메뉴 건너뛰기




Volumn 84, Issue 16, 2010, Pages 8253-8358

Influence of pr-M cleavage on the heterogeneity of extracellular dengue virus particles

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY; PRM PROTEIN, FLAVIVIRUS; VIRUS ENVELOPE PROTEIN;

EID: 77954972691     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00696-10     Document Type: Article
Times cited : (134)

References (37)
  • 1
    • 0030912593 scopus 로고    scopus 로고
    • Activation of endothelial cells via antibody-enhanced dengue virus infection of peripheral blood monocytes
    • Anderson, R., S. Wang, C. Osiowy, and A. C. Issekutz. 1997. Activation of endothelial cells via antibody-enhanced dengue virus infection of peripheral blood monocytes. J. Virol. 71:4226-4232.
    • (1997) J. Virol. , vol.71 , pp. 4226-4232
    • Anderson, R.1    Wang, S.2    Osiowy, C.3    Issekutz, A.C.4
  • 4
    • 0038275943 scopus 로고    scopus 로고
    • Genetic and phenotypic characterization of the newly described insect flavivirus, Kamiti River virus
    • Crabtree, M. B., R. C. Sang, V. Stollar, L. M. Dunster, and B. R. Miller. 2003. Genetic and phenotypic characterization of the newly described insect flavivirus, Kamiti River virus. Arch. Virol. 148:1095-1118.
    • (2003) Arch. Virol. , vol.148 , pp. 1095-1118
    • Crabtree, M.B.1    Sang, R.C.2    Stollar, V.3    Dunster, L.M.4    Miller, B.R.5
  • 5
    • 31144445030 scopus 로고    scopus 로고
    • West Nile virus discriminates between DC-SIGN and DC-SIGNR for cellular attachment and infection
    • Davis, C. W., H. Y. Nguyen, S. L. Hanna, M. D. Sanchez, R. W. Doms, and T. C. Pierson. 2006. West Nile virus discriminates between DC-SIGN and DC-SIGNR for cellular attachment and infection. J. Virol. 80:1290-1301.
    • (2006) J. Virol. , vol.80 , pp. 1290-1301
    • Davis, C.W.1    Nguyen, H.Y.2    Hanna, S.L.3    Sanchez, M.D.4    Doms, R.W.5    Pierson, T.C.6
  • 7
    • 0037236396 scopus 로고    scopus 로고
    • Cleavage of protein prM is necessary for infection of BHK-21 cells by tick-borne encephalitis virus
    • Elshuber, S., S. L. Allison, F. X. Heinz, and C. W. Mandl. 2003. Cleavage of protein prM is necessary for infection of BHK-21 cells by tick-borne encephalitis virus. J. Gen. Virol. 84:183-191.
    • (2003) J. Gen. Virol. , vol.84 , pp. 183-191
    • Elshuber, S.1    Allison, S.L.2    Heinz, F.X.3    Mandl, C.W.4
  • 8
    • 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., R. A. Bolin, and J. T. Roehrig. 1992. 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 191:921-931.
    • (1992) Virology , vol.191 , pp. 921-931
    • Guirakhoo, F.1    Bolin, R.A.2    Roehrig, J.T.3
  • 9
    • 0028921203 scopus 로고
    • Antibodies that block virus attachment to Vero cells are a major component of the human neutralizing antibody response against dengue virus type 2
    • He, R.-T., B. L. Innis, A. Nisalak, W. Usawattanakul, S. Wang, S. Kalayanarooj, and R. Anderson. 1995. Antibodies that block virus attachment to Vero cells are a major component of the human neutralizing antibody response against dengue virus type 2. J. Med. Virol. 45:451-461.
    • (1995) J. Med. Virol. , vol.45 , pp. 451-461
    • He, R.-T.1    Innis, B.L.2    Nisalak, A.3    Usawattanakul, W.4    Wang, S.5    Kalayanarooj, S.6    Anderson, R.7
  • 10
    • 0028278395 scopus 로고
    • Structural changes and functional control of the tick-borne encephalitis virus glycoprotein e by the heterodimeric association with protein prM
    • Heinz, F. X., K. Stiasny, G. Puschner-Auer, H. Holzmann, S. L. Allison, C. W. Mandl, and C. Kunz. 1994. Structural changes and functional control of the tick-borne encephalitis virus glycoprotein E by the heterodimeric association with protein prM. Virology 198:109-117.
    • (1994) Virology , vol.198 , 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    Kunz, C.7
  • 11
    • 0021998750 scopus 로고
    • Epitope analysis of antigenic determinants on the surface of dengue-2 virions using monoclonal antibodies
    • Henchal, E. A., J. M. McCown, D. S. Burke, M. C. Seguin, and W. E. Brandt. 1985. Epitope analysis of antigenic determinants on the surface of dengue-2 virions using monoclonal antibodies. Am. J. Trop. Med. Hyg. 34:162-169.
    • (1985) Am. J. Trop. Med. Hyg. , vol.34 , pp. 162-169
    • Henchal, E.A.1    McCown, J.M.2    Burke, D.S.3    Seguin, M.C.4    Brandt, W.E.5
  • 12
    • 0019979209 scopus 로고
    • Dengue virus-specific and flavivirus group determinants identified with monoclonal antibodies by indirect immunofluorescence
    • Henchal, E. A., M. K. Gentry, J. M. McCown, and W. E. Brandt. 1982. Dengue virus-specific and flavivirus group determinants identified with monoclonal antibodies by indirect immunofluorescence. Am. J. Trop. Med. Hyg. 31:830-836.
    • (1982) Am. J. Trop. Med. Hyg. , vol.31 , pp. 830-836
    • Henchal, E.A.1    Gentry, M.K.2    McCown, J.M.3    Brandt, W.E.4
  • 13
    • 33644549138 scopus 로고    scopus 로고
    • The dual-specific binding of dengue virus and target cells for the antibody-dependent enhancement of dengue virus infection
    • Huang, K. J., Y. C. Yang, Y. S. Lin, J. H. Huang, H.-S. Liu, T. M. Yeh, S. H. Chen, C. C. Liu, and H. Y. Lei. 2006. The dual-specific binding of dengue virus and target cells for the antibody-dependent enhancement of dengue virus infection. J. Immunol. 176:2825-2832.
    • (2006) J. Immunol. , vol.176 , 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    Chen, S.H.7    Liu, C.C.8    Lei, H.Y.9
  • 14
    • 0018160953 scopus 로고
    • Isolation of Singh's Aedes albopictus cell clone sensitive to dengue and chikungunya viruses
    • Igarashi, A. 1978. Isolation of Singh's Aedes albopictus cell clone sensitive to dengue and chikungunya viruses. J. Gen. Virol. 40:531-544.
    • (1978) J. Gen. Virol. , vol.40 , pp. 531-544
    • Igarashi, A.1
  • 18
    • 41349112506 scopus 로고    scopus 로고
    • The flavivirus precursor membrane-envelope protein complex: Structure and maturation
    • Li, L., S.-M. Lok, I.-M. Yu, Y. Zhang, R. J. Kuhn, J. Chen, and M. G. Rossmann. 2008. The flavivirus precursor membrane-envelope protein complex: structure and maturation. Science 319:1830-1834.
    • (2008) Science , vol.319 , pp. 1830-1834
    • Li, L.1    Lok, S.-M.2    Yu, I.-M.3    Zhang, Y.4    Kuhn, R.J.5    Chen, J.6    Rossmann, M.G.7
  • 19
    • 34748873170 scopus 로고    scopus 로고
    • Flaviviridae: The viruses and their replication
    • D. M. Knipe and P. M. Howley (ed.), 5th ed. Lippincott-Raven, Philadelphia, PA
    • Lindenbach, B. D., H.-J. Thiel, and C. M. Rice. 2007. Flaviviridae: the viruses and their replication, p. 1101-1152. In D. M. Knipe and P. M. Howley (ed.), Fields virology, 5th ed. Lippincott-Raven, Philadelphia, PA.
    • (2007) Fields Virology , pp. 1101-1152
    • Lindenbach, B.D.1    Thiel, H.-J.2    Rice, C.M.3
  • 21
    • 0027530821 scopus 로고
    • Processing of the dengue virus type 2 proteins prM and C-prM
    • Murray, J. M., J. G. Aaskov, and P. J. Wright. 1993. Processing of the dengue virus type 2 proteins prM and C-prM. J. Gen. Virol. 74:175-182.
    • (1993) J. Gen. Virol. , vol.74 , pp. 175-182
    • Murray, J.M.1    Aaskov, J.G.2    Wright, P.J.3
  • 23
    • 50849120046 scopus 로고    scopus 로고
    • Structural insights into the mechanisms of antibody-mediated neutralization of flavivirus infection: Implications for vaccine development
    • Pierson, T. C., D. H. Fremont, R. J. Kuhn, and M. S. Diamond. 2008. Structural insights into the mechanisms of antibody-mediated neutralization of flavivirus infection: implications for vaccine development. Cell Host Microbe 4:229-238.
    • (2008) Cell Host Microbe , vol.4 , pp. 229-238
    • Pierson, T.C.1    Fremont, D.H.2    Kuhn, R.J.3    Diamond, M.S.4
  • 25
    • 0025064269 scopus 로고
    • Acidotropic amines inhibit proteolytic processing of flavivirus prM protein
    • Randolph, V. B., G. Winkler, and V. Stollar. 1990. Acidotropic amines inhibit proteolytic processing of flavivirus prM protein. Virology 174:450-458.
    • (1990) Virology , vol.174 , pp. 450-458
    • Randolph, V.B.1    Winkler, G.2    Stollar, V.3
  • 27
    • 0032486594 scopus 로고    scopus 로고
    • Monoclonal antibody mapping of the envelope glycoprotein of the dengue 2 virus, Jamaica
    • Roehrig, J. T., R. A. Bolin, and R. G. Kelly. 1998. Monoclonal antibody mapping of the envelope glycoprotein of the dengue 2 virus, Jamaica. Virology 246:317-328.
    • (1998) Virology , vol.246 , pp. 317-328
    • Roehrig, J.T.1    Bolin, R.A.2    Kelly, R.G.3
  • 28
    • 79952125434 scopus 로고    scopus 로고
    • Functional role of prM glycoprotein in dengue virus replication
    • M. Kalitzky and P. Borowski (ed.), Horizon Bioscience, Norfolk, United Kingdom
    • Sittisombut, N., P. Keelapang, and P. Malasit. 2006. Functional role of prM glycoprotein in dengue virus replication, p. 169-189. In M. Kalitzky and P. Borowski (ed.), Molecular biology of the flavivirus. Horizon Bioscience, Norfolk, United Kingdom.
    • (2006) Molecular Biology of the Flavivirus , pp. 169-189
    • Sittisombut, N.1    Keelapang, P.2    Malasit, P.3
  • 29
    • 0030764780 scopus 로고    scopus 로고
    • Proteolytic activation of tick-borne encephalitis virus by furin
    • Stadler, K., S. L. Allison, J. Schalich, and F. X. Heinz. 1997. Proteolytic activation of tick-borne encephalitis virus by furin. J. Virol. 71:8475-8481.
    • (1997) J. Virol. , vol.71 , pp. 8475-8481
    • Stadler, K.1    Allison, S.L.2    Schalich, J.3    Heinz, F.X.4
  • 30
    • 0036791359 scopus 로고    scopus 로고
    • Furin at the cutting edge: From protein traffic to embryogenesis and disease
    • Thomas, G. 2002. Furin at the cutting edge: from protein traffic to embryogenesis and disease. Nat. Rev. Mol. Cell Biol. 3:753-766.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 753-766
    • Thomas, G.1
  • 31
    • 33947722325 scopus 로고    scopus 로고
    • Mutation analysis of the fusion domain region of St. Louis encephalitis virus envelope protein
    • Trainor, N. B., W. D. Crill, J. A. Roberson, and G.-J. J. Chang. 2007. Mutation analysis of the fusion domain region of St. Louis encephalitis virus envelope protein. Virology 360:398-406.
    • (2007) Virology , vol.360 , pp. 398-406
    • Trainor, N.B.1    Crill, W.D.2    Roberson, J.A.3    Chang, G.-J.J.4
  • 33
    • 0033053594 scopus 로고    scopus 로고
    • PrM- and cell-binding domains of the dengue virus e protein
    • Wang, S., R. He, and R. Anderson. 1999. prM- and cell-binding domains of the dengue virus E protein. J. Virol. 73:2547-2551.
    • (1999) J. Virol. , vol.73 , pp. 2547-2551
    • Wang, S.1    He, R.2    Anderson, R.3
  • 37
    • 58149388463 scopus 로고    scopus 로고
    • Functional importance of dengue virus maturation: Infectious properties of immature virions
    • Zybert, I. A., H. van der Ende-Metselaar, J. Wilschut, and J. M. Smit. 2008. Functional importance of dengue virus maturation: infectious properties of immature virions. J. Gen. Virol. 89:3047-3051.
    • (2008) J. Gen. Virol. , vol.89 , pp. 3047-3051
    • Zybert, I.A.1    Van Der Ende-Metselaar, H.2    Wilschut, J.3    Smit, J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.