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Volumn 13, Issue 9, 2017, Pages

A novel mechanism of antibody-mediated enhancement of flavivirus infection

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY RESPONSE; ARTICLE; CELL MEMBRANE; CROSS LINKING; ENDOCYTOSIS; ENZYME LINKED IMMUNOSORBENT ASSAY; FLAVIVIRUS INFECTION; HUMAN; IMMUNOASSAY; POLYACRYLAMIDE GEL ELECTROPHORESIS; POLYMERASE CHAIN REACTION; VIROGENESIS; VIRUS ATTACHMENT; VIRUS INFECTIVITY; ANTIBODY DEPENDENT ENHANCEMENT; FLAVIVIRUS; IMMUNOLOGY; ISOLATION AND PURIFICATION; METABOLISM; TICK BORNE ENCEPHALITIS VIRUS; VIROLOGY;

EID: 85030455683     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1006643     Document Type: Article
Times cited : (55)

References (93)
  • 2
    • 84891594368 scopus 로고    scopus 로고
    • Flavivirus entry receptors: an update
    • 24381034, Epub 2014/01/02
    • Perera-Lecoin M, Meertens L, Carnec X, Amara A, Flavivirus entry receptors: an update. Viruses. 2014;6(1):69–88. Epub 2014/01/02. doi: 10.3390/v6010069 24381034
    • (2014) Viruses , vol.6 , Issue.1 , pp. 69-88
    • Perera-Lecoin, M.1    Meertens, L.2    Carnec, X.3    Amara, A.4
  • 4
    • 79952140351 scopus 로고    scopus 로고
    • Flavivirus cell entry and membrane fusion
    • 22049308, Epub 2011/11/04
    • Smit JM, Moesker B, Rodenhuis-Zybert I, Wilschut J, Flavivirus cell entry and membrane fusion. Viruses. 2011;3(2):160–71. Epub 2011/11/04. doi: 10.3390/v3020160 22049308
    • (2011) Viruses , vol.3 , Issue.2 , pp. 160-171
    • Smit, J.M.1    Moesker, B.2    Rodenhuis-Zybert, I.3    Wilschut, J.4
  • 5
    • 84937250748 scopus 로고    scopus 로고
    • Viral apoptotic mimicry
    • 2605266
    • Amara A, Mercer J, Viral apoptotic mimicry. Nat Rev Micro. 2015;13(8):461–9. doi: 10.1038/nrmicro3469 26052667
    • (2015) Nat Rev Micro , vol.13 , Issue.8 , pp. 461-469
    • Amara, A.1    Mercer, J.2
  • 6
    • 85011891106 scopus 로고    scopus 로고
    • Zika virus pathogenesis and tissue tropism
    • 2818294
    • Miner JJ, Diamond MS, Zika virus pathogenesis and tissue tropism. Cell Host Microbe. 2017;21(2):134–42. https://doi.org/10.1016/j.chom.2017.01.004. 28182948
    • (2017) Cell Host Microbe , vol.21 , Issue.2 , pp. 134-142
    • Miner, J.J.1    Diamond, M.S.2
  • 8
    • 0038201461 scopus 로고    scopus 로고
    • Structures of immature flavivirus particles
    • 1277337
    • Zhang Y, Corver J, Chipman PR, Zhang W, Pletnev SV, Sedlak D, et al. Structures of immature flavivirus particles. Embo J. 2003;22(11):2604–13. doi: 10.1093/emboj/cdg270 12773377.
    • (2003) Embo J , vol.22 , Issue.11 , pp. 2604-2613
    • Zhang, Y.1    Corver, J.2    Chipman, P.R.3    Zhang, W.4    Pletnev, S.V.5    Sedlak, D.6
  • 9
    • 41349112304 scopus 로고    scopus 로고
    • Structure of the immature dengue virus at low pH primes proteolytic maturation
    • 1836914
    • Yu IM, Zhang W, Holdaway HA, Li L, Kostyuchenko VA, Chipman PR, et al. Structure of the immature dengue virus at low pH primes proteolytic maturation. Science. 2008;319(5871):1834–7. doi: 10.1126/science.1153264 18369148.
    • (2008) Science , vol.319 , Issue.5871 , pp. 1834-1837
    • Yu, I.M.1    Zhang, W.2    Holdaway, H.A.3    Li, L.4    Kostyuchenko, V.A.5    Chipman, P.R.6
  • 10
    • 18344387519 scopus 로고    scopus 로고
    • Structure of dengue virus: implications for flavivirus organization, maturation, and fusion
    • 1189334
    • Kuhn RJ, Zhang W, Rossmann MG, Pletnev SV, Corver J, Lenches E, et al. Structure of dengue virus: implications for flavivirus organization, maturation, and fusion. Cell. 2002;108(5):717–25. 11893341
    • (2002) Cell , vol.108 , Issue.5 , pp. 717-725
    • Kuhn, R.J.1    Zhang, W.2    Rossmann, M.G.3    Pletnev, S.V.4    Corver, J.5    Lenches, E.6
  • 11
    • 0029014434 scopus 로고
    • The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution
    • 775319
    • Rey FA, Heinz FX, Mandl C, Kunz C, Harrison SC, The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution. Nature. 1995;375(6529):291–8. doi: 10.1038/375291a0 7753193.
    • (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
  • 12
    • 32044436044 scopus 로고    scopus 로고
    • Cryo-EM reconstruction of dengue virus in complex with the carbohydrate recognition domain of DC-SIGN
    • 16469696, Epub 2006/02/14
    • Pokidysheva E, Zhang Y, Battisti AJ, Bator-Kelly CM, Chipman PR, Xiao C, et al. Cryo-EM reconstruction of dengue virus in complex with the carbohydrate recognition domain of DC-SIGN. Cell. 2006;124(3):485–93. Epub 2006/02/14. doi: 10.1016/j.cell.2005.11.042 16469696.
    • (2006) Cell , vol.124 , Issue.3 , pp. 485-493
    • Pokidysheva, E.1    Zhang, Y.2    Battisti, A.J.3    Bator-Kelly, C.M.4    Chipman, P.R.5    Xiao, C.6
  • 13
    • 0021246654 scopus 로고
    • Flavivirus infection enhancement in macrophages: radioactive and biological studies on the effect of antibody on viral fate
    • 6086817, Epub 1984/08/01
    • Gollins SW, Porterfield JS, Flavivirus infection enhancement in macrophages: radioactive and biological studies on the effect of antibody on viral fate. J Gen Virol. 1984;65 (Pt 8):1261–72. Epub 1984/08/01. doi: 10.1099/0022-1317-65-8-1261 6086817.
    • (1984) J Gen Virol , vol.65 , pp. 1261-1272
    • Gollins, S.W.1    Porterfield, J.S.2
  • 14
    • 0022239808 scopus 로고
    • Flavivirus infection enhancement in macrophages: an electron microscopic study of viral cellular entry
    • 4031825, Epub 1985/09/01
    • Gollins SW, Porterfield JS, Flavivirus infection enhancement in macrophages: an electron microscopic study of viral cellular entry. J Gen Virol. 1985;66 (Pt 9):1969–82. Epub 1985/09/01. doi: 10.1099/0022-1317-66-9-1969 4031825.
    • (1985) J Gen Virol , vol.66 , pp. 1969-1982
    • Gollins, S.W.1    Porterfield, J.S.2
  • 15
    • 84978370298 scopus 로고    scopus 로고
    • How antibodies alter the cell entry pathway of dengue virus particles in macrophages
    • 27385443,..;:. Epub 2016/07/08
    • Ayala-Nunez NV, Hoornweg TE, van de Pol DP, Sjollema KA, Flipse J, van der Schaar HM, et al. How antibodies alter the cell entry pathway of dengue virus particles in macrophages. Sci Rep. 2016;6:28768. Epub 2016/07/08. doi: 10.1038/srep28768 27385443
    • (2016) Sci Rep , vol.6 , pp. 28768
    • Ayala-Nunez, N.V.1    Hoornweg, T.E.2    van de Pol, D.P.3    Sjollema, K.A.4    Flipse, J.5    van der Schaar, H.M.6
  • 16
    • 79952071242 scopus 로고    scopus 로고
    • Antibody-mediated neutralization of flaviviruses: a reductionist view
    • 21255816, Epub 2011/01/25
    • Dowd KA, Pierson TC, Antibody-mediated neutralization of flaviviruses: a reductionist view. Virology. 2011;411(2):306–15. Epub 2011/01/25. doi: 10.1016/j.virol.2010.12.020 21255816
    • (2011) Virology , vol.411 , Issue.2 , pp. 306-315
    • Dowd, K.A.1    Pierson, T.C.2
  • 17
    • 84932648347 scopus 로고    scopus 로고
    • Dengue antibody-dependent enhancement: Knowns and unknowns
    • 2610444
    • Halstead SB, Dengue antibody-dependent enhancement: Knowns and unknowns. Microbiol Spectr. 2014;2(6). doi: 10.1128/microbiolspec.AID-0022-2014 26104444
    • (2014) Microbiol Spectr , vol.2 , Issue.6
    • Halstead, S.B.1
  • 18
    • 84945307337 scopus 로고    scopus 로고
    • Fc receptors in antibody-dependent enhancement of viral infections
    • 2649753
    • Taylor A, Foo S-S, Bruzzone R, Vu Dinh L, King NJC, Mahalingam S, Fc receptors in antibody-dependent enhancement of viral infections. Immunol Rev. 2015;268(1):340–64. doi: 10.1111/imr.12367 26497532
    • (2015) Immunol Rev , vol.268 , Issue.1 , pp. 340-364
    • Taylor, A.1    Foo, S.-S.2    Bruzzone, R.3    Vu Dinh, L.4    King, N.J.C.5    Mahalingam, S.6
  • 19
    • 85015798173 scopus 로고    scopus 로고
    • Biologic evidence required for Zika disease enhancement by dengue antibodies
    • 2832269
    • Halstead SB, Biologic evidence required for Zika disease enhancement by dengue antibodies. Emerg Infect Dis. 2017;23(4):569–73. doi: 10.3201/eid2304.161879 28322690
    • (2017) Emerg Infect Dis , vol.23 , Issue.4 , pp. 569-573
    • Halstead, S.B.1
  • 20
    • 85016812015 scopus 로고    scopus 로고
    • Enhancement of Zika virus pathogenesis by preexisting antiflavivirus immunity
    • 2836013
    • Bardina SV, Bunduc P, Tripathi S, Duehr J, Frere JJ, Brown JA, et al. Enhancement of Zika virus pathogenesis by preexisting antiflavivirus immunity. Science. 2017;356(6334):175. doi: 10.1126/science.aal4365 28360135
    • (2017) Science , vol.356 , Issue.6334 , pp. 175
    • Bardina, S.V.1    Bunduc, P.2    Tripathi, S.3    Duehr, J.4    Frere, J.J.5    Brown, J.A.6
  • 21
    • 84948706705 scopus 로고    scopus 로고
    • New insights into the immunopathology and control of dengue virus infection
    • 26603900, Epub 2015/11/26
    • Screaton G, Mongkolsapaya J, Yacoub S, Roberts C, New insights into the immunopathology and control of dengue virus infection. Nat Rev Immunol. 2015;15(12):745–59. Epub 2015/11/26. doi: 10.1038/nri3916 26603900.
    • (2015) Nat Rev Immunol , vol.15 , Issue.12 , pp. 745-759
    • Screaton, G.1    Mongkolsapaya, J.2    Yacoub, S.3    Roberts, C.4
  • 22
    • 84937511919 scopus 로고    scopus 로고
    • Shake, rattle, and roll: Impact of the dynamics of flavivirus particles on their interactions with the host
    • 2583572
    • Kuhn RJ, Dowd KA, Beth Post C, Pierson TC, Shake, rattle, and roll: Impact of the dynamics of flavivirus particles on their interactions with the host. Virology. 2015;479–480:508–17. doi: 10.1016/j.virol.2015.03.025 25835729
    • (2015) Virology , vol.479-480 , pp. 508-517
    • Kuhn, R.J.1    Dowd, K.A.2    Beth Post, C.3    Pierson, T.C.4
  • 23
    • 84876842073 scopus 로고    scopus 로고
    • Dengue structure differs at the temperatures of its human and mosquito hosts
    • 23569243, Epub 2013/04/10
    • Zhang X, Sheng J, Plevka P, Kuhn RJ, Diamond MS, Rossmann MG, Dengue structure differs at the temperatures of its human and mosquito hosts. Proc Natl Acad Sci U S A. 2013;110(17):6795–9. Epub 2013/04/10. doi: 10.1073/pnas.1304300110 23569243
    • (2013) Proc Natl Acad Sci U S A , vol.110 , Issue.17 , pp. 6795-6799
    • Zhang, X.1    Sheng, J.2    Plevka, P.3    Kuhn, R.J.4    Diamond, M.S.5    Rossmann, M.G.6
  • 24
    • 84880395430 scopus 로고    scopus 로고
    • Structural changes in dengue virus when exposed to a temperature of 37°C
    • 23637405, Epub 2013/05/03
    • Fibriansah G, Ng TS, Kostyuchenko VA, Lee J, Lee S, Wang J, et al. Structural changes in dengue virus when exposed to a temperature of 37°C. J Virol. 2013;87(13):7585–92. Epub 2013/05/03. doi: 10.1128/JVI.00757-13 23637405.
    • (2013) J Virol , vol.87 , Issue.13 , pp. 7585-7592
    • Fibriansah, G.1    Ng, T.S.2    Kostyuchenko, V.A.3    Lee, J.4    Lee, S.5    Wang, J.6
  • 25
    • 40949161794 scopus 로고    scopus 로고
    • Binding of a neutralizing antibody to dengue virus alters the arrangement of surface glycoproteins
    • 1826411
    • Lok SM, Kostyuchenko V, Nybakken GE, Holdaway HA, Battisti AJ, Sukupolvi-Petty S, et al. Binding of a neutralizing antibody to dengue virus alters the arrangement of surface glycoproteins. Nat Struct Mol Biol. 2008;15(3):312–7. doi: 10.1038/nsmb.1382 18264114.
    • (2008) Nat Struct Mol Biol , vol.15 , Issue.3 , pp. 312-317
    • Lok, S.M.1    Kostyuchenko, V.2    Nybakken, G.E.3    Holdaway, H.A.4    Battisti, A.J.5    Sukupolvi-Petty, S.6
  • 26
    • 84868111424 scopus 로고    scopus 로고
    • Structural basis of differential neutralization of DENV-1 genotypes by an antibody that recognizes a cryptic epitope
    • 23055922,..; ():. Epub 2012/10/12
    • Austin SK, Dowd KA, Shrestha B, Nelson CA, Edeling MA, Johnson S, et al. Structural basis of differential neutralization of DENV-1 genotypes by an antibody that recognizes a cryptic epitope. PLoS pathogens. 2012;8(10):e1002930. Epub 2012/10/12. doi: 10.1371/journal.ppat.1002930 23055922
    • (2012) PLoS pathogens , vol.8 , Issue.10 , pp. e1002930
    • Austin, S.K.1    Dowd, K.A.2    Shrestha, B.3    Nelson, C.A.4    Edeling, M.A.5    Johnson, S.6
  • 27
    • 84856689479 scopus 로고    scopus 로고
    • Mechanism of dengue virus broad cross-neutralization by a monoclonal antibody
    • 2228521
    • Cockburn JJ, Navarro Sanchez ME, Fretes N, Urvoas A, Staropoli I, Kikuti CM, et al. Mechanism of dengue virus broad cross-neutralization by a monoclonal antibody. Structure. 2012;20(2):303–14. doi: 10.1016/j.str.2012.01.001 22285214.
    • (2012) Structure , vol.20 , Issue.2 , pp. 303-314
    • Cockburn, J.J.1    Navarro Sanchez, M.E.2    Fretes, N.3    Urvoas, A.4    Staropoli, I.5    Kikuti, C.M.6
  • 28
    • 84937761010 scopus 로고    scopus 로고
    • Viral membrane fusion
    • 2586637
    • Harrison SC, Viral membrane fusion. Virology. 2015;479–480:498–507. doi: 10.1016/j.virol.2015.03.043 25866377
    • (2015) Virology , vol.479-480 , pp. 498-507
    • Harrison, S.C.1
  • 29
    • 84963657108 scopus 로고    scopus 로고
    • Fusion of enveloped viruses in endosomes
    • 2693585
    • White JM, Whittaker GR, Fusion of enveloped viruses in endosomes. Traffic. 2016;17(6):593–614. doi: 10.1111/tra.12389 26935856
    • (2016) Traffic , vol.17 , Issue.6 , pp. 593-614
    • White, J.M.1    Whittaker, G.R.2
  • 30
    • 42749088709 scopus 로고    scopus 로고
    • Antibody-dependent enhancement of adeno-associated virus infection of human monocytic cell lines
    • 18295295, Epub 2008/02/26
    • Mori S, Takeuchi T, Kanda T, Antibody-dependent enhancement of adeno-associated virus infection of human monocytic cell lines. Virology. 2008;375(1):141–7. Epub 2008/02/26. doi: 10.1016/j.virol.2008.01.033 18295295.
    • (2008) Virology , vol.375 , Issue.1 , pp. 141-147
    • Mori, S.1    Takeuchi, T.2    Kanda, T.3
  • 31
    • 85013896724 scopus 로고    scopus 로고
    • Mechanism of human rhinovirus infections
    • 27251607,.; ():. Epub 2016/06/03
    • Blaas D, Fuchs R, Mechanism of human rhinovirus infections. Mol Cell Pediatr. 2016;3(1):21. Epub 2016/06/03. doi: 10.1186/s40348-016-0049-3 27251607
    • (2016) Mol Cell Pediatr , vol.3 , Issue.1 , pp. 21
    • Blaas, D.1    Fuchs, R.2
  • 32
    • 0015266198 scopus 로고
    • Early interaction of rhinoviruses with host cells
    • 433354
    • Lonberg-Holm K, Korant BD, Early interaction of rhinoviruses with host cells. J Virol. 1972;9(1):29–40. 4333543
    • (1972) J Virol , vol.9 , Issue.1 , pp. 29-40
    • Lonberg-Holm, K.1    Korant, B.D.2
  • 33
    • 2942635082 scopus 로고    scopus 로고
    • Identification of the human rhinovirus serotype 1A binding site on the murine low-density lipoprotein receptor by using human-mouse receptor chimeras
    • 15194751, Epub 2004/06/15
    • Herdy B, Snyers L, Reithmayer M, Hinterdorfer P, Blaas D, Identification of the human rhinovirus serotype 1A binding site on the murine low-density lipoprotein receptor by using human-mouse receptor chimeras. J Virol. 2004;78(13):6766–74. Epub 2004/06/15. doi: 10.1128/JVI.78.13.6766-6774.2004 15194751
    • (2004) J Virol , vol.78 , Issue.13 , pp. 6766-6774
    • Herdy, B.1    Snyers, L.2    Reithmayer, M.3    Hinterdorfer, P.4    Blaas, D.5
  • 34
  • 35
    • 78650710149 scopus 로고    scopus 로고
    • Subversion of innate defenses by the interplay between DENV and pre-existing enhancing antibodies: TLRs signaling collapse
    • 2120042
    • Modhiran N, Kalayanarooj S, Ubol S, Subversion of innate defenses by the interplay between DENV and pre-existing enhancing antibodies: TLRs signaling collapse. PLoS Negl Trop Dis. 2010;4(12):e924. doi: 10.1371/journal.pntd.0000924 21200427
    • (2010) PLoS Negl Trop Dis , vol.4 , Issue.12 , pp. e924
    • Modhiran, N.1    Kalayanarooj, S.2    Ubol, S.3
  • 36
    • 0025921573 scopus 로고
    • Biology of human immunoglobulin G Fc receptors
    • 182672
    • van de Winkel JG, Anderson CL, Biology of human immunoglobulin G Fc receptors. J Leukoc Biol. 1991;49(5):511–24. 1826726
    • (1991) J Leukoc Biol , vol.49 , Issue.5 , pp. 511-524
    • van de Winkel, J.G.1    Anderson, C.L.2
  • 37
    • 10044263508 scopus 로고    scopus 로고
    • Localization and characterization of flavivirus envelope glycoprotein cross-reactive epitopes
    • 1556450
    • Crill WD, Chang G-JJ, Localization and characterization of flavivirus envelope glycoprotein cross-reactive epitopes. J Virol. 2004;78(24):13975–86. doi: 10.1128/JVI.78.24.13975-13986.2004 15564505
    • (2004) J Virol , vol.78 , Issue.24 , pp. 13975-13986
    • Crill, W.D.1    Chang, G.-J.J.2
  • 38
    • 33748948792 scopus 로고    scopus 로고
    • Cryptic properties of a cluster of dominant flavivirus cross-reactive antigenic sites
    • 16973559, Epub 2006/09/16
    • Stiasny K, Kiermayr S, Holzmann H, Heinz FX, Cryptic properties of a cluster of dominant flavivirus cross-reactive antigenic sites. J Virol. 2006;80(19):9557–68. Epub 2006/09/16. doi: 10.1128/JVI.00080-06 16973559
    • (2006) J Virol , vol.80 , Issue.19 , pp. 9557-9568
    • Stiasny, K.1    Kiermayr, S.2    Holzmann, H.3    Heinz, F.X.4
  • 39
    • 0026094713 scopus 로고
    • The flavivirus envelope protein E: isolation of a soluble form from tick-borne encephalitis virus and its crystallization
    • 171669
    • Heinz FX, Mandl CW, Holzmann H, Kunz C, Harris BA, Rey F, et al. The flavivirus envelope protein E: isolation of a soluble form from tick-borne encephalitis virus and its crystallization. J Virol. 1991;65(10):5579–83. 1716695.
    • (1991) J Virol , vol.65 , Issue.10 , pp. 5579-5583
    • Heinz, F.X.1    Mandl, C.W.2    Holzmann, H.3    Kunz, C.4    Harris, B.A.5    Rey, F.6
  • 40
    • 84937686924 scopus 로고    scopus 로고
    • Immunization with immune complexes modulates the fine specificity of antibody responses to a flavivirus antigen
    • 26018152, Epub 2015/05/29
    • Tsouchnikas G, Zlatkovic J, Jarmer J, Strauss J, Vratskikh O, Kundi M, et al. Immunization with immune complexes modulates the fine specificity of antibody responses to a flavivirus antigen. J Virol. 2015;89(15):7970–8. Epub 2015/05/29. doi: 10.1128/JVI.00938-15 26018152
    • (2015) J Virol , vol.89 , Issue.15 , pp. 7970-7978
    • Tsouchnikas, G.1    Zlatkovic, J.2    Jarmer, J.3    Strauss, J.4    Vratskikh, O.5    Kundi, M.6
  • 41
    • 33847246763 scopus 로고    scopus 로고
    • Characterization of a structural intermediate of flavivirus membrane fusion
    • 17305426,.; ():. Epub 2007/02/20
    • Stiasny K, Kossl C, Lepault J, Rey FA, Heinz FX, Characterization of a structural intermediate of flavivirus membrane fusion. PLoS Pathog. 2007;3(2):e20. Epub 2007/02/20. doi: 10.1371/journal.ppat.0030020 17305426
    • (2007) PLoS Pathog , vol.3 , Issue.2 , pp. e20
    • Stiasny, K.1    Kossl, C.2    Lepault, J.3    Rey, F.A.4    Heinz, F.X.5
  • 42
    • 35148859259 scopus 로고    scopus 로고
    • Probing the flavivirus membrane fusion mechanism by using monoclonal antibodies
    • 1767082
    • Stiasny K, Brandler S, Kossl C, Heinz FX, Probing the flavivirus membrane fusion mechanism by using monoclonal antibodies. J Virol. 2007;81(20):11526–31. doi: 10.1128/JVI.01041-07 17670824
    • (2007) J Virol , vol.81 , Issue.20 , pp. 11526-11531
    • Stiasny, K.1    Brandler, S.2    Kossl, C.3    Heinz, F.X.4
  • 43
    • 0035051804 scopus 로고    scopus 로고
    • Mutational evidence for an internal fusion peptide in flavivirus envelope protein E
    • 1128757
    • Allison SL, Schalich J, Stiasny K, Mandl CW, Heinz FX, Mutational evidence for an internal fusion peptide in flavivirus envelope protein E. J Virol. 2001;75(9):4268–75. doi: 10.1128/JVI.75.9.4268-4275.2001 11287576.
    • (2001) J Virol , vol.75 , Issue.9 , pp. 4268-4275
    • Allison, S.L.1    Schalich, J.2    Stiasny, K.3    Mandl, C.W.4    Heinz, F.X.5
  • 44
    • 70350347088 scopus 로고    scopus 로고
    • Structural basis for the preferential recognition of immature flaviviruses by a fusion-loop antibody
    • 1971393
    • Cherrier MV, Kaufmann B, Nybakken GE, Lok SM, Warren JT, Chen BR, et al. Structural basis for the preferential recognition of immature flaviviruses by a fusion-loop antibody. EMBO J. 2009;28(20):3269–76. doi: 10.1038/emboj.2009.245 19713934
    • (2009) EMBO J , vol.28 , Issue.20 , pp. 3269-3276
    • Cherrier, M.V.1    Kaufmann, B.2    Nybakken, G.E.3    Lok, S.M.4    Warren, J.T.5    Chen, B.R.6
  • 45
    • 0034732136 scopus 로고    scopus 로고
    • Membrane fusion activity of tick-borne encephalitis virus and recombinant subviral particles in a liposomal model system
    • 1072519
    • Corver J, Ortiz A, Allison SL, Schalich J, Heinz FX, Wilschut J, Membrane fusion activity of tick-borne encephalitis virus and recombinant subviral particles in a liposomal model system. Virology. 2000;269(1):37–46. doi: 10.1006/viro.1999.0172 10725196.
    • (2000) Virology , vol.269 , Issue.1 , pp. 37-46
    • Corver, J.1    Ortiz, A.2    Allison, S.L.3    Schalich, J.4    Heinz, F.X.5    Wilschut, J.6
  • 46
    • 0034903691 scopus 로고    scopus 로고
    • Role of metastability and acidic pH in membrane fusion by tick-borne encephalitis virus
    • 1146201
    • Stiasny K, Allison SL, Mandl CW, Heinz FX, Role of metastability and acidic pH in membrane fusion by tick-borne encephalitis virus. J Virol. 2001;75(16):7392–8. doi: 10.1128/JVI.75.16.7392-7398.2001 11462011.
    • (2001) J Virol , vol.75 , Issue.16 , pp. 7392-7398
    • Stiasny, K.1    Allison, S.L.2    Mandl, C.W.3    Heinz, F.X.4
  • 47
    • 33845389501 scopus 로고    scopus 로고
    • Antibody recognition and neutralization determinants on domains I and II of West Nile Virus envelope protein
    • 17035317, Epub 2006/10/13
    • Oliphant T, Nybakken GE, Engle M, Xu Q, Nelson CA, Sukupolvi-Petty S, et al. Antibody recognition and neutralization determinants on domains I and II of West Nile Virus envelope protein. J Virol. 2006;80(24):12149–59. Epub 2006/10/13. doi: 10.1128/JVI.01732-06 17035317
    • (2006) J Virol , vol.80 , Issue.24 , pp. 12149-12159
    • Oliphant, T.1    Nybakken, G.E.2    Engle, M.3    Xu, Q.4    Nelson, C.A.5    Sukupolvi-Petty, S.6
  • 48
    • 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
    • 1146205
    • Crill WD, Roehrig JT, 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. 2001;75(16):7769–73. doi: 10.1128/JVI.75.16.7769-7773.2001 11462053
    • (2001) J Virol , vol.75 , Issue.16 , pp. 7769-7773
    • Crill, W.D.1    Roehrig, J.T.2
  • 49
    • 84907979176 scopus 로고    scopus 로고
    • Isolation of dengue virus-specific memory B cells with live virus antigen from human subjects following natural infection reveals the presence of diverse novel functional groups of antibody clones
    • 2510083
    • Smith SA, de Alwis AR, Kose N, Jadi RS, de Silva AM, Crowe JE, Isolation of dengue virus-specific memory B cells with live virus antigen from human subjects following natural infection reveals the presence of diverse novel functional groups of antibody clones. J Virol. 2014;88(21):12233–41. doi: 10.1128/JVI.00247-14 25100837
    • (2014) J Virol , vol.88 , Issue.21 , pp. 12233-12241
    • Smith, S.A.1    de Alwis, A.R.2    Kose, N.3    Jadi, R.S.4    de Silva, A.M.5    Crowe, J.E.6
  • 50
    • 70349199877 scopus 로고    scopus 로고
    • A structural and functional perspective of alphavirus replication and assembly
    • 1972283
    • Jose J, Snyder JE, Kuhn RJ, A structural and functional perspective of alphavirus replication and assembly. Future microbiology. 2009;4:837–56. doi: 10.2217/fmb.09.59 19722838
    • (2009) Future microbiology , vol.4 , pp. 837-856
    • Jose, J.1    Snyder, J.E.2    Kuhn, R.J.3
  • 51
    • 0024076645 scopus 로고
    • Antibody-mediated activation of sindbis virus
    • 341398
    • Flynn DC, Olmsted RA, Mackenzie JM, Johnston RE, Antibody-mediated activation of sindbis virus. Virology. 1988;166(1):82–90. http://dx.doi.org/10.1016/0042-6822(88)90149-3. 3413988
    • (1988) Virology , vol.166 , Issue.1 , pp. 82-90
    • Flynn, D.C.1    Olmsted, R.A.2    Mackenzie, J.M.3    Johnston, R.E.4
  • 52
    • 84952836886 scopus 로고    scopus 로고
    • Genotypic differences in dengue virus neutralization are explained by a single amino acid mutation that modulates virus breathing
    • 2653038
    • Dowd KA, DeMaso CR, Pierson TC, Genotypic differences in dengue virus neutralization are explained by a single amino acid mutation that modulates virus breathing. MBio. 2015;6(6):e01559–15. doi: 10.1128/mBio.01559-15 26530385
    • (2015) MBio , vol.6 , Issue.6 , pp. e01515-e01559
    • Dowd, K.A.1    DeMaso, C.R.2    Pierson, T.C.3
  • 53
    • 85014072004 scopus 로고    scopus 로고
    • A single mutation in the envelope protein modulates flavivirus antigenicity, stability, and pathogenesis
    • 2820791
    • Goo L, VanBlargan LA, Dowd KA, Diamond MS, Pierson TC, A single mutation in the envelope protein modulates flavivirus antigenicity, stability, and pathogenesis. PLoS Pathogens. 2017;13(2):e1006178. doi: 10.1371/journal.ppat.1006178 28207910
    • (2017) PLoS Pathogens , vol.13 , Issue.2 , pp. e1006178
    • Goo, L.1    VanBlargan, L.A.2    Dowd, K.A.3    Diamond, M.S.4    Pierson, T.C.5
  • 54
    • 84964799152 scopus 로고    scopus 로고
    • Evolutionarily successful Asian 1 dengue virus 2 lineages contain one substitution in envelope that increases sensitivity to polyclonal antibody neutralization
    • 2658295
    • Wang C, Katzelnick LC, Montoya M, Hue KDT, Simmons CP, Harris E, Evolutionarily successful Asian 1 dengue virus 2 lineages contain one substitution in envelope that increases sensitivity to polyclonal antibody neutralization. J Infect Dis. 2016;213(6):975–84. doi: 10.1093/infdis/jiv536 26582957
    • (2016) J Infect Dis , vol.213 , Issue.6 , pp. 975-984
    • Wang, C.1    Katzelnick, L.C.2    Montoya, M.3    Hue, K.D.T.4    Simmons, C.P.5    Harris, E.6
  • 55
    • 33644549138 scopus 로고    scopus 로고
    • The dual-specific binding of dengue virus and target cells for the antibody-dependent enhancement of dengue virus infection
    • 16493039, Epub 2006/02/24
    • Huang KJ, Yang YC, Lin YS, Huang JH, Liu HS, Yeh TM, et al. The dual-specific binding of dengue virus and target cells for the antibody-dependent enhancement of dengue virus infection. J Immunol. 2006;176(5):2825–32. Epub 2006/02/24. 16493039.
    • (2006) J Immunol , vol.176 , Issue.5 , pp. 2825-2832
    • Huang, K.J.1    Yang, Y.C.2    Lin, Y.S.3    Huang, J.H.4    Liu, H.S.5    Yeh, T.M.6
  • 56
    • 0021345838 scopus 로고
    • Antibody-induced conformational changes result in enhanced avidity of antibodies to different antigenic sites on the tick-borne encephalitis virus glycoprotein
    • 6199892, Epub 1984/02/01
    • Heinz FX, Mandl C, Berger R, Tuma W, Kunz C, Antibody-induced conformational changes result in enhanced avidity of antibodies to different antigenic sites on the tick-borne encephalitis virus glycoprotein. Virology. 1984;133(1):25–34. Epub 1984/02/01. 6199892.
    • (1984) Virology , vol.133 , Issue.1 , pp. 25-34
    • Heinz, F.X.1    Mandl, C.2    Berger, R.3    Tuma, W.4    Kunz, C.5
  • 57
    • 0021998750 scopus 로고
    • Epitopic analysis of antigenic determinants on the surface of dengue-2 virions using monoclonal antibodies
    • 257875
    • Henchal EA, McCown JM, Burke DS, Seguin MC, Brandt WE, Epitopic analysis of antigenic determinants on the surface of dengue-2 virions using monoclonal antibodies. Am J Trop Med Hyg. 1985;34(1):162–9. 2578750
    • (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
  • 58
    • 0024548815 scopus 로고
    • Antigenic structure of the flavivirus envelope protein E at the molecular level, using tick-borne encephalitis virus as a model
    • 246337
    • Mandl CW, Guirakhoo F, Holzmann H, Heinz FX, Kunz C, Antigenic structure of the flavivirus envelope protein E at the molecular level, using tick-borne encephalitis virus as a model. J Virol. 1989;63(2):564–71. 2463377.
    • (1989) J Virol , vol.63 , Issue.2 , pp. 564-571
    • Mandl, C.W.1    Guirakhoo, F.2    Holzmann, H.3    Heinz, F.X.4    Kunz, C.5
  • 59
    • 69249221492 scopus 로고    scopus 로고
    • Impact of quaternary organization on the antigenic structure of the tick-borne encephalitis virus envelope glycoprotein E
    • 19553320, Epub 2009/06/26
    • Kiermayr S, Stiasny K, Heinz FX, Impact of quaternary organization on the antigenic structure of the tick-borne encephalitis virus envelope glycoprotein E. J Virol. 2009;83(17):8482–91. Epub 2009/06/26. doi: 10.1128/JVI.00660-09 19553320
    • (2009) J Virol , vol.83 , Issue.17 , pp. 8482-8491
    • Kiermayr, S.1    Stiasny, K.2    Heinz, F.X.3
  • 60
    • 84957603435 scopus 로고    scopus 로고
    • The development of therapeutic antibodies against dengue virus
    • 2679439
    • Fibriansah G, Lok SM, The development of therapeutic antibodies against dengue virus. Antiviral Res. 2016;128:7–19. doi: 10.1016/j.antiviral.2016.01.002 26794397.
    • (2016) Antiviral Res , vol.128 , pp. 7-19
    • Fibriansah, G.1    Lok, S.M.2
  • 61
    • 55949108725 scopus 로고    scopus 로고
    • Identification of specific histidines as pH sensors in flavivirus membrane fusion
    • 1893625
    • Fritz R, Stiasny K, Heinz FX, Identification of specific histidines as pH sensors in flavivirus membrane fusion. J Cell Biol. 2008;183(2):353–61. doi: 10.1083/jcb.200806081 18936253.
    • (2008) J Cell Biol , vol.183 , Issue.2 , pp. 353-361
    • Fritz, R.1    Stiasny, K.2    Heinz, F.X.3
  • 62
    • 84919470479 scopus 로고    scopus 로고
    • Dendritic cells in dengue virus infection: targets of virus replication and mediators of immunity
    • 25566258,.;:. Epub 2015/01/08
    • Schmid MA, Diamond MS, Harris E, Dendritic cells in dengue virus infection: targets of virus replication and mediators of immunity. Front Immunol. 2014;5:647. Epub 2015/01/08. doi: 10.3389/fimmu.2014.00647 25566258
    • (2014) Front Immunol , vol.5 , pp. 647
    • Schmid, M.A.1    Diamond, M.S.2    Harris, E.3
  • 63
    • 0025116324 scopus 로고
    • Flavivirus genome organization, expression, and replication
    • 2174669,.;: –. Epub 1990/01/01
    • Chambers TJ, Hahn CS, Galler R, Rice CM, Flavivirus genome organization, expression, and replication. Annu Rev Microbiol. 1990;44:649–88. Epub 1990/01/01. doi: 10.1146/annurev.mi.44.100190.003245 2174669.
    • (1990) Annu Rev Microbiol , vol.44 , pp. 649-688
    • Chambers, T.J.1    Hahn, C.S.2    Galler, R.3    Rice, C.M.4
  • 64
    • 35448960873 scopus 로고    scopus 로고
    • Characterization of the early events in dengue virus cell entry by biochemical assays and single-virus tracking
    • 17728239, Epub 2007/08/31
    • van der Schaar HM, Rust MJ, Waarts BL, van der Ende-Metselaar H, Kuhn RJ, Wilschut J, et al. Characterization of the early events in dengue virus cell entry by biochemical assays and single-virus tracking. J Virol. 2007;81(21):12019–28. Epub 2007/08/31. doi: 10.1128/JVI.00300-07 17728239
    • (2007) J Virol , vol.81 , Issue.21 , pp. 12019-12028
    • van der Schaar, H.M.1    Rust, M.J.2    Waarts, B.L.3    van der Ende-Metselaar, H.4    Kuhn, R.J.5    Wilschut, J.6
  • 65
    • 84879548698 scopus 로고    scopus 로고
    • Dissection of antibody specificities induced by yellow fever vaccination
    • 23818856,..; ():. Epub 2013/07/03
    • Vratskikh O, Stiasny K, Zlatkovic J, Tsouchnikas G, Jarmer J, Karrer U, et al. Dissection of antibody specificities induced by yellow fever vaccination. PLoS Pathog. 2013;9(6):e1003458. Epub 2013/07/03. doi: 10.1371/journal.ppat.1003458 23818856.
    • (2013) PLoS Pathog , vol.9 , Issue.6 , pp. e1003458
    • Vratskikh, O.1    Stiasny, K.2    Zlatkovic, J.3    Tsouchnikas, G.4    Jarmer, J.5    Karrer, U.6
  • 66
    • 84911428961 scopus 로고    scopus 로고
    • Variation of the specificity of the human antibody responses after tick-borne encephalitis virus infection and vaccination
    • 2525334
    • Jarmer J, Zlatkovic J, Tsouchnikas G, Vratskikh O, Strauss J, Aberle JH, et al. Variation of the specificity of the human antibody responses after tick-borne encephalitis virus infection and vaccination. J Virol. 2014;88(23):13845–57. doi: 10.1128/JVI.02086-14 25253341.
    • (2014) J Virol , vol.88 , Issue.23 , pp. 13845-13857
    • Jarmer, J.1    Zlatkovic, J.2    Tsouchnikas, G.3    Vratskikh, O.4    Strauss, J.5    Aberle, J.H.6
  • 67
    • 64249106079 scopus 로고    scopus 로고
    • Humoral immune responses of dengue fever patients using epitope-specific serotype-2 virus-like particle antigens
    • 1933737
    • Crill WD, Hughes HR, Delorey MJ, Chang G-JJ, Humoral immune responses of dengue fever patients using epitope-specific serotype-2 virus-like particle antigens. PLoS One. 2009;4(4):e4991. doi: 10.1371/journal.pone.0004991 19337372
    • (2009) PLoS One , vol.4 , Issue.4 , pp. e4991
    • Crill, W.D.1    Hughes, H.R.2    Delorey, M.J.3    Chang, G.-J.J.4
  • 68
    • 84931081889 scopus 로고    scopus 로고
    • Complexity of neutralizing antibodies against multiple dengue virus serotypes after heterotypic immunization and secondary infection revealed by in-depth analysis of cross-reactive antibodies
    • 2597255
    • Tsai W-Y, Durbin A, Tsai J-J, Hsieh S-C, Whitehead S, Wang W-K, Complexity of neutralizing antibodies against multiple dengue virus serotypes after heterotypic immunization and secondary infection revealed by in-depth analysis of cross-reactive antibodies. J Virol. 2015;89(14):7348–62. doi: 10.1128/JVI.00273-15 25972550
    • (2015) J Virol , vol.89 , Issue.14 , pp. 7348-7362
    • Tsai, W.-Y.1    Durbin, A.2    Tsai, J.-J.3    Hsieh, S.-C.4    Whitehead, S.5    Wang, W.-K.6
  • 69
    • 85000961951 scopus 로고    scopus 로고
    • Protective capacity of the human anamnestic antibody response during acute dengue virus infection
    • 2770793
    • Xu M, Züst R, Toh YX, Pfaff JM, Kahle KM, Davidson E, et al. Protective capacity of the human anamnestic antibody response during acute dengue virus infection. J Virol. 2016;90(24):11122–31. doi: 10.1128/JVI.01096-16 27707930
    • (2016) J Virol , vol.90 , Issue.24 , pp. 11122-11131
    • Xu, M.1    Züst, R.2    Toh, Y.X.3    Pfaff, J.M.4    Kahle, K.M.5    Davidson, E.6
  • 70
    • 85042675338 scopus 로고    scopus 로고
    • Zika virus activates de novo and cross-reactive memory B cell responses in dengue-experienced donors
    • Rogers TF, Goodwin EC, Briney B, Sok D, Beutler N, Strubel A, et al. Zika virus activates de novo and cross-reactive memory B cell responses in dengue-experienced donors. Science Immunology. 2017;2(14).
    • (2017) Science Immunology , vol.2 , Issue.14
    • Rogers, T.F.1    Goodwin, E.C.2    Briney, B.3    Sok, D.4    Beutler, N.5    Strubel, A.6
  • 71
    • 85021637743 scopus 로고    scopus 로고
    • Flavivirus structural heterogeneity: implications for cell entry
    • 2868339
    • Rey FA, Stiasny K, Heinz FX, Flavivirus structural heterogeneity: implications for cell entry. Curr Opin Virol. 2017;24:132–9. https://doi.org/10.1016/j.coviro.2017.06.009. 28683393
    • (2017) Curr Opin Virol , vol.24 , pp. 132-139
    • Rey, F.A.1    Stiasny, K.2    Heinz, F.X.3
  • 72
    • 0028289244 scopus 로고
    • Efficient presentation of soluble antigen by cultured human dendritic cells is maintained by granulocyte/macrophage colony-stimulating factor plus interleukin 4 and downregulated by tumor necrosis factor alpha
    • 8145033, Epub 1994/04/01
    • Sallusto F, Lanzavecchia A, Efficient presentation of soluble antigen by cultured human dendritic cells is maintained by granulocyte/macrophage colony-stimulating factor plus interleukin 4 and downregulated by tumor necrosis factor alpha. J Exp Med. 1994;179(4):1109–18. Epub 1994/04/01. 8145033
    • (1994) J Exp Med , vol.179 , Issue.4 , pp. 1109-1118
    • Sallusto, F.1    Lanzavecchia, A.2
  • 73
    • 84902353893 scopus 로고    scopus 로고
    • Immature dengue virus is infectious in human immature dendritic cells via interaction with the receptor molecule DC-SIGN
    • 24886790,..; ():. Epub 2014/06/03
    • Richter MK, da Silva Voorham JM, Torres Pedraza S, Hoornweg TE, van de Pol DP, Rodenhuis-Zybert IA, et al. Immature dengue virus is infectious in human immature dendritic cells via interaction with the receptor molecule DC-SIGN. PLoS One. 2014;9(6):e98785. Epub 2014/06/03. doi: 10.1371/journal.pone.0098785 24886790
    • (2014) PLoS One , vol.9 , Issue.6 , pp. e98785
    • Richter, M.K.1    da Silva Voorham, J.M.2    Torres Pedraza, S.3    Hoornweg, T.E.4    van de Pol, D.P.5    Rodenhuis-Zybert, I.A.6
  • 74
    • 84893631966 scopus 로고    scopus 로고
    • Langerhans cell maturation is accompanied by induction of N-cadherin and the transcriptional regulators of epithelial—mesenchymal transition ZEB1/2
    • 2416596
    • Konradi S, Yasmin N, Haslwanter D, Weber M, Gesslbauer B, Sixt M, et al. Langerhans cell maturation is accompanied by induction of N-cadherin and the transcriptional regulators of epithelial—mesenchymal transition ZEB1/2. Eur J Immunol. 2014;44(2):553–60. doi: 10.1002/eji.201343681 24165969
    • (2014) Eur J Immunol , vol.44 , Issue.2 , pp. 553-560
    • Konradi, S.1    Yasmin, N.2    Haslwanter, D.3    Weber, M.4    Gesslbauer, B.5    Sixt, M.6
  • 75
    • 0019835410 scopus 로고
    • Homogeneity of the structural glycoprotein from European isolates of tick-borne encephalitis virus: comparison with other flaviviruses
    • 6172553, Epub 1981/12/01
    • Heinz FX, Kunz C, Homogeneity of the structural glycoprotein from European isolates of tick-borne encephalitis virus: comparison with other flaviviruses. J Gen Virol. 1981;57(Pt 2):263–74. Epub 1981/12/01. doi: 10.1099/0022-1317-57-2-263 6172553.
    • (1981) J Gen Virol , vol.57 , pp. 263-274
    • Heinz, F.X.1    Kunz, C.2
  • 76
    • 0028278395 scopus 로고
    • Structural changes and functional control of the tick-borne encephalitis virus glycoprotein E by the heterodimeric association with protein prM
    • 8259646, Epub 1994/01/01
    • Heinz FX, Stiasny K, Puschner-Auer G, Holzmann H, Allison SL, Mandl CW, et al. Structural changes and functional control of the tick-borne encephalitis virus glycoprotein E by the heterodimeric association with protein prM. Virology. 1994;198(1):109–17. Epub 1994/01/01. doi: 10.1006/viro.1994.1013 8259646.
    • (1994) Virology , vol.198 , Issue.1 , pp. 109-117
    • Heinz, F.X.1    Stiasny, K.2    Puschner-Auer, G.3    Holzmann, H.4    Allison, S.L.5    Mandl, C.W.6
  • 77
    • 0019997281 scopus 로고
    • Monoclonal antibodies to the structural glycoprotein of tick-borne encephalitis virus
    • 618210
    • Heinz FX, Berger R, Majdic O, Knapp W, Kunz C, Monoclonal antibodies to the structural glycoprotein of tick-borne encephalitis virus. Infect Immun. 1982;37(3):869–74. 6182103
    • (1982) Infect Immun , vol.37 , Issue.3 , pp. 869-874
    • Heinz, F.X.1    Berger, R.2    Majdic, O.3    Knapp, W.4    Kunz, C.5
  • 78
    • 0024593180 scopus 로고
    • Epitope model of tick-borne encephalitis virus envelope glycoprotein E: analysis of structural properties, role of carbohydrate side chain, and conformational changes occurring at acidic pH
    • 246637
    • Guirakhoo F, Heinz FX, Kunz C, Epitope model of tick-borne encephalitis virus envelope glycoprotein E: analysis of structural properties, role of carbohydrate side chain, and conformational changes occurring at acidic pH. Virology. 1989;169(1):90–9. 2466373.
    • (1989) Virology , vol.169 , Issue.1 , pp. 90-99
    • Guirakhoo, F.1    Heinz, F.X.2    Kunz, C.3
  • 79
    • 0029140422 scopus 로고
    • Tick-borne encephalitis virus envelope protein E-specific monoclonal antibodies for the study of low pH-induced conformational changes and immature virions
    • 753599
    • Holzmann H, Stiasny K, York H, Dorner F, Kunz C, Heinz FX, Tick-borne encephalitis virus envelope protein E-specific monoclonal antibodies for the study of low pH-induced conformational changes and immature virions. Arch Virol. 1995;140(2):213–21. 7535997.
    • (1995) Arch Virol , vol.140 , Issue.2 , pp. 213-221
    • Holzmann, H.1    Stiasny, K.2    York, H.3    Dorner, F.4    Kunz, C.5    Heinz, F.X.6
  • 80
    • 0019979209 scopus 로고
    • Dengue virus-specific and flavivirus group determinants identified with monoclonal antibodies by indirect immunofluorescence
    • 628574
    • Henchal EA, Gentry MK, McCown JM, Brandt WE, Dengue virus-specific and flavivirus group determinants identified with monoclonal antibodies by indirect immunofluorescence. Am J Trop Med Hyg. 1982;31(4):830–6. https://doi.org/10.4269/ajtmh.1982.31.830. 6285749
    • (1982) Am J Trop Med Hyg , vol.31 , Issue.4 , pp. 830-836
    • Henchal, E.A.1    Gentry, M.K.2    McCown, J.M.3    Brandt, W.E.4
  • 81
    • 0031014304 scopus 로고    scopus 로고
    • Characterization of monoclonal antibody-escape mutants of tick-borne encephalitis virus with reduced neuroinvasiveness in mice
    • 9010282, Epub 1997/01/01
    • Holzmann H, Stiasny K, Ecker M, Kunz C, Heinz FX, Characterization of monoclonal antibody-escape mutants of tick-borne encephalitis virus with reduced neuroinvasiveness in mice. J Gen Virol. 1997;78 (Pt 1):31–7. Epub 1997/01/01. doi: 10.1099/0022-1317-78-1-31 9010282.
    • (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
  • 82
    • 0038759003 scopus 로고    scopus 로고
    • Involvement of lipids in different steps of the flavivirus fusion mechanism
    • 1282982
    • Stiasny K, Koessl C, Heinz FX, Involvement of lipids in different steps of the flavivirus fusion mechanism. J Virol. 2003;77(14):7856–62. doi: 10.1128/JVI.77.14.7856-7862.2003 12829825.
    • (2003) J Virol , vol.77 , Issue.14 , pp. 7856-7862
    • Stiasny, K.1    Koessl, C.2    Heinz, F.X.3
  • 83
    • 84863393651 scopus 로고    scopus 로고
    • Cathepsin cleavage potentiates the Ebola virus glycoprotein to undergo a subsequent fusion-relevant conformational change
    • 2203193
    • Brecher M, Schornberg KL, Delos SE, Fusco ML, Saphire EO, White JM, Cathepsin cleavage potentiates the Ebola virus glycoprotein to undergo a subsequent fusion-relevant conformational change. J Virol. 2012;86(1):364–72. doi: 10.1128/JVI.05708-11 22031933
    • (2012) J Virol , vol.86 , Issue.1 , pp. 364-372
    • Brecher, M.1    Schornberg, K.L.2    Delos, S.E.3    Fusco, M.L.4    Saphire, E.O.5    White, J.M.6
  • 84
    • 33645783003 scopus 로고    scopus 로고
    • Functional analysis of the tick-borne encephalitis virus cyclization elements indicates major differences between mosquito-borne and tick-borne flaviviruses
    • 1657182
    • Kofler RM, Hoenninger VM, Thurner C, Mandl CW, Functional analysis of the tick-borne encephalitis virus cyclization elements indicates major differences between mosquito-borne and tick-borne flaviviruses. J Virol. 2006;80(8):4099–113. doi: 10.1128/JVI.80.8.4099-4113.2006 16571826
    • (2006) J Virol , vol.80 , Issue.8 , pp. 4099-4113
    • Kofler, R.M.1    Hoenninger, V.M.2    Thurner, C.3    Mandl, C.W.4
  • 85
    • 72849121447 scopus 로고    scopus 로고
    • A trans-complementing recombination trap demonstrates a low propensity of flaviviruses for intermolecular recombination
    • 1986438
    • Taucher C, Berger A, Mandl CW, A trans-complementing recombination trap demonstrates a low propensity of flaviviruses for intermolecular recombination. J Virol. 2010;84(1):599–611. doi: 10.1128/JVI.01063-09 19864381
    • (2010) J Virol , vol.84 , Issue.1 , pp. 599-611
    • Taucher, C.1    Berger, A.2    Mandl, C.W.3
  • 86
    • 0030922352 scopus 로고    scopus 로고
    • Infectious cDNA clones of tick-borne encephalitis virus European subtype prototypic strain Neudoerfl and high virulence strain Hypr
    • 915242
    • Mandl CW, Ecker M, Holzmann H, Kunz C, Heinz FX, Infectious cDNA clones of tick-borne encephalitis virus European subtype prototypic strain Neudoerfl and high virulence strain Hypr. J Gen Virol. 1997;78:1049–57. doi: 10.1099/0022-1317-78-5-1049 9152422.
    • (1997) J Gen Virol , vol.78 , pp. 1049-1057
    • Mandl, C.W.1    Ecker, M.2    Holzmann, H.3    Kunz, C.4    Heinz, F.X.5
  • 87
    • 0024490440 scopus 로고
    • Human rhinovirus serotype 2: in vitro synthesis of an infectious RNA
    • 253589
    • Duechler M, Skern T, Blaas D, Berger B, Sommergruber W, Kuechler E, Human rhinovirus serotype 2: in vitro synthesis of an infectious RNA. Virology. 1989;168(1):159–61. 2535899.
    • (1989) Virology , vol.168 , Issue.1 , pp. 159-161
    • Duechler, M.1    Skern, T.2    Blaas, D.3    Berger, B.4    Sommergruber, W.5    Kuechler, E.6
  • 88
    • 84977503255 scopus 로고    scopus 로고
    • Membrane anchors of the structural flavivirus proteins and their role in virus assembly
    • 2714773
    • Blazevic J, Rouha H, Bradt V, Heinz FX, Stiasny K, Membrane anchors of the structural flavivirus proteins and their role in virus assembly. J Virol. 2016;90(14):6365–78. doi: 10.1128/JVI.00447-16 27147734.
    • (2016) J Virol , vol.90 , Issue.14 , pp. 6365-6378
    • Blazevic, J.1    Rouha, H.2    Bradt, V.3    Heinz, F.X.4    Stiasny, K.5
  • 89
    • 0028815675 scopus 로고
    • Oligomeric rearrangement of tick-borne encephalitis virus envelope proteins induced by an acidic pH
    • 752933
    • Allison SL, Schalich J, Stiasny K, Mandl CW, Kunz C, Heinz FX, Oligomeric rearrangement of tick-borne encephalitis virus envelope proteins induced by an acidic pH. J Virol. 1995;69(2):695–700. 7529335.
    • (1995) J Virol , vol.69 , Issue.2 , pp. 695-700
    • Allison, S.L.1    Schalich, J.2    Stiasny, K.3    Mandl, C.W.4    Kunz, C.5    Heinz, F.X.6
  • 90
    • 0000923841 scopus 로고
    • Polyacrylamide gel electrophoresis of viral proteins
    • Maizel JV, JrPolyacrylamide gel electrophoresis of viral proteins. Methods Virol. 1971;5:179–246.
    • (1971) Methods Virol , vol.5 , pp. 179-246
    • Maizel, J.V.1
  • 91
    • 0029888374 scopus 로고    scopus 로고
    • Recombinant subviral particles from tick-borne encephalitis virus are fusogenic and provide a model system for studying flavivirus envelope glycoprotein functions
    • 867648
    • Schalich J, Allison SL, Stiasny K, Mandl CW, Kunz C, Heinz FX, Recombinant subviral particles from tick-borne encephalitis virus are fusogenic and provide a model system for studying flavivirus envelope glycoprotein functions. J Virol. 1996;70(7):4549–57. 8676481.
    • (1996) J Virol , vol.70 , Issue.7 , pp. 4549-4557
    • Schalich, J.1    Allison, S.L.2    Stiasny, K.3    Mandl, C.W.4    Kunz, C.5    Heinz, F.X.6
  • 92
    • 84860319107 scopus 로고    scopus 로고
    • Quantitative determination of IgM antibodies reduces the pitfalls in the serodiagnosis of tick-borne encephalitis
    • 22421535, Epub 2012/03/17
    • Stiasny K, Aberle JH, Chmelik V, Karrer U, Holzmann H, Heinz FX, Quantitative determination of IgM antibodies reduces the pitfalls in the serodiagnosis of tick-borne encephalitis. J Clin Virol. 2012;54(2):115–20. Epub 2012/03/17. doi: 10.1016/j.jcv.2012.02.016 22421535.
    • (2012) J Clin Virol , vol.54 , Issue.2 , pp. 115-120
    • Stiasny, K.1    Aberle, J.H.2    Chmelik, V.3    Karrer, U.4    Holzmann, H.5    Heinz, F.X.6
  • 93
    • 84886303938 scopus 로고    scopus 로고
    • Aluminum hydroxide influences not only the extent but also the fine specificity and functional activity of antibody responses to tick-borne encephalitis virus in mice
    • 24006434, Epub 2013/09/06
    • Zlatkovic J, Tsouchnikas G, Jarmer J, Koessl C, Stiasny K, Heinz FX, Aluminum hydroxide influences not only the extent but also the fine specificity and functional activity of antibody responses to tick-borne encephalitis virus in mice. J Virol. 2013;87(22):12187–95. Epub 2013/09/06. doi: 10.1128/JVI.01690-13 24006434.
    • (2013) J Virol , vol.87 , Issue.22 , pp. 12187-12195
    • Zlatkovic, J.1    Tsouchnikas, G.2    Jarmer, J.3    Koessl, C.4    Stiasny, K.5    Heinz, F.X.6


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