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Volumn 121, Issue 1, 2006, Pages 65-73

Amino acid changes in the recombinant Dengue 3 Envelope domain III determine its antigenicity and immunogenicity in mice

Author keywords

Dengue; Domain B; Domain III; Envelope; P64k; Viral strain

Indexed keywords

DENGUE VACCINE; PD 18; PD 9; UNCLASSIFIED DRUG; VIRUS FUSION PROTEIN; VIRUS FUSION PROTEIN PD18; VIRUS FUSION PROTEIN PD9;

EID: 33745899363     PISSN: 01681702     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.virusres.2006.04.003     Document Type: Article
Times cited : (35)

References (45)
  • 1
    • 0036891872 scopus 로고    scopus 로고
    • Identification of neutralizing epitopes within structural domain III of the West Nile virus envelope protein
    • Beasley D.W.C., and Barrett A.D.T. Identification of neutralizing epitopes within structural domain III of the West Nile virus envelope protein. J. Virol. 76 (2002) 13097-13100
    • (2002) J. Virol. , vol.76 , pp. 13097-13100
    • Beasley, D.W.C.1    Barrett, A.D.T.2
  • 2
    • 0024411870 scopus 로고
    • Protein measurement using bicinchoninic acid: elimination of interfering substances
    • Brown R., Jarvis K., and Hyland K. Protein measurement using bicinchoninic acid: elimination of interfering substances. Ann. Biochem. 180 (1989) 136-139
    • (1989) Ann. Biochem. , vol.180 , pp. 136-139
    • Brown, R.1    Jarvis, K.2    Hyland, K.3
  • 3
    • 0000182975 scopus 로고
    • A high efficiency plasmid transforming recA Escherichia coli strain with Beta-Galactosidase selection
    • Bullock W.O., Fernández J.M., and Short J.M. A high efficiency plasmid transforming recA Escherichia coli strain with Beta-Galactosidase selection. Biotechniques 4 (1987) 376-378
    • (1987) Biotechniques , vol.4 , pp. 376-378
    • Bullock, W.O.1    Fernández, J.M.2    Short, J.M.3
  • 4
    • 0029911394 scopus 로고    scopus 로고
    • Demonstration of binding of dengue virus envelope protein to target cells
    • Chen Y., Maguire T., and Marks R.M. Demonstration of binding of dengue virus envelope protein to target cells. J. Virol. 70 (1996) 8765-8772
    • (1996) J. Virol. , vol.70 , pp. 8765-8772
    • Chen, Y.1    Maguire, T.2    Marks, R.M.3
  • 5
    • 0028863047 scopus 로고
    • The use of position-specific rotamers in model building by homology
    • Chinea G., Padron G., Hooft R.W., Sander C., and Vriend G. The use of position-specific rotamers in model building by homology. Proteins 23 (1995) 415-421
    • (1995) Proteins , vol.23 , pp. 415-421
    • Chinea, G.1    Padron, G.2    Hooft, R.W.3    Sander, C.4    Vriend, G.5
  • 6
    • 70449217974 scopus 로고
    • Techniques for hemagglutination and hemagglutination-inhibition with arthropod borne virus
    • Clarke D.H., and Casals J. Techniques for hemagglutination and hemagglutination-inhibition with arthropod borne virus. Am. J. Trop. Med. Hyg. 7 (1958) 561-573
    • (1958) Am. J. Trop. Med. Hyg. , vol.7 , pp. 561-573
    • Clarke, D.H.1    Casals, J.2
  • 7
    • 0037378525 scopus 로고    scopus 로고
    • American genotype structures decrease dengue virus output from human monocytes and dendritic cells
    • Cologna R., and Rico-Hesse R. American genotype structures decrease dengue virus output from human monocytes and dendritic cells. J. Virol. 77 (2003) 3929-3938
    • (2003) J. Virol. , vol.77 , pp. 3929-3938
    • Cologna, R.1    Rico-Hesse, R.2
  • 10
    • 0344196871 scopus 로고    scopus 로고
    • A dengue-2 Envelope fragment inserted within the structure of the P64k meningococcal protein carrier enables a functional immune response against the virus in mice
    • Hermida L., Rodríguez R., Lazo L., Silva R., Zulueta A., Chinea G., López C., Guzmán M.G., and Guillén G. A dengue-2 Envelope fragment inserted within the structure of the P64k meningococcal protein carrier enables a functional immune response against the virus in mice. J. Virol. Methods 115 (2004) 41-49
    • (2004) J. Virol. Methods , vol.115 , pp. 41-49
    • Hermida, L.1    Rodríguez, R.2    Lazo, L.3    Silva, R.4    Zulueta, A.5    Chinea, G.6    López, C.7    Guzmán, M.G.8    Guillén, G.9
  • 11
    • 0030588217 scopus 로고    scopus 로고
    • Analysis of a neutralization epitope on the dengue type 2 virus (DEN2) envelope protein: monoclonal antibody resistant DEN2/DEN4 chimeras exhibit reduced mouse neurovirulence
    • Hiramatsu K., Tadano M., Men R., and Lai C.J. Analysis of a neutralization epitope on the dengue type 2 virus (DEN2) envelope protein: monoclonal antibody resistant DEN2/DEN4 chimeras exhibit reduced mouse neurovirulence. Virology 224 (1996) 437-445
    • (1996) Virology , vol.224 , pp. 437-445
    • Hiramatsu, K.1    Tadano, M.2    Men, R.3    Lai, C.J.4
  • 12
    • 0025012148 scopus 로고
    • A single amino acid substitution in envelope protein E of tick-borne encephalitis virus leads to attenuation in the mouse model
    • Holzmann H., Heinz F.X., Mandl C.W., Guirakhoo F., and Kunz C. A single amino acid substitution in envelope protein E of tick-borne encephalitis virus leads to attenuation in the mouse model. J. Virol. 64 (1990) 5156-5159
    • (1990) J. Virol. , vol.64 , pp. 5156-5159
    • Holzmann, H.1    Heinz, F.X.2    Mandl, C.W.3    Guirakhoo, F.4    Kunz, C.5
  • 13
    • 0031014304 scopus 로고    scopus 로고
    • Characterization of monoclonal antibody-escape mutants of tick-borne encephalitis virus with reduced neuroinvasiveness in mice
    • Holzmann H., Stiasny K., Ecker M., Kunz C., and Heinz F.X. Characterization of monoclonal antibody-escape mutants of tick-borne encephalitis virus with reduced neuroinvasiveness in mice. J. Gen. Virol. 78 (1997) 31-37
    • (1997) J. Gen. Virol. , vol.78 , pp. 31-37
    • Holzmann, H.1    Stiasny, K.2    Ecker, M.3    Kunz, C.4    Heinz, F.X.5
  • 14
    • 0347626038 scopus 로고    scopus 로고
    • An external loop region of domain III of dengue virus type 2 envelope protein is involved in serotype-specific binding to mosquito but not mammalian cells
    • Hung J.J., Hsieh M.T., Young M.J., Kao C.L., King C.C., and Chang W. An external loop region of domain III of dengue virus type 2 envelope protein is involved in serotype-specific binding to mosquito but not mammalian cells. J. Virol. 78 (2004) 378-388
    • (2004) J. Virol. , vol.78 , pp. 378-388
    • Hung, J.J.1    Hsieh, M.T.2    Young, M.J.3    Kao, C.L.4    King, C.C.5    Chang, W.6
  • 15
    • 0028566270 scopus 로고
    • A revised set of potentials for beta-turn formation in proteins
    • Hutchinson E.G., and Thornton J.M. A revised set of potentials for beta-turn formation in proteins. Protein Sci. 3 (1994) 2207-2216
    • (1994) Protein Sci. , vol.3 , pp. 2207-2216
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 16
    • 0018160953 scopus 로고
    • Isolation of a Singh's Aedes albopictus cell clone sensitive to Dengue and Chikungunya viruses
    • Igarashi A. Isolation of a Singh's Aedes albopictus cell clone sensitive to Dengue and Chikungunya viruses. J. Gen. Virol. 40 (1978) 531-544
    • (1978) J. Gen. Virol. , vol.40 , pp. 531-544
    • Igarashi, A.1
  • 17
    • 0026675750 scopus 로고
    • High resolution functional analysis of antibody-antigen interactions
    • Jin L., Fendly B.M., and Wells J.A. High resolution functional analysis of antibody-antigen interactions. J. Mol. Biol. 226 (1992) 851-865
    • (1992) J. Mol. Biol. , vol.226 , pp. 851-865
    • Jin, L.1    Fendly, B.M.2    Wells, J.A.3
  • 19
    • 0017411721 scopus 로고
    • Complementary specificity of restriction endonucleases of Diplococcus pneumoniae with respect to DNA methylation
    • Lacks S., and Greenberg J.R. Complementary specificity of restriction endonucleases of Diplococcus pneumoniae with respect to DNA methylation. J. Mol. Biol. 114 (1977) 153-168
    • (1977) J. Mol. Biol. , vol.114 , pp. 153-168
    • Lacks, S.1    Greenberg, J.R.2
  • 20
    • 0014949207 scopus 로고
    • Protein measurement using bicinchoninic acid: elimination of interfering substances
    • Laemmli U.K. Protein measurement using bicinchoninic acid: elimination of interfering substances. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 16844382354 scopus 로고    scopus 로고
    • Differential expression of domain III neutralizing epitopes on the envelope proteins of West Nile virus strains
    • Li L., Barrett A.D.T., and Beasley D.W.C. Differential expression of domain III neutralizing epitopes on the envelope proteins of West Nile virus strains. Virology 335 (2005) 99-105
    • (2005) Virology , vol.335 , pp. 99-105
    • Li, L.1    Barrett, A.D.T.2    Beasley, D.W.C.3
  • 23
    • 0037323137 scopus 로고    scopus 로고
    • A functional determinant on Domain III of the Japanese Encephalitis virus envelope protein interacted with neutralizing-antibody combining sites
    • Lin C.W., and Wu S.C. A functional determinant on Domain III of the Japanese Encephalitis virus envelope protein interacted with neutralizing-antibody combining sites. J. Virol. 77 (2003) 2600-2606
    • (2003) J. Virol. , vol.77 , pp. 2600-2606
    • Lin, C.W.1    Wu, S.C.2
  • 24
    • 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. Microb. 40 (2002) 4317-4320
    • (2002) J. Clin. Microb. , vol.40 , pp. 4317-4320
    • Ludolfs, D.1    Schilling, S.2    Altenschmidt, J.3    Schmitz, H.4
  • 25
    • 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 (2005) 1223-1231
    • (2005) J. Virol. , vol.79 , pp. 1223-1231
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 26
    • 0001925194 scopus 로고    scopus 로고
    • Flaviviruses
    • Fields B.N., Knipe D.M., and Howley P.M. (Eds), Lippincott-Raven, Philadelphia, PA
    • Monath T.P., and Heinz F.X. Flaviviruses. In: Fields B.N., Knipe D.M., and Howley P.M. (Eds). Fields Virology. third ed. (1996), Lippincott-Raven, Philadelphia, PA
    • (1996) Fields Virology. third ed.
    • Monath, T.P.1    Heinz, F.X.2
  • 27
    • 0021795179 scopus 로고
    • Simplified plaque reduction neutralization assay for dengue viruses by semimicro methods in BHK-21 cells: comparison of the BHK suspension test with standard plaque reduction neutralization
    • Morens D.M., Halstead S.B., Repik P.M., Putvatana R., and Raybourne N. Simplified plaque reduction neutralization assay for dengue viruses by semimicro methods in BHK-21 cells: comparison of the BHK suspension test with standard plaque reduction neutralization. J. Clin. Microbiol. 22 (1985) 250-254
    • (1985) J. Clin. Microbiol. , vol.22 , pp. 250-254
    • Morens, D.M.1    Halstead, S.B.2    Repik, P.M.3    Putvatana, R.4    Raybourne, N.5
  • 28
  • 29
    • 0027156564 scopus 로고
    • Correlation between the location of antigenic sites and the prediction of turns in proteins
    • Pellequer J.L., Westhof E., and Van Regenmortel M.H. Correlation between the location of antigenic sites and the prediction of turns in proteins. Immunol. Lett. 36 (1993) 83-99
    • (1993) Immunol. Lett. , vol.36 , pp. 83-99
    • Pellequer, J.L.1    Westhof, E.2    Van Regenmortel, M.H.3
  • 31
    • 0029014434 scopus 로고
    • The envelope glycoprotein from tick-borne encephalitis virus at 2 Å resolution
    • Rey F.A., Heinz F.X., Mandl C.W.C., Kunz C., and 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.W.C.3    Kunz, C.4    Harrison, S.C.5
  • 33
    • 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
  • 34
    • 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 (1998) 317-328
    • (1998) Virology , vol.246 , pp. 317-328
    • Roehrig, J.T.1    Bolin, R.A.2    Kelly, R.G.3
  • 37
    • 0029993135 scopus 로고    scopus 로고
    • Replication of yellow fever virus in the mouse central nervous system: comparison of neuroadapted and nonneuroadapted virus and partial sequence analysis of the neuroadapted strain
    • Schlesinger J.J., Chapman S., Nestorowicz A., Rice C.M., Ginocchio T.E., and Chambers T.J. Replication of yellow fever virus in the mouse central nervous system: comparison of neuroadapted and nonneuroadapted virus and partial sequence analysis of the neuroadapted strain. J. Gen. Virol. 77 (1996) 1277-1285
    • (1996) J. Gen. Virol. , vol.77 , pp. 1277-1285
    • Schlesinger, J.J.1    Chapman, S.2    Nestorowicz, A.3    Rice, C.M.4    Ginocchio, T.E.5    Chambers, T.J.6
  • 38
    • 33745909595 scopus 로고    scopus 로고
    • Silva, R., Selmán, M., Guillén, G., Herrera, L., Fernández, J.R., Novoa, L.I., Morales, J., Morera, V., González, S., Tamargo, B., del Valle, J., Caballero, E., Álvarez, A., Coizeau, E., Cruz, S., Musacchio, A., 1992. Nucleotide sequence coding for an outer membrane protein from Neisseria meningitidis and use of said protein in vaccine preparations, European Patent Application EP 0474313 A2.
  • 39
    • 0031808680 scopus 로고    scopus 로고
    • Evaluation of the protective efficacy of a recombinant Dengue envelope B domain fusion protein against Dengue 2 virus infection in mice
    • Simmons M., Nelson W.M., Wu S.J., and Hayes C.G. Evaluation of the protective efficacy of a recombinant Dengue envelope B domain fusion protein against Dengue 2 virus infection in mice. Am. J. Trop. Med. Hyg. 58 (1998) 655-662
    • (1998) Am. J. Trop. Med. Hyg. , vol.58 , pp. 655-662
    • Simmons, M.1    Nelson, W.M.2    Wu, S.J.3    Hayes, C.G.4
  • 40
    • 0028784620 scopus 로고
    • Mice immunized with a Dengue type 2 virus E and NS1 fusion protein made in Escherichia coli are protected against lethal Dengue virus infection
    • Srivastava A.K., Putnak R.J., Warren R.L., and Hoke C.H. Mice immunized with a Dengue type 2 virus E and NS1 fusion protein made in Escherichia coli are protected against lethal Dengue virus infection. Vaccine 13 (1995) 1251-1258
    • (1995) Vaccine , vol.13 , pp. 1251-1258
    • Srivastava, A.K.1    Putnak, R.J.2    Warren, R.L.3    Hoke, C.H.4
  • 41
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and applications
    • Towbin H., Staehelin T., and Gordon H. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and applications. Proc. Natl. Acad. Sci. U.S.A. 76 (1979) 4350-4354
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, H.3
  • 42
    • 0025398721 scopus 로고
    • WHAT IF: a molecular modeling and drug design program
    • Vriend G. WHAT IF: a molecular modeling and drug design program. J. Mol. Graph. 8 (1990) 52-56
    • (1990) J. Mol. Graph. , vol.8 , pp. 52-56
    • Vriend, G.1
  • 44
    • 0023392056 scopus 로고
    • Characterization of a disulfide bridge-stabilized antigenic domain of tick-borne encephalitis virus structural glycoprotein
    • Winkler G., Heinz F.X., and Kunz C. Characterization of a disulfide bridge-stabilized antigenic domain of tick-borne encephalitis virus structural glycoprotein. J. Gen. Virol. 68 (1987) 2239-2244
    • (1987) J. Gen. Virol. , vol.68 , pp. 2239-2244
    • Winkler, G.1    Heinz, F.X.2    Kunz, C.3


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