol.75 , pp. 4268-4275
    • Allison, S.L.1    Schalich, J.2    Stiasny, K.3    Mandl, C.W.4    Heinz, F.X.5
  • 3
    • 0000445568 scopus 로고    scopus 로고
    • Molecular biology of dengue viruses
    • D.J. Gubler, & G. Kuno. New York, NY: CAB International
    • Chang G.J. Molecular biology of dengue viruses. Gubler D.J., Kuno G. Dengue and Dengue Hemorrhagic Fever. 1997;175-198 CAB International, New York, NY. Crill W.D., Roehrig J.T. Monoclonal antibodies that bind to domain III of dengue virus E glycoprotein are the most efficient blockers of virus adsorption to Vero cells. J. Virol. 75:2001;7769-7773.
    • (1997) Dengue and Dengue Hemorrhagic Fever , pp. 175-198
    • Chang, G.J.1
  • 4
    • 0034899311 scopus 로고    scopus 로고
    • Monoclonal antibodies that bind to domain III of dengue virus E glycoprotein are the most efficient blockers of virus adsorption to Vero cells
    • Crill W.D., Roehrig J.T. Monoclonal antibodies that bind to domain III of dengue virus E glycoprotein are the most efficient blockers of virus adsorption to Vero cells. J. Virol. 75:2001;7769-7773. Delenda C., Staropoli I., Frenkiel M.P., Cabanie L., Deubel V. Analysis of C-terminally truncated dengue 2 and dengue 3 virus envelope glycoproteins: processing in insect cells and immunogenic properties in mice. J. Gen. Virol. 75:1994;1569-1578.
    • (2001) J. Virol. , vol.75 , pp. 7769-7773
    • Crill, W.D.1    Roehrig, J.T.2
  • 5
    • 0028302115 scopus 로고
    • Analysis of C-terminally truncated dengue 2 and dengue 3 virus envelope glycoproteins: Processing in insect cells and immunogenic properties in mice
    • Delenda C., Staropoli I., Frenkiel M.P., Cabanie L., Deubel V. Analysis of C-terminally truncated dengue 2 and dengue 3 virus envelope glycoproteins: processing in insect cells and immunogenic properties in mice. J. Gen. Virol. 75:1994;1569-1578.
    • (1994) J. Gen. Virol. , vol.75 , pp. 1569-1578
    • Delenda, C.1    Staropoli, I.2    Frenkiel, M.P.3    Cabanie, L.4    Deubel, V.5
  • 6
    • 0003075995 scopus 로고    scopus 로고
    • Clinical spectrum of dengue infection
    • D.J. Gubler, & G. Kuno. New York, NY: CAB International
    • George R., Lum L.C.S. Clinical spectrum of dengue infection. Gubler D.J., Kuno G. Dengue and Dengue Hemorrhagic Fever. 1997;23-44 CAB International, New York, NY.
    • (1997) Dengue and Dengue Hemorrhagic Fever , pp. 23-44
    • George, R.1    Lum, L.C.S.2
  • 7
    • 0002540391 scopus 로고    scopus 로고
    • Dengue and dengue hemorrhagic fever: Its history and resurgence as a global public health problem
    • D.J. Gubler. New York, NY: CAB International
    • Gubler D.J. Dengue and dengue hemorrhagic fever: its history and resurgence as a global public health problem. Gubler D.J. Dengue and Dengue Hemorrhagic Fever. 1997;1-22 CAB International, New York, NY.
    • (1997) Dengue and Dengue Hemorrhagic Fever , pp. 1-22
    • Gubler, D.J.1
  • 8
    • 0034623662 scopus 로고    scopus 로고
    • Recombinant plasmid expressing a truncated dengue-2 virus E protein without co-expression of prM protein induces partial protection in mice
    • Jimenez R.O., da Fonseca B.A.L. Recombinant plasmid expressing a truncated dengue-2 virus E protein without co-expression of prM protein induces partial protection in mice. Vaccine. 19:2001;648-654.
    • (2001) Vaccine , vol.19 , pp. 648-654
    • Jimenez, R.O.1    Da Fonseca, B.A.L.2
  • 9
    • 0034702096 scopus 로고    scopus 로고
    • Purified dengue 2 virus envelope glycoprotein aggregates produced by baculovirus are immunogenic in mice
    • Kelly E.P., Greene J.J., King A.D., Innis B.L. Purified dengue 2 virus envelope glycoprotein aggregates produced by baculovirus are immunogenic in mice. Vaccine. 18:2000;2549-2559. Lee E., Lobigs M. Substitutions at the putative receptor-binding site of an encephalitic flavivirus alter virulence and host cell tropism and reveal a role for glycosaminoglycans in entry. J. Virol. 74:2000;8867-8875.
    • (2000) Vaccine , vol.18 , pp. 2549-2559
    • Kelly, E.P.1    Greene, J.J.2    King, A.D.3    Innis, B.L.4
  • 10
    • 0033804366 scopus 로고    scopus 로고
    • Substitutions at the putative receptor-binding site of an encephalitic flavivirus alter virulence and host cell tropism and reveal a role for glycosaminoglycans in entry
    • Lee E., Lobigs M. Substitutions at the putative receptor-binding site of an encephalitic flavivirus alter virulence and host cell tropism and reveal a role for glycosaminoglycans in entry. J. Virol. 74:2000;8867-8875.
    • (2000) J. Virol. , vol.74 , pp. 8867-8875
    • Lee, E.1    Lobigs, M.2
  • 11
    • 0033982257 scopus 로고    scopus 로고
    • Perspectives for the treatment of infections with Flaviviridae
    • table
    • Leyssen P., De Clercq E., Neyts J. Perspectives for the treatment of infections with Flaviviridae. Clin. Microbiol. Rev. 13:2000;67-82. table.
    • (2000) Clin. Microbiol. Rev. , vol.13 , pp. 67-82
    • Leyssen, P.1    De Clercq, E.2    Neyts, J.3
  • 12
    • 0025031982 scopus 로고
    • The antigenic structure of dengue type 1 virus envelope and NS1 proteins expressed in Escherichia coli
    • Mason P.W., Zugel M.U., Semproni A.R., Fournier M.J., Mason T.L. The antigenic structure of dengue type 1 virus envelope and NS1 proteins expressed in Escherichia coli. J. Gen. Virol. 71:1990;2107-2114.
    • (1990) J. Gen. Virol. , vol.71 , pp. 2107-2114
    • Mason, P.W.1    Zugel, M.U.2    Semproni, A.R.3    Fournier, M.J.4    Mason, T.L.5
  • 13
    • 0037495036 scopus 로고    scopus 로고
    • A ligand-binding pocket in the dengue virus envelope glycoprotein
    • Modis Y., Ogata S., Clements D., Harrison S.C. A ligand-binding pocket in the dengue virus envelope glycoprotein. Proc. Natl. Acad. Sci. USA. 100:2003;6986-6991. Monath T.P., Henize F.X. Flaviviruses. third ed. Fields B.N., Knipe D.M., Howley P.M. Fields Virology. vol. 1:1996;961-1034 Lipponcott-Raven Publishers, Philadelphia, PA.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 6986-6991
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 14
    • 0001925194 scopus 로고    scopus 로고
    • Flaviviruses
    • third ed. B.N. Fields, D.M. Knipe, Howley P.M. Philadelphia, PA: Lipponcott-Raven Publishers
    • Monath T.P., Henize F.X. Flaviviruses. third ed. Fields B.N., Knipe D.M., Howley P.M. Fields Virology. vol. 1:1996;961-1034 Lipponcott-Raven Publishers, Philadelphia, PA.
    • (1996) Fields Virology , vol.1 , pp. 961-1034
    • Monath, T.P.1    Henize, F.X.2
  • 15
    • 0029014434 scopus 로고
    • The envelope glycoprotein from tick-borne encephalitis virus at 2 Å resolution
    • Rey F.A., Heinz F.X., Mandl C., Kunz C., Harrison S.C. The envelope glycoprotein from tick-borne encephalitis virus at 2. Å resolution Nature. 375:1995;291-298.
    • (1995) Nature , vol.375 , pp. 291-298
    • Rey, F.A.1    Heinz, F.X.2    Mandl, C.3    Kunz, C.4    Harrison, S.C.5
  • 16
    • 0032486594 scopus 로고    scopus 로고
    • Monoclonal antibody mapping of the envelope glycoprotein of the dengue 2 virus, Jamaica
    • Roehrig J.T., Bolin R.A., Kelly R.G. Monoclonal antibody mapping of the envelope glycoprotein of the dengue 2 virus, Jamaica. Virology. 246:1998;317-328.
    • (1998) Virology , vol.246 , pp. 317-328
    • Roehrig, J.T.1    Bolin, R.A.2    Kelly, R.G.3
  • 17
    • 0343831399 scopus 로고    scopus 로고
    • Dengue virus envelope glycoprotein can be secreted from insect cells as a fusion with the maltose-binding protein
    • Staropoli I., Clement J.M., Frenkiel M.P., Hofnung M., Deubel V. Dengue virus envelope glycoprotein can be secreted from insect cells as a fusion with the maltose-binding protein. J. Virol. Methods. 56:1996;179-189.
    • (1996) J. Virol. Methods , vol.56 , pp. 179-189
    • Staropoli, I.1    Clement, J.M.2    Frenkiel, M.P.3    Hofnung, M.4    Deubel, V.5
  • 18
    • 0030846892 scopus 로고    scopus 로고
    • Affinity-purified dengue-2 virus envelope glycoprotein induces neutralizing antibodies and protective immunity in mice
    • Staropoli I., Frenkiel M.P., Megret F., Deubel V. Affinity-purified dengue-2 virus envelope glycoprotein induces neutralizing antibodies and protective immunity in mice. Vaccine. 15:1997;1946-1954. Sugrue R.J., Cui T., Xu Q., Fu J., Chan Y.C. The production of recombinant dengue virus E protein using Escherichia coli and Pichia pastoris. J. Virol. Methods. 69:1997;159-169.
    • (1997) Vaccine , vol.15 , pp. 1946-1954
    • Staropoli, I.1    Frenkiel, M.P.2    Megret, F.3    Deubel, V.4
  • 19
    • 0031471296 scopus 로고    scopus 로고
    • The production of recombinant dengue virus E protein using Escherichia coli and Pichia pastoris
    • Sugrue R.J., Cui T., Xu Q., Fu J., Chan Y.C. The production of recombinant dengue virus E protein using Escherichia coli and Pichia pastoris. J. Virol. Methods. 69:1997;159-169.
    • (1997) J. Virol. Methods , vol.69 , pp. 159-169
    • Sugrue, R.J.1    Cui, T.2    Xu, Q.3    Fu, J.4    Chan, Y.C.5
  • 20
    • 0034909177 scopus 로고    scopus 로고
    • Mapping of a dengue virus neutralizing epitope critical for the infectivity of all serotypes: Insight into the neutralization mechanism
    • Thullier P., Demangel C., Bedouelle H., Megret F., Jouan A., Deubel V.et al. Mapping of a dengue virus neutralizing epitope critical for the infectivity of all serotypes: insight into the neutralization mechanism. J. Gen. Virol. 82:2001;1885-1892.
    • (2001) J. Gen. Virol. , vol.82 , pp. 1885-1892
    • Thullier, P.1    Demangel, C.2    Bedouelle, H.3    Megret, F.4    Jouan, A.5    Deubel, V.6
  • 22
    • 0037377629 scopus 로고    scopus 로고
    • Secreted expression of dengue virus type 2 full-length envelope glycoprotein in Pichia pastoris
    • Wei H.Y., Jiang L.F., Xue Y.H., Fang D.Y., Guo H.Y. Secreted expression of dengue virus type 2 full-length envelope glycoprotein in Pichia pastoris. J. Virol. Methods. 109:2003;17-23.
    • (2003) J. Virol. Methods , vol.109 , pp. 17-23
    • Wei, H.Y.1    Jiang, L.F.2    Xue, Y.H.3    Fang, D.Y.4    Guo, H.Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.