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Volumn 392, Issue 1, 2009, Pages 103-113

Dengue virus neutralization by human immune sera: Role of envelope protein domain III-reactive antibody

Author keywords

Antibody; Dengue; Flavivirus; Human immune serum; Recombinant viral protein; Virus neutralization

Indexed keywords

ANTISERUM; CROSS REACTING ANTIBODY; EPITOPE; MONOCLONAL ANTIBODY; UNCLASSIFIED DRUG; VIRUS ANTIBODY; VIRUS ENVELOPE DOMAIN PROTEIN III; VIRUS ENVELOPE PROTEIN;

EID: 69249213373     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2009.06.037     Document Type: Article
Times cited : (230)

References (38)
  • 1
    • 48649102965 scopus 로고    scopus 로고
    • Immunogenicity of a recombinant envelope domain III protein of dengue virus type-4 with various adjuvants in mice
    • Babu J.P., Pattnaik P., Gupta N., Shrivastava A., Khan M., and Rao P.V. Immunogenicity of a recombinant envelope domain III protein of dengue virus type-4 with various adjuvants in mice. Vaccine 26 36 (2008) 4655-4663
    • (2008) Vaccine , vol.26 , Issue.36 , pp. 4655-4663
    • Babu, J.P.1    Pattnaik, P.2    Gupta, N.3    Shrivastava, A.4    Khan, M.5    Rao, P.V.6
  • 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
    • 10.1128/JVI.75.16.7769-7773.2001
    • Crill W.D., and 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 16 (2001) 7769-7773 10.1128/JVI.75.16.7769-7773.2001
    • (2001) J. Virol. , vol.75 , Issue.16 , pp. 7769-7773
    • Crill, W.D.1    Roehrig, J.T.2
  • 5
    • 64249106079 scopus 로고    scopus 로고
    • Humoral immune responses of dengue fever patients using epitope-specific serotype-2 virus-like particle antigens
    • Crill W.D., Hughes H.R., Delorey M.J., and Chang G.J. Humoral immune responses of dengue fever patients using epitope-specific serotype-2 virus-like particle antigens. PLoS ONE 4 4 (2009) e4991
    • (2009) PLoS ONE , vol.4 , Issue.4
    • Crill, W.D.1    Hughes, H.R.2    Delorey, M.J.3    Chang, G.J.4
  • 6
    • 34447134784 scopus 로고    scopus 로고
    • Dengue vaccines approach the finish line
    • Edelman R. Dengue vaccines approach the finish line. Clin. Infect. Dis. 45 Suppl. 1 (2007) S56-60
    • (2007) Clin. Infect. Dis. , vol.45 , Issue.SUPPL. 1
    • Edelman, R.1
  • 7
    • 51949088329 scopus 로고    scopus 로고
    • An envelope domain III-based chimeric antigen produced in Pichia pastoris elicits neutralizing antibodies against all four dengue virus serotypes
    • Etemad B., Batra G., Raut R., Dahiya S., Khanam S., Swaminathan S., and Khanna N. An envelope domain III-based chimeric antigen produced in Pichia pastoris elicits neutralizing antibodies against all four dengue virus serotypes. Am. J. Trop. Med. Hyg. 79 3 (2008) 353-363
    • (2008) Am. J. Trop. Med. Hyg. , vol.79 , Issue.3 , pp. 353-363
    • Etemad, B.1    Batra, G.2    Raut, R.3    Dahiya, S.4    Khanam, S.5    Swaminathan, S.6    Khanna, N.7
  • 8
    • 8644261541 scopus 로고    scopus 로고
    • Chimpanzee Fab fragments and a derived humanized immunoglobulin G1 antibody that efficiently cross-neutralize dengue type 1 and type 2 viruses
    • Goncalvez A.P., Men R., Wernly C., Purcell R.H., and Lai C.J. Chimpanzee Fab fragments and a derived humanized immunoglobulin G1 antibody that efficiently cross-neutralize dengue type 1 and type 2 viruses. J. Virol. 78 23 (2004) 12910-12918
    • (2004) J. Virol. , vol.78 , Issue.23 , pp. 12910-12918
    • Goncalvez, A.P.1    Men, R.2    Wernly, C.3    Purcell, R.H.4    Lai, C.J.5
  • 9
    • 34548627957 scopus 로고    scopus 로고
    • Characterization of an antigenic site that contains a dominant, type-specific neutralization determinant on the envelope protein domain III (ED3) of dengue 2 virus
    • Gromowski G.D., and Barrett A.D. Characterization of an antigenic site that contains a dominant, type-specific neutralization determinant on the envelope protein domain III (ED3) of dengue 2 virus. Virology 366 (2007) 349-360
    • (2007) Virology , vol.366 , pp. 349-360
    • Gromowski, G.D.1    Barrett, A.D.2
  • 10
    • 50149096815 scopus 로고    scopus 로고
    • Characterization of dengue virus complex-specific neutralizing epitopes on envelope protein domain III of dengue 2 virus
    • Gromowski G.D., Barrett N.D., and Barrett A.D. Characterization of dengue virus complex-specific neutralizing epitopes on envelope protein domain III of dengue 2 virus. J. Virol. 82 17 (2008) 8828-8837
    • (2008) J. Virol. , vol.82 , Issue.17 , pp. 8828-8837
    • Gromowski, G.D.1    Barrett, N.D.2    Barrett, A.D.3
  • 12
    • 0642287817 scopus 로고    scopus 로고
    • Neutralization and antibody-dependent enhancement of dengue viruses
    • Halstead S.B. Neutralization and antibody-dependent enhancement of dengue viruses. Adv. Virus Res. 60 (2003) 421-467
    • (2003) Adv. Virus Res. , vol.60 , pp. 421-467
    • Halstead, S.B.1
  • 13
    • 37349119683 scopus 로고    scopus 로고
    • Single antigen detects both immunoglobulin M (IgM) and IgG antibodies elicited by all four dengue virus serotypes
    • Hapugoda M.D., Batra G., Abeyewickreme W., Swaminathan S., and Khanna N. Single antigen detects both immunoglobulin M (IgM) and IgG antibodies elicited by all four dengue virus serotypes. Clin. Vaccine Immunol. 14 11 (2007) 1505-1514
    • (2007) Clin. Vaccine Immunol. , vol.14 , Issue.11 , pp. 1505-1514
    • Hapugoda, M.D.1    Batra, G.2    Abeyewickreme, W.3    Swaminathan, S.4    Khanna, N.5
  • 14
    • 0021998750 scopus 로고
    • Epitopic Analysis of antigenic determinants on the surface of dengue-2 virions using monoclonal antibodies
    • Henchal E.A., McCown J.M., Burke D.S., Seguin M.C., and Brandt W.E. Epitopic Analysis of antigenic determinants on the surface of dengue-2 virions using monoclonal antibodies. Am. J. Trop. Med. Hyg. 34 1 (1985) 162-169
    • (1985) Am. J. Trop. Med. Hyg. , vol.34 , Issue.1 , pp. 162-169
    • Henchal, E.A.1    McCown, J.M.2    Burke, D.S.3    Seguin, M.C.4    Brandt, W.E.5
  • 15
    • 4644327330 scopus 로고    scopus 로고
    • Use of recombinant E protein domain III-based enzyme-linked immunosorbent assays for differentiation of tick-borne encephalitis serocomplex flaviviruses from mosquito-borne flaviviruses
    • Holbrook M.R., Shope R.E., and Barrett A.D. Use of recombinant E protein domain III-based enzyme-linked immunosorbent assays for differentiation of tick-borne encephalitis serocomplex flaviviruses from mosquito-borne flaviviruses. J. Clin. Microbiol. 42 9 (2004) 4101-4110
    • (2004) J. Clin. Microbiol. , vol.42 , Issue.9 , pp. 4101-4110
    • Holbrook, M.R.1    Shope, R.E.2    Barrett, A.D.3
  • 16
    • 36349025968 scopus 로고    scopus 로고
    • Comparison of plaque- and flow cytometry-based methods for measuring dengue virus neutralization
    • Kraus A.A., Messer W., Haymore L.B., and de Silva A.M. Comparison of plaque- and flow cytometry-based methods for measuring dengue virus neutralization. J. Clin. Microbiol. 45 (2007) 3777-3780
    • (2007) J. Clin. Microbiol. , vol.45 , pp. 3777-3780
    • Kraus, A.A.1    Messer, W.2    Haymore, L.B.3    de Silva, A.M.4
  • 17
    • 45749131789 scopus 로고    scopus 로고
    • Antibodies to envelope glycoprotein of dengue virus during the natural course of infection are predominantly cross-reactive and recognize epitopes containing highly conserved residues at the fusion loop of domain II
    • Lai C.Y., Tsai W.Y., Lin S.R., Kao C.L., Hu H.P., King C.C., Wu H.C., Chang G.J., and Wang W.K. Antibodies to envelope glycoprotein of dengue virus during the natural course of infection are predominantly cross-reactive and recognize epitopes containing highly conserved residues at the fusion loop of domain II. J. Virol. 82 13 (2008) 6631-6643
    • (2008) J. Virol. , vol.82 , Issue.13 , pp. 6631-6643
    • Lai, C.Y.1    Tsai, W.Y.2    Lin, S.R.3    Kao, C.L.4    Hu, H.P.5    King, C.C.6    Wu, H.C.7    Chang, G.J.8    Wang, W.K.9
  • 18
    • 0028059533 scopus 로고
    • Localization of a neutralizing epitope on the envelope protein of dengue virus type 2
    • Lin B., Parrish C.R., Murray J.M., and Wright P.J. Localization of a neutralizing epitope on the envelope protein of dengue virus type 2. Virology 202 2 (1994) 885-890
    • (1994) Virology , vol.202 , Issue.2 , pp. 885-890
    • Lin, B.1    Parrish, C.R.2    Murray, J.M.3    Wright, P.J.4
  • 20
    • 0036841969 scopus 로고    scopus 로고
    • Serological differentiation of infections with dengue virus serotypes 1 to 4 by using recombinant antigens
    • Ludolfs D., Schilling S., Altenschmidt J., and Schmitz H. Serological differentiation of infections with dengue virus serotypes 1 to 4 by using recombinant antigens. J. Clin. Microbiol. 40 11 (2002) 4317-4320
    • (2002) J. Clin. Microbiol. , vol.40 , Issue.11 , pp. 4317-4320
    • Ludolfs, D.1    Schilling, S.2    Altenschmidt, J.3    Schmitz, H.4
  • 21
    • 38049123828 scopus 로고    scopus 로고
    • Long range communication in the envelope protein domain III and its effect on the resistance of West Nile virus to antibody-mediated neutralization
    • Maillard R.A., Jordan M., Beasley D.W., Barrett A.D., and Lee J.C. Long range communication in the envelope protein domain III and its effect on the resistance of West Nile virus to antibody-mediated neutralization. J. Biol. Chem. 283 1 (2008) 613-622
    • (2008) J. Biol. Chem. , vol.283 , Issue.1 , pp. 613-622
    • Maillard, R.A.1    Jordan, M.2    Beasley, D.W.3    Barrett, A.D.4    Lee, J.C.5
  • 23
    • 11144244755 scopus 로고    scopus 로고
    • Variable surface epitopes in the crystal structure of dengue virus type 3 envelope glycoprotein
    • Modis Y., Ogata S., Clements D., and Harrison S.C. Variable surface epitopes in the crystal structure of dengue virus type 3 envelope glycoprotein. J. Virol. 79 2 (2005) 1223-1231
    • (2005) J. Virol. , vol.79 , Issue.2 , pp. 1223-1231
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 24
    • 26944454471 scopus 로고    scopus 로고
    • Structural basis of West Nile virus neutralization by a therapeutic antibody
    • Nybakken G.E., Oliphant T., Johnson S., Burke S., Diamond M.S., and Fremont D.H. Structural basis of West Nile virus neutralization by a therapeutic antibody. Nature 437 7059 (2005) 764-769
    • (2005) Nature , vol.437 , Issue.7059 , pp. 764-769
    • Nybakken, G.E.1    Oliphant, T.2    Johnson, S.3    Burke, S.4    Diamond, M.S.5    Fremont, D.H.6
  • 27
    • 0029014434 scopus 로고
    • The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution
    • Rey F.A., Heinz F.X., Mandl C., Kunz C., and Harrison S.C. The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution. Nature 375 6529 (1995) 291-298
    • (1995) Nature , vol.375 , Issue.6529 , pp. 291-298
    • Rey, F.A.1    Heinz, F.X.2    Mandl, C.3    Kunz, C.4    Harrison, S.C.5
  • 28
    • 1542466883 scopus 로고    scopus 로고
    • Antigenic structure of flavivirus proteins
    • Roehrig J.T. Antigenic structure of flavivirus proteins. Adv. Virus Res. 59 (2003) 141-175
    • (2003) Adv. Virus Res. , vol.59 , pp. 141-175
    • Roehrig, J.T.1
  • 29
    • 0032486594 scopus 로고    scopus 로고
    • Monoclonal antibody mapping of the envelope glycoprotein of the dengue 2 virus, Jamaica
    • Roehrig J.T., Bolin R.A., and Kelly R.G. Monoclonal antibody mapping of the envelope glycoprotein of the dengue 2 virus, Jamaica. Virology 246 2 (1998) 317-328
    • (1998) Virology , vol.246 , Issue.2 , pp. 317-328
    • Roehrig, J.T.1    Bolin, R.A.2    Kelly, R.G.3
  • 30
    • 2142827156 scopus 로고    scopus 로고
    • Dengue: defining protective versus pathologic immunity
    • Rothman A.L. Dengue: defining protective versus pathologic immunity. J. Clin. Invest. 113 7 (2004) 946-951
    • (2004) J. Clin. Invest. , vol.113 , Issue.7 , pp. 946-951
    • Rothman, A.L.1
  • 32
    • 0023128744 scopus 로고
    • Protection of mice against dengue 2 virus encephalitis by immunization with the dengue 2 virus non-structural glycoprotein NS1
    • Schlesinger J.J., Brandriss M.W., and Walsh E.E. Protection of mice against dengue 2 virus encephalitis by immunization with the dengue 2 virus non-structural glycoprotein NS1. J. Gen. Virol. 68 Pt 3 (1987) 853-857
    • (1987) J. Gen. Virol. , vol.68 , Issue.PART 3 , pp. 853-857
    • Schlesinger, J.J.1    Brandriss, M.W.2    Walsh, E.E.3
  • 33
    • 0035558433 scopus 로고    scopus 로고
    • Identification of epitopes on the envelope (E) protein of dengue 2 and dengue 3 viruses using monoclonal antibodies
    • Serafin I.L., and Aaskov J.G. Identification of epitopes on the envelope (E) protein of dengue 2 and dengue 3 viruses using monoclonal antibodies. Arch. Virol. 146 12 (2001) 2469-2479
    • (2001) Arch. Virol. , vol.146 , Issue.12 , pp. 2469-2479
    • Serafin, I.L.1    Aaskov, J.G.2
  • 36
    • 4644372800 scopus 로고    scopus 로고
    • Solution structure and antibody binding studies of the envelope protein domain III from the New York strain of West Nile virus
    • Volk D.E., Beasley D.W., Kallick D.A., Holbrook M.R., Barrett A.D., and Gorenstein D.G. Solution structure and antibody binding studies of the envelope protein domain III from the New York strain of West Nile virus. J. Biol. Chem. 279 37 (2004) 38755-38761
    • (2004) J. Biol. Chem. , vol.279 , Issue.37 , pp. 38755-38761
    • Volk, D.E.1    Beasley, D.W.2    Kallick, D.A.3    Holbrook, M.R.4    Barrett, A.D.5    Gorenstein, D.G.6
  • 38
    • 3142777804 scopus 로고    scopus 로고
    • Solution structure and structural dynamics of envelope protein domain III of mosquito- and tick-borne flaviviruses
    • Yu S., Wuu A., Basu R., Holbrook M.R., Barrett A.D., and Lee J.C. Solution structure and structural dynamics of envelope protein domain III of mosquito- and tick-borne flaviviruses. Biochemistry 43 28 (2004) 9168-9176
    • (2004) Biochemistry , vol.43 , Issue.28 , pp. 9168-9176
    • Yu, S.1    Wuu, A.2    Basu, R.3    Holbrook, M.R.4    Barrett, A.D.5    Lee, J.C.6


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