메뉴 건너뛰기




Volumn 396, Issue 2, 2010, Pages 305-315

The dengue virus type 2 envelope protein fusion peptide is essential for membrane fusion

Author keywords

Dengue; Envelope; Flavivirus; Fusion; Mutagenesis; Virus uncoating; Virus endosome membrane fusion

Indexed keywords

COMPLEMENTARY DNA; ENVELOPE PROTEIN; HYBRID PROTEIN; RNA;

EID: 70949093288     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2009.10.027     Document Type: Article
Times cited : (66)

References (56)
  • 1
    • 41649101680 scopus 로고    scopus 로고
    • Functional entry of dengue virus into Aedes albopictus mosquito cells is dependent on clathrin-mediated endocytosis
    • Acosta E.G., Castilla V., and Damonte E.B. Functional entry of dengue virus into Aedes albopictus mosquito cells is dependent on clathrin-mediated endocytosis. J. Gen. Virol. 89 (2008) 474-484
    • (2008) J. Gen. Virol. , vol.89 , pp. 474-484
    • Acosta, E.G.1    Castilla, V.2    Damonte, E.B.3
  • 2
    • 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., and 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
  • 4
    • 34548605884 scopus 로고    scopus 로고
    • Glycosylation of the dengue 2 virus E protein at N67 is critical for virus growth in vitro but not for growth in intrathoracically inoculated Aedes aegypti mosquitoes
    • Bryant J.E., Calvert A.E., Mesesan K., Crabtree M.B., Volpe K.E., Silengo S., Kinney R.M., Huang C.Y., Miller B.R., and Roehrig J.T. Glycosylation of the dengue 2 virus E protein at N67 is critical for virus growth in vitro but not for growth in intrathoracically inoculated Aedes aegypti mosquitoes. Virology 366 (2007) 415-423
    • (2007) Virology , vol.366 , pp. 415-423
    • Bryant, J.E.1    Calvert, A.E.2    Mesesan, K.3    Crabtree, M.B.4    Volpe, K.E.5    Silengo, S.6    Kinney, R.M.7    Huang, C.Y.8    Miller, B.R.9    Roehrig, J.T.10
  • 5
    • 28844441250 scopus 로고    scopus 로고
    • Determining genetic stabilities of chimeric dengue vaccine candidates based on dengue 2 PDK-53 virus by sequencing and quantitative TaqMAMA
    • Butrapet S., Kinney R.M., and Huang C.Y. Determining genetic stabilities of chimeric dengue vaccine candidates based on dengue 2 PDK-53 virus by sequencing and quantitative TaqMAMA. J. Virol. Methods 131 (2006) 1-9
    • (2006) J. Virol. Methods , vol.131 , pp. 1-9
    • Butrapet, S.1    Kinney, R.M.2    Huang, C.Y.3
  • 6
    • 4544266363 scopus 로고    scopus 로고
    • Infectious entry of West Nile virus occurs through a clathrin-mediated endocytic pathway
    • Chu J.J., and Ng M.L. Infectious entry of West Nile virus occurs through a clathrin-mediated endocytic pathway. J. Virol. 78 (2004) 10543-10555
    • (2004) J. Virol. , vol.78 , pp. 10543-10555
    • Chu, J.J.1    Ng, M.L.2
  • 7
    • 33646867001 scopus 로고    scopus 로고
    • Analysis of the endocytic pathway mediating the infectious entry of mosquito-borne flavivirus West Nile into Aedes albopictus mosquito (C6/36) cells
    • Chu J.J., Leong P.W., and Ng M.L. Analysis of the endocytic pathway mediating the infectious entry of mosquito-borne flavivirus West Nile into Aedes albopictus mosquito (C6/36) cells. Virology 349 (2006) 463-475
    • (2006) Virology , vol.349 , pp. 463-475
    • Chu, J.J.1    Leong, P.W.2    Ng, M.L.3
  • 8
    • 0034732136 scopus 로고    scopus 로고
    • Membrane fusion activity of tick-borne encephalitis virus and recombinant subviral particles in a liposomal model system
    • Corver J., Ortiz A., Allison S.L., Schalich J., Heinz F.X., and Wilschut J. Membrane fusion activity of tick-borne encephalitis virus and recombinant subviral particles in a liposomal model system. Virology 269 (2000) 37-46
    • (2000) Virology , vol.269 , pp. 37-46
    • Corver, J.1    Ortiz, A.2    Allison, S.L.3    Schalich, J.4    Heinz, F.X.5    Wilschut, J.6
  • 9
    • 10044263508 scopus 로고    scopus 로고
    • Localization and characterization of flavivirus envelope glycoprotein cross-reactive epitopes
    • Crill W.D., and Chang G.J. Localization and characterization of flavivirus envelope glycoprotein cross-reactive epitopes. J. Virol. 78 (2004) 13975-13986
    • (2004) J. Virol. , vol.78 , pp. 13975-13986
    • Crill, W.D.1    Chang, G.J.2
  • 10
    • 34047178962 scopus 로고    scopus 로고
    • A detailed mutagenesis study of flavivirus cross-reactive epitopes using West Nile virus-like particles
    • Crill W.D., Trainor N.B., and Chang G.J. A detailed mutagenesis study of flavivirus cross-reactive epitopes using West Nile virus-like particles. J. Gen. Virol. 88 (2007) 1169-1174
    • (2007) J. Gen. Virol. , vol.88 , pp. 1169-1174
    • Crill, W.D.1    Trainor, N.B.2    Chang, G.J.3
  • 11
    • 55949108725 scopus 로고    scopus 로고
    • Identification of specific histidines as pH sensors in flavivirus membrane fusion
    • Fritz R., Stiasny K., and Heinz F.X. Identification of specific histidines as pH sensors in flavivirus membrane fusion. J. Cell. Biol. 183 (2008) 353-361
    • (2008) J. Cell. Biol. , vol.183 , pp. 353-361
    • Fritz, R.1    Stiasny, K.2    Heinz, F.X.3
  • 12
    • 0022450456 scopus 로고
    • A new mechanism for the neutralization of enveloped viruses by antiviral antibody
    • Gollins S.W., and Porterfield J.S. A new mechanism for the neutralization of enveloped viruses by antiviral antibody. Nature 321 (1986) 244-246
    • (1986) Nature , vol.321 , pp. 244-246
    • Gollins, S.W.1    Porterfield, J.S.2
  • 13
    • 0022632105 scopus 로고
    • pH-dependent fusion between the flavivirus West Nile and liposomal model membranes
    • Gollins S.W., and Porterfield J.S. pH-dependent fusion between the flavivirus West Nile and liposomal model membranes. J. Gen. Virol. 67 (1986) 157-166
    • (1986) J. Gen. Virol. , vol.67 , pp. 157-166
    • Gollins, S.W.1    Porterfield, J.S.2
  • 14
    • 8644255116 scopus 로고    scopus 로고
    • Epitope determinants of a chimpanzee Fab antibody that efficiently cross-neutralizes dengue type 1 and type 2 viruses map to inside and in close proximity to fusion loop of the dengue type 2 virus envelope glycoprotein
    • Goncalvez A.P., Purcell R.H., and Lai C.J. Epitope determinants of a chimpanzee Fab antibody that efficiently cross-neutralizes dengue type 1 and type 2 viruses map to inside and in close proximity to fusion loop of the dengue type 2 virus envelope glycoprotein. J. Virol. 78 (2004) 12919-12928
    • (2004) J. Virol. , vol.78 , pp. 12919-12928
    • Goncalvez, A.P.1    Purcell, R.H.2    Lai, C.J.3
  • 15
    • 0033258362 scopus 로고    scopus 로고
    • Impact of dengue/dengue hemorrhagic fever on the developing world
    • Gubler D.J., and Meltzer M. Impact of dengue/dengue hemorrhagic fever on the developing world. Adv. Virus Res. 53 (1999) 35-70
    • (1999) Adv. Virus Res. , vol.53 , pp. 35-70
    • Gubler, D.J.1    Meltzer, M.2
  • 16
    • 0025855266 scopus 로고
    • Fusion activity of flaviviruses: comparison of mature and immature (prM-containing) tick-borne encephalitis virions
    • Guirakhoo F., Heinz F.X., Mandl C.W., Holzmann H., and Kunz C. Fusion activity of flaviviruses: comparison of mature and immature (prM-containing) tick-borne encephalitis virions. J. Gen. Virol. 72 (1991) 1323-1329
    • (1991) J. Gen. Virol. , vol.72 , pp. 1323-1329
    • Guirakhoo, F.1    Heinz, F.X.2    Mandl, C.W.3    Holzmann, H.4    Kunz, C.5
  • 17
    • 0027081630 scopus 로고
    • The Murray Valley encephalitis virus prM protein confers acid resistance to virus particles and alters the expression of epitopes within the R2 domain of E glycoprotein
    • Guirakhoo F., Bolin R.A., and Roehrig J.T. The Murray Valley encephalitis virus prM protein confers acid resistance to virus particles and alters the expression of epitopes within the R2 domain of E glycoprotein. Virology 191 (1992) 921-931
    • (1992) Virology , vol.191 , pp. 921-931
    • Guirakhoo, F.1    Bolin, R.A.2    Roehrig, J.T.3
  • 18
    • 0027169938 scopus 로고
    • Selection and partial characterization of dengue 2 virus mutants that induce fusion at elevated pH
    • Guirakhoo F., Hunt A.R., Lewis J.G., and Roehrig J.T. Selection and partial characterization of dengue 2 virus mutants that induce fusion at elevated pH. Virology 194 (1993) 219-223
    • (1993) Virology , vol.194 , pp. 219-223
    • Guirakhoo, F.1    Hunt, A.R.2    Lewis, J.G.3    Roehrig, J.T.4
  • 19
    • 0022522522 scopus 로고
    • Epitope mapping of flavivirus glycoproteins
    • Heinz F.X. Epitope mapping of flavivirus glycoproteins. Adv. Virus Res. 31 (1986) 103-168
    • (1986) Adv. Virus Res. , vol.31 , pp. 103-168
    • Heinz, F.X.1
  • 20
    • 0034567567 scopus 로고    scopus 로고
    • Structures and mechanisms in flavivirus fusion
    • Heinz F.X., and Allison S.L. Structures and mechanisms in flavivirus fusion. Adv. Virus Res. 55 (2000) 231-269
    • (2000) Adv. Virus Res. , vol.55 , pp. 231-269
    • Heinz, F.X.1    Allison, S.L.2
  • 21
    • 1542466884 scopus 로고    scopus 로고
    • Flavivirus structure and membrane fusion
    • Heinz F.X., and Allison S.L. Flavivirus structure and membrane fusion. Adv. Virus Res. 59 (2003) 63-97
    • (2003) Adv. Virus Res. , vol.59 , pp. 63-97
    • Heinz, F.X.1    Allison, S.L.2
  • 22
    • 0035021836 scopus 로고    scopus 로고
    • Development of a fluorogenic RT-PCR system for quantitative identification of dengue virus serotypes 1-4 using conserved and serotype-specific 3′ noncoding sequences
    • Houng H.S., Chung-Ming Chen R., Vaughn D.W., and Kanesa-thasan N. Development of a fluorogenic RT-PCR system for quantitative identification of dengue virus serotypes 1-4 using conserved and serotype-specific 3′ noncoding sequences. J. Virol. Methods 95 (2001) 19-32
    • (2001) J. Virol. Methods , vol.95 , pp. 19-32
    • Houng, H.S.1    Chung-Ming Chen, R.2    Vaughn, D.W.3    Kanesa-thasan, N.4
  • 23
    • 0034096441 scopus 로고    scopus 로고
    • Chimeric dengue type 2 (vaccine strain PDK-53)/dengue type 1 virus as a potential candidate dengue type 1 virus vaccine
    • Huang C.Y., Butrapet S., Pierro D.J., Chang G.J., Hunt A.R., Bhamarapravati N., Gubler D.J., and Kinney R.M. Chimeric dengue type 2 (vaccine strain PDK-53)/dengue type 1 virus as a potential candidate dengue type 1 virus vaccine. J. Virol. 74 (2000) 3020-3028
    • (2000) J. Virol. , vol.74 , pp. 3020-3028
    • Huang, C.Y.1    Butrapet, S.2    Pierro, D.J.3    Chang, G.J.4    Hunt, A.R.5    Bhamarapravati, N.6    Gubler, D.J.7    Kinney, R.M.8
  • 25
    • 29144497159 scopus 로고    scopus 로고
    • Class II virus membrane fusion proteins
    • Kielian M. Class II virus membrane fusion proteins. Virology 344 (2006) 38-47
    • (2006) Virology , vol.344 , pp. 38-47
    • Kielian, M.1
  • 26
    • 0022968098 scopus 로고
    • The effect of pH on the early interaction of West Nile virus with P388D1 cells
    • Kimura T., Gollins S.W., and Porterfield J.S. The effect of pH on the early interaction of West Nile virus with P388D1 cells. J. Gen. Virol. 67 (1986) 2423-2433
    • (1986) J. Gen. Virol. , vol.67 , pp. 2423-2433
    • Kimura, T.1    Gollins, S.W.2    Porterfield, J.S.3
  • 27
    • 0030996972 scopus 로고    scopus 로고
    • Construction of infectious cDNA clones for dengue 2 virus: strain 16681 and its attenuated vaccine derivative, strain PDK-53
    • Kinney R.M., Butrapet S., Chang G.J., Tsuchiya K.R., Roehrig J.T., Bhamarapravati N., and Gubler D.J. Construction of infectious cDNA clones for dengue 2 virus: strain 16681 and its attenuated vaccine derivative, strain PDK-53. Virology 230 (1997) 300-308
    • (1997) Virology , vol.230 , pp. 300-308
    • Kinney, R.M.1    Butrapet, S.2    Chang, G.J.3    Tsuchiya, K.R.4    Roehrig, J.T.5    Bhamarapravati, N.6    Gubler, D.J.7
  • 31
    • 43649094583 scopus 로고    scopus 로고
    • Distribution of amino acids in a lipid bilayer from computer simulations
    • MacCallum J.L., Bennett W.F., and Tieleman D.P. Distribution of amino acids in a lipid bilayer from computer simulations. Biophys. J. 94 (2008) 3393-3404
    • (2008) Biophys. J. , vol.94 , pp. 3393-3404
    • MacCallum, J.L.1    Bennett, W.F.2    Tieleman, D.P.3
  • 32
    • 0024548815 scopus 로고
    • Antigenic structure of the flavivirus envelope protein E at the molecular level, using tick-borne encephalitis virus as a model
    • Mandl C.W., Guirakhoo F., Holzmann H., Heinz F.X., and Kunz C. Antigenic structure of the flavivirus envelope protein E at the molecular level, using tick-borne encephalitis virus as a model. J. Virol. 63 (1989) 564-571
    • (1989) J. Virol. , vol.63 , pp. 564-571
    • Mandl, C.W.1    Guirakhoo, F.2    Holzmann, H.3    Heinz, F.X.4    Kunz, C.5
  • 34
    • 1642499388 scopus 로고    scopus 로고
    • Structure of the dengue virus envelope protein after membrane fusion
    • Modis Y., Ogata S., Clements D., and Harrison S.C. Structure of the dengue virus envelope protein after membrane fusion. Nature 427 (2004) 313-319
    • (2004) Nature , vol.427 , pp. 313-319
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 35
    • 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
  • 36
    • 47749122553 scopus 로고    scopus 로고
    • Endocytic pathway followed by dengue virus to infect the mosquito cell line C6/36 HT
    • Mosso C., Galvan-Mendoza I.J., Ludert J.E., and del Angel R.M. Endocytic pathway followed by dengue virus to infect the mosquito cell line C6/36 HT. Virology 378 (2008) 193-199
    • (2008) Virology , vol.378 , pp. 193-199
    • Mosso, C.1    Galvan-Mendoza, I.J.2    Ludert, J.E.3    del Angel, R.M.4
  • 37
    • 34347344857 scopus 로고    scopus 로고
    • Plaque formation by Japanese encephalitis virus bound to mosquito C6/36 cells after low pH exposure on the cell surface
    • Nawa M., Machida S., Takasaki T., and Kurane I. Plaque formation by Japanese encephalitis virus bound to mosquito C6/36 cells after low pH exposure on the cell surface. Jpn. J. Infect. Dis. 60 (2007) 118-120
    • (2007) Jpn. J. Infect. Dis. , vol.60 , pp. 118-120
    • Nawa, M.1    Machida, S.2    Takasaki, T.3    Kurane, I.4
  • 38
    • 0028798804 scopus 로고
    • Molecular basis of attenuation of neurovirulence of wild-type Japanese encephalitis virus strain SA14
    • Ni H., Chang G.J., Xie H., Trent D.W., and Barrett A.D. Molecular basis of attenuation of neurovirulence of wild-type Japanese encephalitis virus strain SA14. J. Gen. Virol. 76 (1995) 409-413
    • (1995) J. Gen. Virol. , vol.76 , pp. 409-413
    • Ni, H.1    Chang, G.J.2    Xie, H.3    Trent, D.W.4    Barrett, A.D.5
  • 39
    • 0142091698 scopus 로고    scopus 로고
    • Evidence for in vitro falsely-primed cDNAs that prevent specific detection of virus negative strand RNAs in dengue-infected cells: improvement by tagged RT-PCR
    • Peyrefitte C.N., Pastorino B., Bessaud M., Tolou H.J., and Couissinier-Paris P. Evidence for in vitro falsely-primed cDNAs that prevent specific detection of virus negative strand RNAs in dengue-infected cells: improvement by tagged RT-PCR. J. Virol. Methods 113 (2003) 19-28
    • (2003) J. Virol. Methods , vol.113 , pp. 19-28
    • Peyrefitte, C.N.1    Pastorino, B.2    Bessaud, M.3    Tolou, H.J.4    Couissinier-Paris, P.5
  • 40
    • 35348866182 scopus 로고    scopus 로고
    • Versatile annotation and publication quality visualization of protein complexes using POLYVIEW-3D
    • Porollo A., and Meller J. Versatile annotation and publication quality visualization of protein complexes using POLYVIEW-3D. BMC Bioinformatics 8 (2007) 316
    • (2007) BMC Bioinformatics , vol.8 , pp. 316
    • Porollo, A.1    Meller, J.2
  • 41
    • 0025030596 scopus 로고
    • Low pH-induced cell fusion in flavivirus-infected Aedes albopictus cell cultures
    • Randolph V.B., and Stollar V. Low pH-induced cell fusion in flavivirus-infected Aedes albopictus cell cultures. J. Gen. Virol. 71 (1990) 1845-1850
    • (1990) J. Gen. Virol. , vol.71 , pp. 1845-1850
    • Randolph, V.B.1    Stollar, V.2
  • 42
    • 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 (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
  • 43
    • 0025347479 scopus 로고
    • Antibodies to dengue 2 virus E-glycoprotein synthetic peptides identify antigenic conformation
    • Roehrig J.T., Johnson A.J., Hunt A.R., Bolin R.A., and Chu M.C. Antibodies to dengue 2 virus E-glycoprotein synthetic peptides identify antigenic conformation. Virology 177 (1990) 668-675
    • (1990) Virology , vol.177 , pp. 668-675
    • Roehrig, J.T.1    Johnson, A.J.2    Hunt, A.R.3    Bolin, R.A.4    Chu, M.C.5
  • 44
    • 0032486594 scopus 로고    scopus 로고
    • Monoclonal antibody mapping of the envelope glycoprotein of the dengue 2 virus
    • 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) Jamaica Virology , vol.246 , pp. 317-328
    • Roehrig, J.T.1    Bolin, R.A.2    Kelly, R.G.3
  • 45
    • 42449092928 scopus 로고    scopus 로고
    • Constancy and diversity in the flavivirus fusion peptide
    • Seligman S.J. Constancy and diversity in the flavivirus fusion peptide. Virol. J. 5 (2008) 27
    • (2008) Virol. J. , vol.5 , pp. 27
    • Seligman, S.J.1
  • 46
    • 3543095614 scopus 로고    scopus 로고
    • Effect of membrane curvature-modifying lipids on membrane fusion by tick-borne encephalitis virus
    • Stiasny K., and Heinz F.X. Effect of membrane curvature-modifying lipids on membrane fusion by tick-borne encephalitis virus. J. Virol. 78 (2004) 8536-8542
    • (2004) J. Virol. , vol.78 , pp. 8536-8542
    • Stiasny, K.1    Heinz, F.X.2
  • 47
    • 1542347705 scopus 로고    scopus 로고
    • Characterization of a membrane-associated trimeric low-pH-induced Form of the class II viral fusion protein E from tick-borne encephalitis virus and its crystallization
    • Stiasny K., Bressanelli S., Lepault J., Rey F.A., and Heinz F.X. Characterization of a membrane-associated trimeric low-pH-induced Form of the class II viral fusion protein E from tick-borne encephalitis virus and its crystallization. J. Virol. 78 (2004) 3178-3183
    • (2004) J. Virol. , vol.78 , pp. 3178-3183
    • Stiasny, K.1    Bressanelli, S.2    Lepault, J.3    Rey, F.A.4    Heinz, F.X.5
  • 48
    • 33947493080 scopus 로고    scopus 로고
    • Entry functions and antigenic structure of flavivirus envelope proteins
    • discussion 65-73, 251-3
    • Stiasny K., Kiermayr S., and Heinz F.X. Entry functions and antigenic structure of flavivirus envelope proteins. Novartis. Found. Symp. 277 (2006) 57-65 discussion 65-73, 251-3
    • (2006) Novartis. Found. Symp. , vol.277 , pp. 57-65
    • Stiasny, K.1    Kiermayr, S.2    Heinz, F.X.3
  • 49
    • 35148859259 scopus 로고    scopus 로고
    • Probing the flavivirus membrane fusion mechanism using monoclonal antibodies
    • Stiasny K., Brandler S., Kossl C., and Heinz F.X. Probing the flavivirus membrane fusion mechanism using monoclonal antibodies. J. Virol. 81 (2007) 11526-11531
    • (2007) J. Virol. , vol.81 , pp. 11526-11531
    • Stiasny, K.1    Brandler, S.2    Kossl, C.3    Heinz, F.X.4
  • 50
    • 33847246763 scopus 로고    scopus 로고
    • Characterization of a structural intermediate of flavivirus membrane fusion
    • Stiasny K., Kossl C., Lepault J., Rey F.A., and Heinz F.X. Characterization of a structural intermediate of flavivirus membrane fusion. PLoS Pathog. e20 (2007) 3
    • (2007) PLoS Pathog. , vol.e20 , pp. 3
    • Stiasny, K.1    Kossl, C.2    Lepault, J.3    Rey, F.A.4    Heinz, F.X.5
  • 51
    • 63449089372 scopus 로고    scopus 로고
    • Characterization of dengue virus entry into HepG2 cells
    • Suksanpaisan L., Susantad T., and Smith D.R. Characterization of dengue virus entry into HepG2 cells. J. Biomed. Sci. 16 (2009) 17
    • (2009) J. Biomed. Sci. , vol.16 , pp. 17
    • Suksanpaisan, L.1    Susantad, T.2    Smith, D.R.3
  • 52
    • 0024536540 scopus 로고
    • Flaviviruses can mediate fusion from without in Aedes albopictus mosquito cell cultures
    • Summers P.L., Cohen W.H., Ruiz M.M., Hase T., and Eckels K.H. Flaviviruses can mediate fusion from without in Aedes albopictus mosquito cell cultures. Virus Res. 12 (1989) 383-392
    • (1989) Virus Res. , vol.12 , pp. 383-392
    • Summers, P.L.1    Cohen, W.H.2    Ruiz, M.M.3    Hase, T.4    Eckels, K.H.5
  • 53
    • 33947722325 scopus 로고    scopus 로고
    • Mutation analysis of the fusion domain region of St. Louis encephalitis virus envelope protein
    • Trainor N.B., Crill W.D., Roberson J.A., and Chang G.J. Mutation analysis of the fusion domain region of St. Louis encephalitis virus envelope protein. Virology 360 (2007) 398-406
    • (2007) Virology , vol.360 , pp. 398-406
    • Trainor, N.B.1    Crill, W.D.2    Roberson, J.A.3    Chang, G.J.4
  • 55
    • 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., and Beasley D.W. A mutation in the envelope protein fusion loop attenuates mouse neuroinvasiveness of the NY99 strain of West Nile virus. Virology 353 (2006) 35-40
    • (2006) Virology , vol.353 , 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.