메뉴 건너뛰기
Journal of Virology
Volumn 89, Issue 10, 2015, Pages 5668-5686
Structure-based mutational analysis of several sites in the E protein: Implications for understanding the entry mechanism of Japanese encephalitis virus
Author keywords

[No Author keywords available]
Indexed keywords

E PROTEIN; MUTANT PROTEIN; UNCLASSIFIED DRUG; VIRUS PROTEIN; VIRUS DNA; VIRUS ENVELOPE PROTEIN;
EID: 84928534686     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00293-15     Document Type: Article
Times cited : (42)
References (69)
  • 1
    • 10944252079 scopus 로고    scopus 로고
    • Emerging flaviviruses: the spread and resurgence of Japanese encephalitis, West Nile and dengue viruses
    • Mackenzie JS, Gubler DJ, Petersen LR. 2004. Emerging flaviviruses: the spread and resurgence of Japanese encephalitis, West Nile and dengue viruses. Nat Med 10:S98-109. http://dx.doi.org/10.1038/nm1144.
    • (2004) Nat Med , vol.10 , pp. S98-S109
    • Mackenzie, J.S.1    Gubler, D.J.2    Petersen, L.R.3
  • 2
    • 0036116402 scopus 로고    scopus 로고
    • Japanese encephalitis virus: ecology and epidemiology
    • Endy TP, Nisalak A. 2002. Japanese encephalitis virus: ecology and epidemiology. Curr Top Microbiol Immunol 267:11-48. http://dx.doi.org/10.1007/978-3-642-59403-8.
    • (2002) Curr Top Microbiol Immunol , vol.267 , pp. 11-48
    • Endy, T.P.1    Nisalak, A.2
  • 3
    • 84896984783 scopus 로고    scopus 로고
    • Japanese encephalitis: the virus and vaccines
    • Yun SI, Lee YM. 2014. Japanese encephalitis: the virus and vaccines. Hum Vaccin Immunother 10:263-279. http://dx.doi.org/10.4161/hv.26902.
    • (2014) Hum Vaccin Immunother , vol.10 , pp. 263-279
    • Yun, S.I.1    Lee, Y.M.2
  • 4
    • 60549105745 scopus 로고    scopus 로고
    • Ecology and geographical expansion of Japanese encephalitis virus
    • van den Hurk AF, Ritchie SA, Mackenzie JS. 2009. Ecology and geographical expansion of Japanese encephalitis virus. Annu Rev Entomol 54:17-35. http://dx.doi.org/10.1146/annurev.ento.54.110807.090510.
    • (2009) Annu Rev Entomol , vol.54 , pp. 17-35
    • van den Hurk, A.F.1    Ritchie, S.A.2    Mackenzie, J.S.3
  • 6
    • 77952293291 scopus 로고    scopus 로고
    • Overview: Japanese encephalitis
    • Misra UK, Kalita J. 2010. Overview: Japanese encephalitis. Prog Neurobiol 91:108-120. http://dx.doi.org/10.1016/j.pneurobio.2010.01.008.
    • (2010) Prog Neurobiol , vol.91 , pp. 108-120
    • Misra, U.K.1    Kalita, J.2
  • 8
    • 0038150878 scopus 로고    scopus 로고
    • Interference in Japanese encephalitis virus infection of Vero cells by a cationic amphiphilic drug, chlorpromazine
    • Nawa M, Takasaki T, Yamada K, Kurane I, Akatsuka T. 2003. Interference in Japanese encephalitis virus infection of Vero cells by a cationic amphiphilic drug, chlorpromazine. J Gen Virol 84:1737-1741. http://dx.doi.org/10.1099/vir.0.18883-0.
    • (2003) J Gen Virol , vol.84 , pp. 1737-1741
    • Nawa, M.1    Takasaki, T.2    Yamada, K.3    Kurane, I.4    Akatsuka, T.5
  • 9
    • 78651253906 scopus 로고    scopus 로고
    • Critical role of lipid rafts in virus entry and activation of phosphoinositide 3' kinase/Akt signaling during early stages of Japanese encephalitis virus infection in neural stem/progenitor cells
    • Das S, Chakraborty S, Basu A. 2010. Critical role of lipid rafts in virus entry and activation of phosphoinositide 3' kinase/Akt signaling during early stages of Japanese encephalitis virus infection in neural stem/progenitor cells. J Neurochem 115:537-549. http://dx.doi.org/10.1111/j.1471-4159.2010.06951.x.
    • (2010) J Neurochem , vol.115 , pp. 537-549
    • Das, S.1    Chakraborty, S.2    Basu, A.3
  • 10
    • 84870664901 scopus 로고    scopus 로고
    • Japanese encephalitis virus enters rat neuroblastoma cells via a pH-dependent, dynamin and caveolamediated endocytosis pathway
    • Zhu YZ, Xu QQ, Wu DG, Ren H, Zhao P, Lao WG, Wang Y, Tao QY, Qian XJ, Wei YH, Cao MM, Qi ZT. 2012. Japanese encephalitis virus enters rat neuroblastoma cells via a pH-dependent, dynamin and caveolamediated endocytosis pathway. J Virol 86:13407-13422. http://dx.doi.org/10.1128/JVI.00903-12.
    • (2012) J Virol , vol.86 , pp. 13407-13422
    • Zhu, Y.Z.1    Xu, Q.Q.2    Wu, D.G.3    Ren, H.4    Zhao, P.5    Lao, W.G.6    Wang, Y.7    Tao, Q.Y.8    Qian, X.J.9    Wei, Y.H.10    Cao, M.M.11    Qi, Z.T.12
  • 11
    • 84871972407 scopus 로고    scopus 로고
    • Japanese encephalitis virus infects neuronal cells through a clathrin-independent endocytic mechanism
    • Kalia M, Khasa R, Sharma M, Nain M, Vrati S. 2013. Japanese encephalitis virus infects neuronal cells through a clathrin-independent endocytic mechanism. J Virol 87:148-162. http://dx.doi.org/10.1128/JVI.01399-12.
    • (2013) J Virol , vol.87 , pp. 148-162
    • Kalia, M.1    Khasa, R.2    Sharma, M.3    Nain, M.4    Vrati, S.5
  • 12
    • 31344432402 scopus 로고    scopus 로고
    • Virus membrane-fusion proteins: more than one way to make a hairpin
    • Kielian M, Rey FA. 2006. Virus membrane-fusion proteins: more than one way to make a hairpin. Nat Rev Microbiol 4:67-76. http://dx.doi.org/10.1038/nrmicro1326.
    • (2006) Nat Rev Microbiol , vol.4 , pp. 67-76
    • Kielian, M.1    Rey, F.A.2
  • 13
    • 84874650957 scopus 로고    scopus 로고
    • Flaviviruses: braking the entering
    • Pierson TC, Kielian M. 2013. Flaviviruses: braking the entering. Curr Opin Virol 3:3-12. http://dx.doi.org/10.1016/j.coviro.2012.12.001.
    • (2013) Curr Opin Virol , vol.3 , pp. 3-12
    • Pierson, T.C.1    Kielian, M.2
  • 14
    • 29144497159 scopus 로고    scopus 로고
    • Class II virus membrane fusion proteins
    • Kielian M. 2006. Class II virus membrane fusion proteins. Virology 344: 38-47. http://dx.doi.org/10.1016/j.virol.2005.09.036.
    • (2006) Virology , vol.344 , pp. 38-47
    • Kielian, M.1
  • 16
    • 84857082391 scopus 로고    scopus 로고
    • Crystal structure of the Japanese encephalitis virus envelope protein
    • Luca VC, AbiMansour J, Nelson CA, Fremont DH. 2012. Crystal structure of the Japanese encephalitis virus envelope protein. J Virol 86:2337-2346. http://dx.doi.org/10.1128/JVI.06072-11.
    • (2012) J Virol , vol.86 , pp. 2337-2346
    • Luca, V.C.1    AbiMansour, J.2    Nelson, C.A.3    Fremont, D.H.4
  • 17
    • 0029014434 scopus 로고
    • The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution
    • Rey FA, Heinz FX, Mandl C, Kunz C, Harrison SC. 1995. The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution. Nature 375:291-298. http://dx.doi.org/10.1038/375291a0.
    • (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
  • 18
    • 84860293221 scopus 로고    scopus 로고
    • Inhibition of Japanese encephalitis virus entry into the cells by the envelope glycoprotein domain III (EDIII) and the loop 3 peptide derived from EDIII
    • Li C, Zhang LY, Sun MX, Li PP, Huang L, Wei JC, Yao YL, Isahg H, Chen PY, Mao X. 2012. Inhibition of Japanese encephalitis virus entry into the cells by the envelope glycoprotein domain III (EDIII) and the loop 3 peptide derived from EDIII. Antiviral Res 94:179-183. http://dx.doi.org/10.1016/j.antiviral.2012.03.002.
    • (2012) Antiviral Res , vol.94 , pp. 179-183
    • Li, C.1    Zhang, L.Y.2    Sun, M.X.3    Li, P.P.4    Huang, L.5    Wei, J.C.6    Yao, Y.L.7    Isahg, H.8    Chen, P.Y.9    Mao, X.10
  • 19
    • 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 JJ, Hsieh MT, Young MJ, Kao CL, King CC, Chang W. 2004. 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 78:378-388. http://dx.doi.org/10.1128/JVI.78.1.378-388.2004.
    • (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
  • 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. 2000. 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 74:8867-8875. http://dx.doi.org/10.1128/JVI.74.19.8867-8875.2000.
    • (2000) J Virol , vol.74 , pp. 8867-8875
    • Lee, E.1    Lobigs, M.2
  • 21
    • 84894210072 scopus 로고    scopus 로고
    • Peptide inhibitor of Japanese encephalitis virus infection targeting envelope protein domain III
    • Zu X, Liu Y, Wang S, Jin R, Zhou Z, Liu H, Gong R, Xiao G, Wang W. 2014. Peptide inhibitor of Japanese encephalitis virus infection targeting envelope protein domain III. Antiviral Res 104:7-14. http://dx.doi.org/10.1016/j.antiviral.2014.01.011.
    • (2014) Antiviral Res , vol.104 , pp. 7-14
    • Zu, X.1    Liu, Y.2    Wang, S.3    Jin, R.4    Zhou, Z.5    Liu, H.6    Gong, R.7    Xiao, G.8    Wang, W.9
  • 22
    • 9744228670 scopus 로고    scopus 로고
    • Novel cell adhesive glycosaminoglycan-binding proteins of Japanese encephalitis virus
    • Wu SC, Chiang JR, Lin CW. 2004. Novel cell adhesive glycosaminoglycan-binding proteins of Japanese encephalitis virus. Biomacromolecules 5:2160-2164. http://dx.doi.org/10.1021/bm0498068.
    • (2004) Biomacromolecules , vol.5 , pp. 2160-2164
    • Wu, S.C.1    Chiang, J.R.2    Lin, C.W.3
  • 23
    • 21744440122 scopus 로고    scopus 로고
    • Fitness of Japanese encephalitis virus to Neuro-2a cells is determined by interactions of the viral envelope protein with highly sulfated glycosaminoglycans on the cell surface
    • Chiou SS, Liu H, Chuang CK, Lin CC, Chen WJ. 2005. Fitness of Japanese encephalitis virus to Neuro-2a cells is determined by interactions of the viral envelope protein with highly sulfated glycosaminoglycans on the cell surface. J Med Virol 76:583-592. http://dx.doi.org/10.1002/jmv.20406.
    • (2005) J Med Virol , vol.76 , pp. 583-592
    • Chiou, S.S.1    Liu, H.2    Chuang, C.K.3    Lin, C.C.4    Chen, W.J.5
  • 24
    • 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, Harrison SC. 2005. Variable surface epitopes in the crystal structure of dengue virus type 3 envelope glycoprotein. J Virol 79:1223-1231. http://dx.doi.org/10.1128/JVI.79.2.1223-1231.2005.
    • (2005) J Virol , vol.79 , pp. 1223-1231
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 25
    • 84905256517 scopus 로고    scopus 로고
    • Distinct usage of three C-type lectins by Japanese encephalitis virus: DCSIGN, DC-SIGNR, and LSECtin
    • Shimojima M, Takenouchi A, Shimoda H, Kimura N, Maeda K. 2014. Distinct usage of three C-type lectins by Japanese encephalitis virus: DCSIGN, DC-SIGNR, and LSECtin. Arch Virol 159:2023-2031. http://dx.doi.org/10.1007/s00705-014-2042-2.
    • (2014) Arch Virol , vol.159 , pp. 2023-2031
    • Shimojima, M.1    Takenouchi, A.2    Shimoda, H.3    Kimura, N.4    Maeda, K.5
  • 26
    • 60349109590 scopus 로고    scopus 로고
    • Heat shock protein 70 on Neuro2a cells is a putative receptor for Japanese encephalitis virus
    • Das S, Laxminarayana SV, Chandra N, Ravi V, Desai A. 2009. Heat shock protein 70 on Neuro2a cells is a putative receptor for Japanese encephalitis virus. Virology 385:47-57. http://dx.doi.org/10.1016/j.virol.2008.10.025.
    • (2009) Virology , vol.385 , pp. 47-57
    • Das, S.1    Laxminarayana, S.V.2    Chandra, N.3    Ravi, V.4    Desai, A.5
  • 27
    • 80051819329 scopus 로고    scopus 로고
    • Vimentin binding is critical for infection by the virulent strain of Japanese encephalitis virus
    • Liang JJ, Yu CY, Liao CL, Lin YL. 2011. Vimentin binding is critical for infection by the virulent strain of Japanese encephalitis virus. Cell Microbiol 13:1358-1370. http://dx.doi.org/10.1111/j.1462-5822.2011.01624.x.
    • (2011) Cell Microbiol , vol.13 , pp. 1358-1370
    • Liang, J.J.1    Yu, C.Y.2    Liao, C.L.3    Lin, Y.L.4
  • 28
    • 1842526097 scopus 로고    scopus 로고
    • Structure of a flavivirus envelope glycoprotein in its low-pH-induced membrane fusion conformation
    • Bressanelli S, Stiasny K, Allison SL, Stura EA, Duquerroy S, Lescar J, Heinz FX, Rey FA. 2004. Structure of a flavivirus envelope glycoprotein in its low-pH-induced membrane fusion conformation. EMBO J 23:728-738. http://dx.doi.org/10.1038/sj.emboj.7600064.
    • (2004) EMBO J , vol.23 , pp. 728-738
    • Bressanelli, S.1    Stiasny, K.2    Allison, S.L.3    Stura, E.A.4    Duquerroy, S.5    Lescar, J.6    Heinz, F.X.7    Rey, F.A.8
  • 29
    • 0037495036 scopus 로고    scopus 로고
    • A ligand-binding pocket in the dengue virus envelope glycoprotein
    • Modis Y, Ogata S, Clements D, Harrison SC. 2003. A ligand-binding pocket in the dengue virus envelope glycoprotein. Proc Natl Acad Sci U S A 100:6986-6991. http://dx.doi.org/10.1073/pnas.0832193100.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 6986-6991
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 30
    • 1642499388 scopus 로고    scopus 로고
    • Structure of the dengue virus envelope protein after membrane fusion
    • Modis Y, Ogata S, Clements D, Harrison SC. 2004. Structure of the dengue virus envelope protein after membrane fusion. Nature 427:313-319. http://dx.doi.org/10.1038/nature02165.
    • (2004) Nature , vol.427 , pp. 313-319
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 31
    • 0030738578 scopus 로고    scopus 로고
    • Changes in the dengue virus major envelope protein on passaging and their localization on the threedimensional structure of the protein
    • Lee E, Weir RC, Dalgarno L. 1997. Changes in the dengue virus major envelope protein on passaging and their localization on the threedimensional structure of the protein. Virology 232:281-290. http://dx.doi.org/10.1006/viro.1997.8570.
    • (1997) Virology , vol.232 , pp. 281-290
    • Lee, E.1    Weir, R.C.2    Dalgarno, L.3
  • 32
    • 0035864283 scopus 로고    scopus 로고
    • Epitopes on the dengue 1 virus envelope protein recognized by neutralizing IgM monoclonal antibodies
    • Beasley DW, Aaskov JG. 2001. Epitopes on the dengue 1 virus envelope protein recognized by neutralizing IgM monoclonal antibodies. Virology 279:447-458. http://dx.doi.org/10.1006/viro.2000.0721.
    • (2001) Virology , vol.279 , pp. 447-458
    • Beasley, D.W.1    Aaskov, J.G.2
  • 33
    • 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 RJ, McMinn PC. 2001. Attenuation of Murray Valley encephalitis virus by site-directed mutagenesis of the hinge and putative receptor-binding regions of the envelope protein. J Virol 75:7692-7702. http://dx.doi.org/10.1128/JVI.75.16.7692-7702.2001.
    • (2001) J Virol , vol.75 , pp. 7692-7702
    • Hurrelbrink, R.J.1    McMinn, P.C.2
  • 34
    • 0036148484 scopus 로고    scopus 로고
    • Single mutation in the flavivirus envelope protein hinge region increases neurovirulence for mice and monkeys but decreases viscerotropism for monkeys: relevance to development and safety testing of live, attenuated vaccines
    • Monath TP, Arroyo J, Levenbook I, Zhang ZX, Catalan J, Draper K, Guirakhoo F. 2002. Single mutation in the flavivirus envelope protein hinge region increases neurovirulence for mice and monkeys but decreases viscerotropism for monkeys: relevance to development and safety testing of live, attenuated vaccines. J Virol 76:1932-1943. http://dx.doi.org/10.1128/JVI.76.4.1932-1943.2002.
    • (2002) J Virol , vol.76 , pp. 1932-1943
    • Monath, T.P.1    Arroyo, J.2    Levenbook, I.3    Zhang, Z.X.4    Catalan, J.5    Draper, K.6    Guirakhoo, F.7
  • 35
    • 79953094417 scopus 로고    scopus 로고
    • Amino acid changes within the E protein hinge region that affect dengue virus type 2 infectivity and fusion
    • Butrapet S, Childers T, Moss KJ, Erb SM, Luy BE, Calvert AE, Blair CD, Roehrig JT, Huang CY. 2011. Amino acid changes within the E protein hinge region that affect dengue virus type 2 infectivity and fusion. Virology 413:118-127. http://dx.doi.org/10.1016/j.virol.2011.01.030.
    • (2011) Virology , vol.413 , pp. 118-127
    • Butrapet, S.1    Childers, T.2    Moss, K.J.3    Erb, S.M.4    Luy, B.E.5    Calvert, A.E.6    Blair, C.D.7    Roehrig, J.T.8    Huang, C.Y.9
  • 37
    • 79960951066 scopus 로고    scopus 로고
    • A concerted action of hepatitis C virus p7 and nonstructural protein 2 regulates core localization at the endoplasmic reticulum and virus assembly
    • Boson B, Granio O, Bartenschlager R, Cosset FL. 2011. A concerted action of hepatitis C virus p7 and nonstructural protein 2 regulates core localization at the endoplasmic reticulum and virus assembly. PLoS Pathog 7:e1002144. http://dx.doi.org/10.1371/journal.ppat.1002144.
    • (2011) PLoS Pathog , vol.7
    • Boson, B.1    Granio, O.2    Bartenschlager, R.3    Cosset, F.L.4
  • 38
    • 84864143276 scopus 로고    scopus 로고
    • Mutagenesis of the DI/DIII linker in dengue virus envelope protein impairs viral particle assembly
    • de Wispelaere M, Yang PL. 2012. Mutagenesis of the DI/DIII linker in dengue virus envelope protein impairs viral particle assembly. J Virol 86: 7072-7083. http://dx.doi.org/10.1128/JVI.00224-12.
    • (2012) J Virol , vol.86 , pp. 7072-7083
    • de Wispelaere, M.1    Yang, P.L.2
  • 39
    • 0027169938 scopus 로고
    • Selection and partial characterization of dengue 2 virus mutants that induce fusion at elevated pH
    • Guirakhoo F, Hunt AR, Lewis JG, Roehrig JT. 1993. Selection and partial characterization of dengue 2 virus mutants that induce fusion at elevated pH. Virology 194:219-223. http://dx.doi.org/10.1006/viro.1993.1252.
    • (1993) Virology , vol.194 , pp. 219-223
    • Guirakhoo, F.1    Hunt, A.R.2    Lewis, J.G.3    Roehrig, J.T.4
  • 40
    • 79952423390 scopus 로고    scopus 로고
    • Successful propagation of flavivirus infectious cDNAs by a novel method to reduce the cryptic bacterial promoter activity of virus genomes
    • Pu SY, Wu RH, Yang CC, Jao TM, Tsai MH, Wang JC, Lin HM, Chao YS, Yueh A. 2011. Successful propagation of flavivirus infectious cDNAs by a novel method to reduce the cryptic bacterial promoter activity of virus genomes. J Virol 85:2927-2941. http://dx.doi.org/10.1128/JVI.01986-10.
    • (2011) J Virol , vol.85 , pp. 2927-2941
    • Pu, S.Y.1    Wu, R.H.2    Yang, C.C.3    Jao, T.M.4    Tsai, M.H.5    Wang, J.C.6    Lin, H.M.7    Chao, Y.S.8    Yueh, A.9
  • 41
    • 84899845392 scopus 로고    scopus 로고
    • Dengue virus-and hepatitis C virus-induced replication and assembly compartments: the enemy inside-caught in the web
    • Chatel-Chaix L, Bartenschlager R. 2014. Dengue virus-and hepatitis C virus-induced replication and assembly compartments: the enemy inside-caught in the web. J Virol 88:5907-5911. http://dx.doi.org/10.1128/JVI.03404-13.
    • (2014) J Virol , vol.88 , pp. 5907-5911
    • Chatel-Chaix, L.1    Bartenschlager, R.2
  • 43
    • 79955417646 scopus 로고    scopus 로고
    • The helical domains of the stem region of dengue virus envelope protein are involved in both virus assembly and entry
    • Lin SR, Zou G, Hsieh SC, Qing M, Tsai WY, Shi PY, Wang WK. 2011. The helical domains of the stem region of dengue virus envelope protein are involved in both virus assembly and entry. J Virol 85:5159-5171. http://dx.doi.org/10.1128/JVI.02099-10.
    • (2011) J Virol , vol.85 , pp. 5159-5171
    • Lin, S.R.1    Zou, G.2    Hsieh, S.C.3    Qing, M.4    Tsai, W.Y.5    Shi, P.Y.6    Wang, W.K.7
  • 45
    • 70450208515 scopus 로고    scopus 로고
    • Association of the pr peptides with dengue virus at acidic pH blocks membrane fusion
    • Yu IM, Holdaway HA, Chipman PR, Kuhn RJ, Rossmann MG, Chen J. 2009. Association of the pr peptides with dengue virus at acidic pH blocks membrane fusion. J Virol 83:12101-12107. http://dx.doi.org/10.1128/JVI.01637-09.
    • (2009) J Virol , vol.83 , pp. 12101-12107
    • Yu, I.M.1    Holdaway, H.A.2    Chipman, P.R.3    Kuhn, R.J.4    Rossmann, M.G.5    Chen, J.6
  • 46
    • 0032989258 scopus 로고    scopus 로고
    • Mapping of functional elements in the stem-anchor region of tick-borne encephalitis virus envelope protein E
    • Allison SL, Stiasny K, Stadler K, Mandl CW, Heinz FX. 1999. Mapping of functional elements in the stem-anchor region of tick-borne encephalitis virus envelope protein E. J Virol 73:5605-5612.
    • (1999) J Virol , vol.73 , pp. 5605-5612
    • Allison, S.L.1    Stiasny, K.2    Stadler, K.3    Mandl, C.W.4    Heinz, F.X.5
  • 47
    • 79953287551 scopus 로고    scopus 로고
    • Endoglycosidase and glycoamidase release of N-linked glycans
    • Chapter 12. Unit 12.4
    • Freeze HH, Kranz C. 2010. Endoglycosidase and glycoamidase release of N-linked glycans. Curr Protoc Protein Sci Chapter 12:Unit 12.4. http://dx.doi.org/10.1002/0471140864.ps1204s62.
    • (2010) Curr Protoc Protein Sci
    • Freeze, H.H.1    Kranz, C.2
  • 48
    • 55949108725 scopus 로고    scopus 로고
    • Identification of specific histidines as pH sensors in flavivirus membrane fusion
    • Fritz R, Stiasny K, Heinz FX. 2008. Identification of specific histidines as pH sensors in flavivirus membrane fusion. J Cell Biol 183:353-361. http://dx.doi.org/10.1083/jcb.200806081.
    • (2008) J Cell Biol , vol.183 , pp. 353-361
    • Fritz, R.1    Stiasny, K.2    Heinz, F.X.3
  • 49
    • 70450162409 scopus 로고    scopus 로고
    • Protonation of individual histidine residues is not required for the pH-dependent entry of West Nile virus: evaluation of the "histidine switch" hypothesis
    • Nelson S, Poddar S, Lin TY, Pierson TC. 2009. Protonation of individual histidine residues is not required for the pH-dependent entry of West Nile virus: evaluation of the "histidine switch" hypothesis. J Virol 83:12631-12635. http://dx.doi.org/10.1128/JVI.01072-09.
    • (2009) J Virol , vol.83 , pp. 12631-12635
    • Nelson, S.1    Poddar, S.2    Lin, T.Y.3    Pierson, T.C.4
  • 51
    • 84877920902 scopus 로고    scopus 로고
    • Mutation of the dengue virus type 2 envelope protein heparan sulfate binding sites or the domain III lateral ridge blocks replication in Vero cells prior to membrane fusion
    • Roehrig JT, Butrapet S, Liss NM, Bennett SL, Luy BE, Childers T, Boroughs KL, Stovall JL, Calvert AE, Blair CD, Huang CY. 2013. Mutation of the dengue virus type 2 envelope protein heparan sulfate binding sites or the domain III lateral ridge blocks replication in Vero cells prior to membrane fusion. Virology 441:114-125. http://dx.doi.org/10.1016/j.virol.2013.03.011.
    • (2013) Virology , vol.441 , pp. 114-125
    • Roehrig, J.T.1    Butrapet, S.2    Liss, N.M.3    Bennett, S.L.4    Luy, B.E.5    Childers, T.6    Boroughs, K.L.7    Stovall, J.L.8    Calvert, A.E.9    Blair, C.D.10    Huang, C.Y.11
  • 52
    • 79953105927 scopus 로고    scopus 로고
    • Domain-III FG loop of the dengue virus type 2 envelope protein is important for infection of mammalian cells and Aedes aegypti mosquitoes
    • Erb SM, Butrapet S, Moss KJ, Luy BE, Childers T, Calvert AE, Silengo SJ, Roehrig JT, Huang CY, Blair CD. 2010. Domain-III FG loop of the dengue virus type 2 envelope protein is important for infection of mammalian cells and Aedes aegypti mosquitoes. Virology 406:328-335. http://dx.doi.org/10.1016/j.virol.2010.07.024.
    • (2010) Virology , vol.406 , pp. 328-335
    • Erb, S.M.1    Butrapet, S.2    Moss, K.J.3    Luy, B.E.4    Childers, T.5    Calvert, A.E.6    Silengo, S.J.7    Roehrig, J.T.8    Huang, C.Y.9    Blair, C.D.10
  • 54
    • 84891594368 scopus 로고    scopus 로고
    • Flavivirus entry receptors: an update
    • Perera-Lecoin M, Meertens L, Carnec X, Amara A. 2014. Flavivirus entry receptors: an update. Viruses 6:69-88. http://dx.doi.org/10.3390/v6010069.
    • (2014) Viruses , vol.6 , pp. 69-88
    • Perera-Lecoin, M.1    Meertens, L.2    Carnec, X.3    Amara, A.4
  • 56
    • 0030908029 scopus 로고    scopus 로고
    • Integrins as signaling molecules and targets for tumor therapy
    • Ruoslahti E. 1997. Integrins as signaling molecules and targets for tumor therapy. Kidney Int 51:1413-1417. http://dx.doi.org/10.1038/ki.1997.193.
    • (1997) Kidney Int , vol.51 , pp. 1413-1417
    • Ruoslahti, E.1
  • 57
    • 0041561082 scopus 로고    scopus 로고
    • Characterization of a 105-kDa plasma membrane associated glycoprotein that is involved in West Nile virus binding and infection
    • Chu JJ, Ng ML. 2003. Characterization of a 105-kDa plasma membrane associated glycoprotein that is involved in West Nile virus binding and infection. Virology 312:458-469. http://dx.doi.org/10.1016/S0042-6822(03)00261-7.
    • (2003) Virology , vol.312 , pp. 458-469
    • Chu, J.J.1    Ng, M.L.2
  • 58
    • 11144227268 scopus 로고    scopus 로고
    • Interaction of West Nile virus with αvβ3 integrin mediates virus entry into cells
    • Chu JJ, Ng ML. 2004. Interaction of West Nile virus with αvβ3 integrin mediates virus entry into cells. J Biol Chem 279:54533-54541. http://dx.doi.org/10.1074/jbc.M410208200.
    • (2004) J Biol Chem , vol.279 , pp. 54533-54541
    • Chu, J.J.1    Ng, M.L.2
  • 59
    • 0041563793 scopus 로고    scopus 로고
    • Dendritic-cellspecific ICAM3-grabbing non-integrin is essential for the productive infection of human dendritic cells by mosquito-cell-derived dengue viruses
    • Navarro-Sanchez E, Altmeyer R, Amara A, Schwartz O, Fieschi F, Virelizier JL, Arenzana-Seisdedos F, Despres P. 2003. Dendritic-cellspecific ICAM3-grabbing non-integrin is essential for the productive infection of human dendritic cells by mosquito-cell-derived dengue viruses. EMBO Rep 4:723-728. http://dx.doi.org/10.1038/sj.embor.embor866.
    • (2003) EMBO Rep , vol.4 , pp. 723-728
    • Navarro-Sanchez, E.1    Altmeyer, R.2    Amara, A.3    Schwartz, O.4    Fieschi, F.5    Virelizier, J.L.6    Arenzana-Seisdedos, F.7    Despres, P.8
  • 62
    • 33749266195 scopus 로고    scopus 로고
    • The Role of histidine residues in low-pH-mediated viral membrane fusion
    • Kampmann T, Mueller DS, Mark AE, Young PR, Kobe B. 2006. The Role of histidine residues in low-pH-mediated viral membrane fusion. Structure 14:1481-1487. http://dx.doi.org/10.1016/j.str.2006.07.011.
    • (2006) Structure , vol.14 , pp. 1481-1487
    • Kampmann, T.1    Mueller, D.S.2    Mark, A.E.3    Young, P.R.4    Kobe, B.5
  • 63
    • 80052302239 scopus 로고    scopus 로고
    • Mutational analysis of the zippering reaction during flavivirus membrane fusion
    • Pangerl K, Heinz FX, Stiasny K. 2011. Mutational analysis of the zippering reaction during flavivirus membrane fusion. J Virol 85:8495-8501. http://dx.doi.org/10.1128/JVI.05129-11.
    • (2011) J Virol , vol.85 , pp. 8495-8501
    • Pangerl, K.1    Heinz, F.X.2    Stiasny, K.3
  • 64
    • 84873849253 scopus 로고    scopus 로고
    • Structure of a dengue virus envelope protein late-stage fusion intermediate
    • Klein DE, Choi JL, Harrison SC. 2013. Structure of a dengue virus envelope protein late-stage fusion intermediate. J Virol 87:2287-2293. http://dx.doi.org/10.1128/JVI.02957-12.
    • (2013) J Virol , vol.87 , pp. 2287-2293
    • Klein, D.E.1    Choi, J.L.2    Harrison, S.C.3
  • 65
    • 77954044356 scopus 로고    scopus 로고
    • Peptide inhibitors of denguevirus entry target a late-stage fusion intermediate
    • Schmidt AG, Yang PL, Harrison SC. 2010. Peptide inhibitors of denguevirus entry target a late-stage fusion intermediate. PLoS Pathog 6:e1000851. http://dx.doi.org/10.1371/journal.ppat.1000851.
    • (2010) PLoS Pathog , vol.6
    • Schmidt, A.G.1    Yang, P.L.2    Harrison, S.C.3
  • 66
    • 23744446349 scopus 로고    scopus 로고
    • Peptide inhibitors of dengue virus and West Nile virus infectivity
    • Hrobowski YM, Garry RF, Michael SF. 2005. Peptide inhibitors of dengue virus and West Nile virus infectivity. Virol J 2:49. http://dx.doi.org/10.1186/1743-422X-2-49.
    • (2005) Virol J , vol.2 , pp. 49
    • Hrobowski, Y.M.1    Garry, R.F.2    Michael, S.F.3
  • 67
    • 3242705779 scopus 로고    scopus 로고
    • Common E protein determinants for attenuation of glycosaminoglycan-binding variants of Japanese encephalitis and West Nile viruses
    • Lee E, Hall RA, Lobigs M. 2004. Common E protein determinants for attenuation of glycosaminoglycan-binding variants of Japanese encephalitis and West Nile viruses. J Virol 78:8271-8280. http://dx.doi.org/10.1128/JVI.78.15.8271-8280.2004.
    • (2004) J Virol , vol.78 , pp. 8271-8280
    • Lee, E.1    Hall, R.A.2    Lobigs, M.3
  • 68
    • 0036239935 scopus 로고    scopus 로고
    • Mechanism of virulence attenuation of glycosaminoglycan-binding variants of Japanese encephalitis virus and Murray Valley encephalitis virus
    • Lee E, Lobigs M. 2002. Mechanism of virulence attenuation of glycosaminoglycan-binding variants of Japanese encephalitis virus and Murray Valley encephalitis virus. J Virol 76:4901-4911. http://dx.doi.org/10.1128/JVI.76.10.4901-4911.2002.
    • (2002) J Virol , vol.76 , pp. 4901-4911
    • Lee, E.1    Lobigs, M.2
  • 69
    • 84930342444 scopus 로고    scopus 로고
    • Progress in the identification of dengue virus entry/fusion inhibitors
    • 825039
    • De La Guardia C, Lleonart R. 2014. Progress in the identification of dengue virus entry/fusion inhibitors. Biomed Res Int 2014:825039. http://dx.doi.org/10.1155/2014/825039.
    • (2014) Biomed Res Int , vol.2014
    • De La Guardia, C.1    Lleonart, R.2

* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.