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Volumn 403, Issue 1, 2010, Pages 85-91

Role of BC loop residues in structure, function and antigenicity of the West Nile virus envelope protein receptor-binding domain III

Author keywords

Attenuation; Envelope protein; Flavivirus; Neutralization; Receptor binding domain; West Nile virus

Indexed keywords

VIRUS ENVELOPE PROTEIN;

EID: 77953291917     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2010.03.038     Document Type: Article
Times cited : (25)

References (41)
  • 1
    • 0036891872 scopus 로고    scopus 로고
    • Identification of neutralizing epitopes within structural domain III of the West Nile virus envelope protein
    • Beasley D.W., Barrett A.D. Identification of neutralizing epitopes within structural domain III of the West Nile virus envelope protein. J. Virol. 2002, 76(24):13097-13100.
    • (2002) J. Virol. , vol.76 , Issue.24 , pp. 13097-13100
    • Beasley, D.W.1    Barrett, A.D.2
  • 2
    • 0036343422 scopus 로고    scopus 로고
    • Mouse neuroinvasive phenotype of West Nile virus strains varies depending upon virus genotype
    • Beasley D.W., Li L., Suderman M.T., Barrett A.D. Mouse neuroinvasive phenotype of West Nile virus strains varies depending upon virus genotype. Virology 2002, 296(1):17-23.
    • (2002) Virology , vol.296 , Issue.1 , pp. 17-23
    • Beasley, D.W.1    Li, L.2    Suderman, M.T.3    Barrett, A.D.4
  • 4
    • 33846496754 scopus 로고    scopus 로고
    • The envelope glycoprotein domain III of dengue virus serotypes 1 and 2 inhibit virus entry
    • Chin J.F., Chu J.J., Ng M.L. The envelope glycoprotein domain III of dengue virus serotypes 1 and 2 inhibit virus entry. Microbes Infect. 2007, 9(1):1-6.
    • (2007) Microbes Infect. , vol.9 , Issue.1 , pp. 1-6
    • Chin, J.F.1    Chu, J.J.2    Ng, M.L.3
  • 5
    • 33845986356 scopus 로고    scopus 로고
    • The DE loop of the domain III of the envelope protein appears to be associated with West Nile virus neutralization
    • Choi K.S., Nah J.J., Ko Y.J., Kim Y.J., Joo Y.S. The DE loop of the domain III of the envelope protein appears to be associated with West Nile virus neutralization. Virus Res. 2007, 123(2):216-218.
    • (2007) Virus Res. , vol.123 , Issue.2 , pp. 216-218
    • Choi, K.S.1    Nah, J.J.2    Ko, Y.J.3    Kim, Y.J.4    Joo, Y.S.5
  • 6
    • 13644262812 scopus 로고    scopus 로고
    • Inhibition of West Nile virus entry by using a recombinant domain III from the envelope glycoprotein
    • Chu J.J., Rajamanonmani R., Li J., Bhuvanakantham R., Lescar J., Ng M.L. Inhibition of West Nile virus entry by using a recombinant domain III from the envelope glycoprotein. J. Gen. Virol. 2005, 86(Pt 2):405-412.
    • (2005) J. Gen. Virol. , vol.86 , Issue.PART 2 , pp. 405-412
    • Chu, J.J.1    Rajamanonmani, R.2    Li, J.3    Bhuvanakantham, R.4    Lescar, J.5    Ng, M.L.6
  • 7
    • 0001528720 scopus 로고    scopus 로고
    • Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules
    • Fraczkiewicz R., Braun W. Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules. J. Comp. Chem. 1998, 19:319-333.
    • (1998) J. Comp. Chem. , vol.19 , pp. 319-333
    • Fraczkiewicz, R.1    Braun, W.2
  • 8
    • 0034898671 scopus 로고    scopus 로고
    • Phylogenetic relationships of flaviviruses correlate with their epidemiology, disease association and biogeography
    • Gaunt M.W., Sall A.A., de Lamballerie X., Falconar A.K., Dzhivanian T.I., Gould E.A. Phylogenetic relationships of flaviviruses correlate with their epidemiology, disease association and biogeography. J. Gen. Virol. 2001, 82(Pt 8):1867-1876.
    • (2001) J. Gen. Virol. , vol.82 , Issue.PART 8 , pp. 1867-1876
    • Gaunt, M.W.1    Sall, A.A.2    de Lamballerie, X.3    Falconar, A.K.4    Dzhivanian, T.I.5    Gould, E.A.6
  • 9
    • 0019948788 scopus 로고
    • Identification of distinct antigenic determinants on dengue-2 virus using monoclonal antibodies
    • Gentry M.K., Henchal E.A., McCown J.M., Brandt W.E., Dalrymple J.M. Identification of distinct antigenic determinants on dengue-2 virus using monoclonal antibodies. Am. J. Trop. Med. Hyg. 1982, 31(3 Pt 1):548-555.
    • (1982) Am. J. Trop. Med. Hyg. , vol.31 , Issue.3 PART 1 , pp. 548-555
    • Gentry, M.K.1    Henchal, E.A.2    McCown, J.M.3    Brandt, W.E.4    Dalrymple, J.M.5
  • 12
    • 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., 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 2007, 366(2):349-360.
    • (2007) Virology , vol.366 , Issue.2 , pp. 349-360
    • Gromowski, G.D.1    Barrett, A.D.2
  • 13
    • 0034695407 scopus 로고    scopus 로고
    • Conservation of folding and stability within a protein family: the tyrosine corner as an evolutionary cul-de-sac
    • Hamill S.J., Cota E., Chothia C., Clarke J. Conservation of folding and stability within a protein family: the tyrosine corner as an evolutionary cul-de-sac. J. Mol. Biol. 2000, 295(3):641-649.
    • (2000) J. Mol. Biol. , vol.295 , Issue.3 , pp. 641-649
    • Hamill, S.J.1    Cota, E.2    Chothia, C.3    Clarke, J.4
  • 14
    • 0028568291 scopus 로고
    • The tyrosine corner: a feature of most Greek key beta-barrel proteins
    • Hemmingsen J.M., Gernert K.M., Richardson J.S., Richardson D.C. The tyrosine corner: a feature of most Greek key beta-barrel proteins. Protein Sci. 1994, 3(11):1927-1937.
    • (1994) Protein Sci. , vol.3 , Issue.11 , pp. 1927-1937
    • Hemmingsen, J.M.1    Gernert, K.M.2    Richardson, J.S.3    Richardson, D.C.4
  • 15
    • 0036841628 scopus 로고    scopus 로고
    • Creating randomized amino acid libraries with the QuikChange Multi Site-Directed Mutagenesis Kit. Biotechniques, 1162, 1164-5
    • Hogrefe, H. H., Cline, J., Youngblood, G. L., and Allen, R. M. (2002). Creating randomized amino acid libraries with the QuikChange Multi Site-Directed Mutagenesis Kit. Biotechniques 33(5), 1158-60, 1162, 1164-5.
    • (2002) , vol.33 , Issue.5 , pp. 1158-60
    • Hogrefe, H.H.1    Cline, J.2    Youngblood, G.L.3    Allen, R.M.4
  • 16
    • 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., 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. 2004, 78(1):378-388.
    • (2004) J. Virol. , vol.78 , Issue.1 , 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
  • 17
    • 0034909241 scopus 로고    scopus 로고
    • Attenuation of Murray Valley encephalitis virus by site-directed mutagenesis of the hinge and putative receptor-binding regions of the envelope protein
    • Hurrelbrink R.J., McMinn P.C. Attenuation of Murray Valley encephalitis virus by site-directed mutagenesis of the hinge and putative receptor-binding regions of the envelope protein. J. Virol. 2001, 75(16):7692-7702.
    • (2001) J. Virol. , vol.75 , Issue.16 , pp. 7692-7702
    • Hurrelbrink, R.J.1    McMinn, P.C.2
  • 20
    • 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. 2000, 74(19):8867-8875.
    • (2000) J. Virol. , vol.74 , Issue.19 , pp. 8867-8875
    • Lee, E.1    Lobigs, M.2
  • 21
    • 33644973069 scopus 로고    scopus 로고
    • Quantifying the specific binding between West Nile virus envelope domain III protein and the cellular receptor alphaVbeta3 integrin
    • Lee J.W., Chu J.J., Ng M.L. Quantifying the specific binding between West Nile virus envelope domain III protein and the cellular receptor alphaVbeta3 integrin. J. Biol. Chem. 2006, 281(3):1352-1360.
    • (2006) J. Biol. Chem. , vol.281 , Issue.3 , pp. 1352-1360
    • Lee, J.W.1    Chu, J.J.2    Ng, M.L.3
  • 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., Beasley D.W. Differential expression of domain III neutralizing epitopes on the envelope proteins of West Nile virus strains. Virology 2005, 335(1):99-105.
    • (2005) Virology , vol.335 , Issue.1 , pp. 99-105
    • Li, L.1    Barrett, A.D.2    Beasley, D.W.3
  • 23
    • 34548278532 scopus 로고    scopus 로고
    • Mapping to completeness and transplantation of a group-specific, discontinuous, neutralizing epitope in the envelope protein of dengue virus
    • Lisova O., Hardy F., Petit V., Bedouelle H. Mapping to completeness and transplantation of a group-specific, discontinuous, neutralizing epitope in the envelope protein of dengue virus. J. Gen. Virol. 2007, 88(Pt 9):2387-2397.
    • (2007) J. Gen. Virol. , vol.88 , Issue.PART 9 , pp. 2387-2397
    • Lisova, O.1    Hardy, F.2    Petit, V.3    Bedouelle, H.4
  • 24
    • 0033818910 scopus 로고    scopus 로고
    • Attenuation of tick-borne encephalitis virus by structure-based site-specific mutagenesis of a putative flavivirus receptor binding site
    • Mandl C.W., Allison S.L., Holzmann H., Meixner T., Heinz F.X. Attenuation of tick-borne encephalitis virus by structure-based site-specific mutagenesis of a putative flavivirus receptor binding site. J. Virol. 2000, 74(20):9601-9609.
    • (2000) J. Virol. , vol.74 , Issue.20 , pp. 9601-9609
    • Mandl, C.W.1    Allison, S.L.2    Holzmann, H.3    Meixner, T.4    Heinz, F.X.5
  • 25
    • 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. U S A 2003, 100(12):6986-6991.
    • (2003) Proc. Natl. Acad. Sci. U S A , vol.100 , Issue.12 , pp. 6986-6991
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 28
    • 33751223215 scopus 로고    scopus 로고
    • Crystal structure of the West Nile virus envelope glycoprotein
    • Nybakken G.E., Nelson C.A., Chen B.R., Diamond M.S., Fremont D.H. Crystal structure of the West Nile virus envelope glycoprotein. J Virol 2006, 80(23):11467-11474.
    • (2006) J Virol , vol.80 , Issue.23 , pp. 11467-11474
    • Nybakken, G.E.1    Nelson, C.A.2    Chen, B.R.3    Diamond, M.S.4    Fremont, D.H.5
  • 29
    • 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., Fremont D.H. Structural basis of West Nile virus neutralization by a therapeutic antibody. Nature 2005, 437(7059):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
  • 31
    • 33846409495 scopus 로고    scopus 로고
    • Bacterially expressed and refolded envelope protein (domain III) of dengue virus type-4 binds heparan sulfate
    • Pattnaik P., Babu J.P., Verma S.K., Tak V., Rao P.V. Bacterially expressed and refolded envelope protein (domain III) of dengue virus type-4 binds heparan sulfate. J. Chromatogr. B. Analyt. Technol. Biomed. Life Sci. 2007, 846(1-2):184-194.
    • (2007) J. Chromatogr. B. Analyt. Technol. Biomed. Life Sci. , vol.846 , Issue.1-2 , pp. 184-194
    • Pattnaik, P.1    Babu, J.P.2    Verma, S.K.3    Tak, V.4    Rao, P.V.5
  • 32
    • 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., Harrison S.C. The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution. Nature 1995, 375(6529):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
  • 33
    • 1542466883 scopus 로고    scopus 로고
    • Antigenic structure of flavivirus proteins
    • Roehrig J.T. Antigenic structure of flavivirus proteins. Adv. Virus Res. 2003, 59:141-175.
    • (2003) Adv. Virus Res. , vol.59 , pp. 141-175
    • Roehrig, J.T.1
  • 35
    • 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., 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. 2004, 279(37):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
    • 0242580241 scopus 로고    scopus 로고
    • Structural basis of a flavivirus recognized by its neutralizing antibody: solution structure of the domain III of the Japanese encephalitis virus envelope protein
    • Wu K.P., Wu C.W., Tsao Y.P., Kuo T.W., Lou Y.C., Lin C.W., Wu S.C., Cheng J.W. Structural basis of a flavivirus recognized by its neutralizing antibody: solution structure of the domain III of the Japanese encephalitis virus envelope protein. J. Biol. Chem. 2003, 278(46):46007-46013.
    • (2003) J. Biol. Chem. , vol.278 , Issue.46 , pp. 46007-46013
    • Wu, K.P.1    Wu, C.W.2    Tsao, Y.P.3    Kuo, T.W.4    Lou, Y.C.5    Lin, C.W.6    Wu, S.C.7    Cheng, J.W.8
  • 39
    • 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., Lee J.C. Solution structure and structural dynamics of envelope protein domain III of mosquito- and tick-borne flaviviruses. Biochemistry 2004, 43(28):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
  • 40
    • 33748205133 scopus 로고    scopus 로고
    • A mutation in the envelope protein fusion loop attenuates mouse neuroinvasiveness of the NY99 strain of West Nile virus
    • Zhang S., Li L., Woodson S.E., Huang C.Y., Kinney R.M., Barrett A.D., Beasley D.W. A mutation in the envelope protein fusion loop attenuates mouse neuroinvasiveness of the NY99 strain of West Nile virus. Virology 2006, 353(1):35-40.
    • (2006) Virology , vol.353 , Issue.1 , pp. 35-40
    • Zhang, S.1    Li, L.2    Woodson, S.E.3    Huang, C.Y.4    Kinney, R.M.5    Barrett, A.D.6    Beasley, D.W.7
  • 41
    • 67650697066 scopus 로고    scopus 로고
    • Development of resistance to passive therapy with a potently neutralizing humanized monoclonal antibody against West Nile virus
    • Zhang S., Vogt M.R., Oliphant T., Engle M., Bovshik E.I., Diamond M.S., Beasley D.W. Development of resistance to passive therapy with a potently neutralizing humanized monoclonal antibody against West Nile virus. J. Infect. Dis. 2009, 200(2):202-205.
    • (2009) J. Infect. Dis. , vol.200 , Issue.2 , pp. 202-205
    • Zhang, S.1    Vogt, M.R.2    Oliphant, T.3    Engle, M.4    Bovshik, E.I.5    Diamond, M.S.6    Beasley, D.W.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.