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Volumn 75, Issue 12, 2001, Pages 5627-5637

Adaptation of tick-borne encephalitis virus to BHK-21 cells results in the formation of multiple heparan sulfate binding sites in the envelope protein and attenuation in vivo

Author keywords

[No Author keywords available]

Indexed keywords

ENVELOPE PROTEIN; GLYCOPROTEIN E; HEPARAN SULFATE;

EID: 0035024156     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.75.12.5627-5637.2001     Document Type: Article
Times cited : (187)

References (70)
  • 1
    • 0031242317 scopus 로고    scopus 로고
    • Overview of vaccines
    • Ada, G. 1997. Overview of vaccines. Mol. Biotechnol. 8:123-134.
    • (1997) Mol. Biotechnol. , vol.8 , pp. 123-134
    • Ada, G.1
  • 2
    • 0035051804 scopus 로고    scopus 로고
    • Mutational evidence for an internal fusion peptide in flavivirus envelope protein E
    • Allison, S. L., J. Schalich, K. Stiasny, C. W. Mandl, and F. X. Heinz. 2001. Mutational evidence for an internal fusion peptide in flavivirus envelope protein E. J. Virol. 75:4268-4275.
    • (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
  • 3
    • 0022897789 scopus 로고
    • Chlorate - A potent inhibitor of protein sulfation in intact cells
    • Baeuerle, P. A., and W. B. Huttner. 1986. Chlorate - a potent inhibitor of protein sulfation in intact cells. Biochem. Biophys. Res. Commun. 141:870-877.
    • (1986) Biochem. Biophys. Res. Commun. , vol.141 , pp. 870-877
    • Baeuerle, P.A.1    Huttner, W.B.2
  • 4
    • 0033012398 scopus 로고    scopus 로고
    • Chemokine receptors as HIV-1 coreceptors: Roles in viral entry, tropism, and disease
    • Berger, E. A., P. M. Murphy, and J. M. Farber. 1999. Chemokine receptors as HIV-1 coreceptors: roles in viral entry, tropism, and disease. Annu. Rev. Immunol. 17:657-700.
    • (1999) Annu. Rev. Immunol. , vol.17 , pp. 657-700
    • Berger, E.A.1    Murphy, P.M.2    Farber, J.M.3
  • 5
    • 0034633834 scopus 로고    scopus 로고
    • Mutations in the E2 glycoprotein of Venezuelan equine encephalitis virus confer heparan sulfate interaction, low morbidity, and rapin clearance from blood of mice
    • Bernard, K. A., W. B. Klimstra, and R. E. Johnston. 2000. Mutations in the E2 glycoprotein of Venezuelan equine encephalitis virus confer heparan sulfate interaction, low morbidity, and rapin clearance from blood of mice. Virology 276:93-103.
    • (2000) Virology , vol.276 , pp. 93-103
    • Bernard, K.A.1    Klimstra, W.B.2    Johnston, R.E.3
  • 7
    • 0034713441 scopus 로고    scopus 로고
    • Characterization of a membrane-associated protein implicated in visna virus binding and infection
    • Bruett, L., S. A. Barber, and J. E. Clements. 2000. Characterization of a membrane-associated protein implicated in visna virus binding and infection. Virology 271:132-141.
    • (2000) Virology , vol.271 , pp. 132-141
    • Bruett, L.1    Barber, S.A.2    Clements, J.E.3
  • 8
    • 0031849754 scopus 로고    scopus 로고
    • Binding of Sindbis virus to cell surface heparan sulfate
    • Byrnes, A. P., and D. E. Griffin. 1998. Binding of Sindbis virus to cell surface heparan sulfate. J. Virol. 72:7349-7356.
    • (1998) J. Virol. , vol.72 , pp. 7349-7356
    • Byrnes, A.P.1    Griffin, D.E.2
  • 9
    • 0033989275 scopus 로고    scopus 로고
    • Large-plaque mutants of Sindbis virus show reduced binding to heparan sulfate, heightened viremia, and slower clearance from the circulation
    • Byrnes, A. P., and D. E. Griffin. 2000. Large-plaque mutants of Sindbis virus show reduced binding to heparan sulfate, heightened viremia, and slower clearance from the circulation. J. Virol. 74:644-651.
    • (2000) J. Virol. , vol.74 , pp. 644-651
    • Byrnes, A.P.1    Griffin, D.E.2
  • 10
    • 0024584913 scopus 로고
    • Molecular modeling of protein-glycosaminoglycan interactions
    • Cardin, A. D., and H. J. R. Weintraub. 1989. Molecular modeling of protein-glycosaminoglycan interactions. Arteriosclerosis 9:21-32.
    • (1989) Arteriosclerosis , vol.9 , pp. 21-32
    • Cardin, A.D.1    Weintraub, H.J.R.2
  • 11
    • 0030764559 scopus 로고    scopus 로고
    • Dengue virus infectivity depends on envelope protein binding to target cell heparan sulfate
    • Chen, Y., T. Maguire, R. E. Hileman, J. R. Fromm, J. D. Esko, R. J. Linhardt, and R. M. Marks. 1997. Dengue virus infectivity depends on envelope protein binding to target cell heparan sulfate. Nat. Med. 3:866-871.
    • (1997) Nat. Med. , vol.3 , pp. 866-871
    • Chen, Y.1    Maguire, T.2    Hileman, R.E.3    Fromm, J.R.4    Esko, J.D.5    Linhardt, R.J.6    Marks, R.M.7
  • 12
    • 0031906150 scopus 로고    scopus 로고
    • A27L protein mediates vaccinia virus interaction with cell surface heparan sulfate
    • Chung, C.-S., J.-C. Hsiao, Y.-S. Chang, and W. Chang. 1998. A27L protein mediates vaccinia virus interaction with cell surface heparan sulfate. J. Virol. 72:1577-1585.
    • (1998) J. Virol. , vol.72 , pp. 1577-1585
    • Chung, C.-S.1    Hsiao, J.-C.2    Chang, Y.-S.3    Chang, W.4
  • 13
    • 70449217974 scopus 로고
    • Techniques for hemagglutination and hemagglutination inhibition with arthropod-borne viruses
    • Clarke, D. H., and J. Casals. 1958. Techniques for hemagglutination and hemagglutination inhibition with arthropod-borne viruses. Am. J. Trop. Med. Hyg. 7:561-573.
    • (1958) Am. J. Trop. Med. Hyg. , vol.7 , pp. 561-573
    • Clarke, D.H.1    Casals, J.2
  • 14
    • 0027315907 scopus 로고
    • Initiation of human cytomegalovirus infection requires initial interaction with cell surface heparan sulfate
    • Compton, T., D. M. Nowlin, and N. R. Cooper. 1993. Initiation of human cytomegalovirus infection requires initial interaction with cell surface heparan sulfate. Virology 193:834-841.
    • (1993) Virology , vol.193 , pp. 834-841
    • Compton, T.1    Nowlin, D.M.2    Cooper, N.R.3
  • 15
    • 0034654569 scopus 로고    scopus 로고
    • Heparan sulfate glycosaminoglycans are involved in adenovirus type 5 and type 2 host-cell interactions
    • Dechecchi, M. C., A. Tamanini, A. Bonizzato, and G. Cabrini. 2000. Heparan sulfate glycosaminoglycans are involved in adenovirus type 5 and type 2 host-cell interactions. Virology 268:382-390.
    • (2000) Virology , vol.268 , pp. 382-390
    • Dechecchi, M.C.1    Tamanini, A.2    Bonizzato, A.3    Cabrini, G.4
  • 16
    • 0033084784 scopus 로고    scopus 로고
    • Baculovirus vector requires electrostatic interactions including heparan sulfate for efficient gene transfer in mammalian cells
    • Duisit, G., S. Saleun, S. Douthe, J. Barsoum, G. Chadeuf, and P. Moullier. 1999. Baculovirus vector requires electrostatic interactions including heparan sulfate for efficient gene transfer in mammalian cells. J. Gene Med. 1:93-102.
    • (1999) J. Gene Med. , vol.1 , pp. 93-102
    • Duisit, G.1    Saleun, S.2    Douthe, S.3    Barsoum, J.4    Chadeuf, G.5    Moullier, P.6
  • 18
    • 0032798395 scopus 로고    scopus 로고
    • Identification of a linear heparin binding domain for human respiratory syncytial virus attachment glycoprotein G
    • Feldmann, S. A., R. M. Hendry, and J. A. Beeler. 1999. Identification of a linear heparin binding domain for human respiratory syncytial virus attachment glycoprotein G. J. Virol. 73:6610-6617.
    • (1999) J. Virol. , vol.73 , pp. 6610-6617
    • Feldmann, S.A.1    Hendry, R.M.2    Beeler, J.A.3
  • 20
    • 0028794483 scopus 로고
    • A heterologous heparin-binding domain can promote functional attachment of a pseudorabies virus gC mutant to cell surfaces
    • Flynn, S. J., and P. Ryan. 1995. A heterologous heparin-binding domain can promote functional attachment of a pseudorabies virus gC mutant to cell surfaces. J. Virol. 69:834-839.
    • (1995) J. Virol. , vol.69 , pp. 834-839
    • Flynn, S.J.1    Ryan, P.2
  • 22
    • 0023681294 scopus 로고
    • Influence of chlorate on proteoglycan biosynthesis by cultured human fibroblasts
    • Greve, H., Z. Cully, P. Blumberg, and H. Kresse. 1988. Influence of chlorate on proteoglycan biosynthesis by cultured human fibroblasts. J. Biol. Chem. 263:12886-12892.
    • (1988) J. Biol. Chem. , vol.263 , pp. 12886-12892
    • Greve, H.1    Cully, Z.2    Blumberg, P.3    Kresse, H.4
  • 23
    • 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
    • Guirakhoo, F., F. X. Heinz, and C. Kunz. 1989. 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 169:90-99.
    • (1989) Virology , vol.169 , pp. 90-99
    • Guirakhoo, F.1    Heinz, F.X.2    Kunz, C.3
  • 24
    • 0034567567 scopus 로고    scopus 로고
    • Structures and mechanisms in flavivirus fusion
    • Heinz, F. X., and S. L. Allison. 2000. Structures and mechanisms in flavivirus fusion. Adv. Virus Res. 55:231-269.
    • (2000) Adv. Virus Res. , vol.55 , pp. 231-269
    • Heinz, F.X.1    Allison, S.L.2
  • 25
    • 0020535267 scopus 로고
    • A topological and functional model of epitopes on the structural glycoprotein of tick-borne encephalitis virus defined by monoclonal antibodies
    • Heinz, F. X., R. Berger, W. Tuma, and C. Kunz. 1983. A topological and functional model of epitopes on the structural glycoprotein of tick-borne encephalitis virus defined by monoclonal antibodies. Virology 126:525-537.
    • (1983) Virology , vol.126 , pp. 525-537
    • Heinz, F.X.1    Berger, R.2    Tuma, W.3    Kunz, C.4
  • 26
    • 0019294978 scopus 로고
    • Preparation of a highly purified vaccine against tick-borne encephalitis by continuous flow zonal ultracentrifugation
    • Heinz, F, X., C. Kunz, and H. Fauma. 1980. Preparation of a highly purified vaccine against tick-borne encephalitis by continuous flow zonal ultracentrifugation. J. Med. Virol. 6:213-221.
    • (1980) J. Med. Virol. , vol.6 , pp. 213-221
    • Heinz, F.1    Kunz, C.2    Fauma, H.3
  • 27
    • 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. Püschner-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    Püschner-Auer, G.3    Holzmann, H.4    Allison, S.L.5    Mandl, C.W.6    Kunz, C.7
  • 28
    • 0022522033 scopus 로고
    • A model study of the use of monoclonal antibodies in capture enzyme immunoassays for antigen quantification exploiting the epitope map of tick-borne encephalitis virus
    • Heinz, F. X., W. Tuma, F. Guirakhoo, and C. Kunz. 1986. A model study of the use of monoclonal antibodies in capture enzyme immunoassays for antigen quantification exploiting the epitope map of tick-borne encephalitis virus. J. Biol. Stand. 14:133-141.
    • (1986) J. Biol. Stand. , vol.14 , pp. 133-141
    • Heinz, F.X.1    Tuma, W.2    Guirakhoo, F.3    Kunz, C.4
  • 29
    • 0032006909 scopus 로고    scopus 로고
    • Glycosaminoglycan-protein interactions: Definition of consensus sites in glycosaminoglycan binding proteins
    • Hileman, R. E., J. R. Fromm, J. M. Weiler, and R. J. Linhardt. 1998. Glycosaminoglycan-protein interactions: definition of consensus sites in glycosaminoglycan binding proteins. BioEssays 20:156-167.
    • (1998) BioEssays , vol.20 , pp. 156-167
    • Hileman, R.E.1    Fromm, J.R.2    Weiler, J.M.3    Linhardt, R.J.4
  • 30
    • 0033765641 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans initiate dengue virus infection of hepatocytes
    • Hilgard, P., and R. Stockert. 2000. Heparan sulfate proteoglycans initiate dengue virus infection of hepatocytes. Hepatology 32:1069-1077.
    • (2000) Hepatology , vol.32 , pp. 1069-1077
    • Hilgard, P.1    Stockert, R.2
  • 31
    • 0031014304 scopus 로고    scopus 로고
    • Characterization of monoclonal antibody-escape mutants of tick-borne encephalitis virus with reduced neuroinvasiveness in mice
    • Holzmann, H., K. Stiasny, M. Ecker, C. Kunz, and F. X. Heinz. 1997. Characterization of monoclonal antibody-escape mutants of tick-borne encephalitis virus with reduced neuroinvasiveness in mice. J. Gen. Virol. 78: 31-37.
    • (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
  • 33
    • 0033602564 scopus 로고    scopus 로고
    • Analysis of the steps involved in dengue virus entry into host cells
    • Hung, S.-L., P.-L. Lee, H.-W. Chen, L.-K. Chen, C.-L. Kao, and C.-C. King. 1999. Analysis of the steps involved in dengue virus entry into host cells. Virology 257:156-167.
    • (1999) Virology , vol.257 , pp. 156-167
    • Hung, S.-L.1    Lee, P.-L.2    Chen, H.-W.3    Chen, L.-K.4    Kao, C.-L.5    King, C.-C.6
  • 35
    • 0033033071 scopus 로고    scopus 로고
    • Characterization of a Chinese hamster ovary cell line developed by retroviral insertional mutagenesis that is resistant to Sindbis virus infection
    • Jan, J. T., A. P. Byrnes, and D. E. Griffin. 1999. Characterization of a Chinese hamster ovary cell line developed by retroviral insertional mutagenesis that is resistant to Sindbis virus infection. J. Virol. 73:4919-4924.
    • (1999) J. Virol. , vol.73 , pp. 4919-4924
    • Jan, J.T.1    Byrnes, A.P.2    Griffin, D.E.3
  • 36
    • 0032757364 scopus 로고    scopus 로고
    • Infection of neonatal mice with Sindbis virus results in a systemic inflammatory response syndrome
    • Klimstra, W. B., K. D. Ryman, K. A. Bernard, K. B. Nguyen, C. A. Biron, and R. E. Johnston. 1999. Infection of neonatal mice with Sindbis virus results in a systemic inflammatory response syndrome. J. Virol. 73:10387-10398.
    • (1999) J. Virol. , vol.73 , pp. 10387-10398
    • Klimstra, W.B.1    Ryman, K.D.2    Bernard, K.A.3    Nguyen, K.B.4    Biron, C.A.5    Johnston, R.E.6
  • 37
    • 0031869503 scopus 로고    scopus 로고
    • Adaptation of Sindbis virus to BHK cells selects for use of heparan sulfate as an attachment receptor
    • Klimstra, W. B., K. D. Ryman, and R. E. Johnston. 1998. Adaptation of Sindbis virus to BHK cells selects for use of heparan sulfate as an attachment receptor. J. Virol. 72:7357-7366.
    • (1998) J. Virol. , vol.72 , pp. 7357-7366
    • Klimstra, W.B.1    Ryman, K.D.2    Johnston, R.E.3
  • 38
    • 0030973338 scopus 로고    scopus 로고
    • Heparin-dependent attachment of respiratory syncytial virus (RSV) to host cells
    • Krusat, T., and H. J. Strecken. 1997. Heparin-dependent attachment of respiratory syncytial virus (RSV) to host cells. Arch. Virol. 142:1247-1254.
    • (1997) Arch. Virol. , vol.142 , pp. 1247-1254
    • Krusat, T.1    Strecken, H.J.2
  • 39
    • 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 glycosaminoglycan in entry
    • Lee, E., and M. Lobigs. 2000. Substitutions at the putative receptor-binding site of an encephalitic flavivirus alter virulence and host cell tropism and reveal a role for glycosaminoglycan in entry. J. Virol. 74:8867-8875.
    • (2000) J. Virol. , vol.74 , pp. 8867-8875
    • Lee, E.1    Lobigs, M.2
  • 40
    • 0034012233 scopus 로고    scopus 로고
    • Vaccinia virus envelope H3L protein binds to cell surface heparan sulfate and is important for intracellular mature virion morphogenesis and virus infection in vitro and in vivo
    • Lin, C.-L., C.-S. Chung, H. G. Heine, and W. Chang. 2000. Vaccinia virus envelope H3L protein binds to cell surface heparan sulfate and is important for intracellular mature virion morphogenesis and virus infection in vitro and in vivo. J. Virol. 74:3353-3365.
    • (2000) J. Virol. , vol.74 , pp. 3353-3365
    • Lin, C.-L.1    Chung, C.-S.2    Heine, H.G.3    Chang, W.4
  • 41
    • 0033818910 scopus 로고    scopus 로고
    • Attenuation of tick-borne encephalitis virus by structure-based site-specific mutagenesis of a putative flavivirus receptor binding site
    • Mandl, C. W., S. L. Allison, H. Holzmann, T. Meixner, and F. X. Heinz. 2000 Attenuation of tick-borne encephalitis virus by structure-based site-specific mutagenesis of a putative flavivirus receptor binding site. J. Virol. 74:9601-9609.
    • (2000) J. Virol. , vol.74 , pp. 9601-9609
    • Mandl, C.W.1    Allison, S.L.2    Holzmann, H.3    Meixner, T.4    Heinz, F.X.5
  • 42
    • 0030922352 scopus 로고    scopus 로고
    • Infectious cDNA clones of tick-borne encephalitis virus European subtype prototypic strain Neudoerfl and high virulence strain Hypr
    • Mandl, C. W., M. Ecker, H. Holzmann, C. Kunz, and F. X. Heinz. 1997. Infectious cDNA clones of tick-borne encephalitis virus European subtype prototypic strain Neudoerfl and high virulence strain Hypr. J. Gen. Virol. 78:1049-1057.
    • (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
  • 43
    • 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., F. Guirakhoo, H. Holzmann, F. X. Heinz, and C. Kunz. 1989. Antigenic structure of the flavivirus envelope protein E at the molecular level, using tick-borne encephalitis virus as a model. J. Virol. 63:564-571.
    • (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
  • 44
    • 0031887847 scopus 로고    scopus 로고
    • Spontaneous and engineered deletions in the 3′ noncoding region of tick-borne encephalitis virus: Construction of highly attenuated mutants of a flavivirus
    • Mandl, C. W., H. Holzmann, T. Meixner, S. Rauscher, P. F. Stadler, S. L. Allison, and F. X. Heinz. 1998. Spontaneous and engineered deletions in the 3′ noncoding region of tick-borne encephalitis virus: construction of highly attenuated mutants of a flavivirus. J. Virol. 72:2132-2140.
    • (1998) J. Virol. , vol.72 , pp. 2132-2140
    • Mandl, C.W.1    Holzmann, H.2    Meixner, T.3    Rauscher, S.4    Stadler, P.F.5    Allison, S.L.6    Heinz, F.X.7
  • 45
    • 0030698026 scopus 로고    scopus 로고
    • The molecular basis of virulence of the encephalitogenic flaviviruses
    • McMinn, P. C. 1997. The molecular basis of virulence of the encephalitogenic flaviviruses. J. Gen. Virol. 78:2711-2722.
    • (1997) J. Gen. Virol. , vol.78 , pp. 2711-2722
    • McMinn, P.C.1
  • 46
    • 0031976829 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 attachment to HeLa CD4 cells is CD4 independent and gp120 dependent and requires cell surface heparans
    • Mondor, I., S. Ugolini, and Q. J. Sattentau. 1998. Human immunodeficiency virus type 1 attachment to HeLa CD4 cells is CD4 independent and gp120 dependent and requires cell surface heparans. J. Virol. 72:3623-3634.
    • (1998) J. Virol. , vol.72 , pp. 3623-3634
    • Mondor, I.1    Ugolini, S.2    Sattentau, Q.J.3
  • 48
    • 2642681650 scopus 로고    scopus 로고
    • Foot-and-mouth disease virus virulent for cattle utilizes the integrin alpha(v)beta3 as its receptor
    • Neff, S., D. Sa-Carvalho, E. Rieder, P. W. Mason, S. D. Blystone, E. J. Brown, and B. Baxt. 1998. Foot-and-mouth disease virus virulent for cattle utilizes the integrin alpha(v)beta3 as its receptor. J. Virol. 72:3587-3594.
    • (1998) J. Virol. , vol.72 , pp. 3587-3594
    • Neff, S.1    Sa-Carvalho, D.2    Rieder, E.3    Mason, P.W.4    Blystone, S.D.5    Brown, E.J.6    Baxt, B.7
  • 49
    • 0025308663 scopus 로고
    • Nucleotide sequence of the virulent SA-14 strain of Japanese encephalitis virus and its attenuated derivative, SA-14-14-2
    • Nitayaphan, S., J. A. Grant, G.-J. J. Chang, and D. W. Trent. 1990. Nucleotide sequence of the virulent SA-14 strain of Japanese encephalitis virus and its attenuated derivative, SA-14-14-2. Virology 177:541-552.
    • (1990) Virology , vol.177 , pp. 541-552
    • Nitayaphan, S.1    Grant, J.A.2    Chang, G.-J.J.3    Trent, D.W.4
  • 51
    • 0034718796 scopus 로고    scopus 로고
    • Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin
    • Pellegrini, L., D. F. Burke, F. von Delft, B. Mulloy, and T. L. Blundell. 2000. Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin. Nature 407:1029-1034.
    • (2000) Nature , vol.407 , pp. 1029-1034
    • Pellegrini, L.1    Burke, D.F.2    Von Delft, F.3    Mulloy, B.4    Blundell, T.L.5
  • 52
    • 0026749906 scopus 로고
    • Heterogeneity in envelope protein sequences and N-linked glycosylation among yellow fever virus vaccine strains
    • Post, P. R., C. N. D. Santos, R. Carvalho, A. C. R. Cruz, C. M. Rice, and R. Galler. 1992. Heterogeneity in envelope protein sequences and N-linked glycosylation among yellow fever virus vaccine strains. Virology 188:160-167.
    • (1992) Virology , vol.188 , pp. 160-167
    • Post, P.R.1    Santos, C.N.D.2    Carvalho, R.3    Cruz, A.C.R.4    Rice, C.M.5    Galler, R.6
  • 53
    • 0034732236 scopus 로고    scopus 로고
    • The interaction of heparin sulfate and adeno-associated virus 2
    • Qiu, J., A. Handa, M. Kirby, and K. E. Brown. 2000. The interaction of heparin sulfate and adeno-associated virus 2. Virology 269:137-147.
    • (2000) Virology , vol.269 , pp. 137-147
    • Qiu, J.1    Handa, A.2    Kirby, M.3    Brown, K.E.4
  • 54
    • 33745158157 scopus 로고
    • A simple method for estimating fifty percent endpoints
    • Reed, J. L., and H. Muench. 1938. A simple method for estimating fifty percent endpoints. Am. J. Hyg. 27:493.
    • (1938) Am. J. Hyg. , vol.27 , pp. 493
    • Reed, J.L.1    Muench, H.2
  • 55
    • 0029014434 scopus 로고
    • The envelope glycoprotein from tick-borne encephalitis virus at 2 Å resolution
    • Rey, F. A., F. X. Heinz, C. Mandl, C. Kunz, and S. C. Harrison. 1995. The envelope glycoprotein from tick-borne encephalitis virus at 2 Å resolution. Nature 375:291-298.
    • (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
  • 56
    • 0030971779 scopus 로고    scopus 로고
    • Tissue culture adaptation of foot-and-mouth disease virus selects viruses that bind to heparin and are attenuated in cattle
    • Sa-Carvalho, D., E. Rieder, B. Baxt, R. Rodarte, A. Tanuri, and P. W. Mason. 1997. Tissue culture adaptation of foot-and-mouth disease virus selects viruses that bind to heparin and are attenuated in cattle. J. Virol. 71:5115-5123.
    • (1997) J. Virol. , vol.71 , pp. 5115-5123
    • Sa-Carvalho, D.1    Rieder, E.2    Baxt, B.3    Rodarte, R.4    Tanuri, A.5    Mason, P.W.6
  • 58
    • 0034077911 scopus 로고    scopus 로고
    • Cellular receptors for viruses: Links to tropism and pathogenesis
    • Schneider-Schaulies, J. 2000. Cellular receptors for viruses: links to tropism and pathogenesis. J. Gen. Virol. 81:1413-1429.
    • (2000) J. Gen. Virol. , vol.81 , pp. 1413-1429
    • Schneider-Schaulies, J.1
  • 59
    • 0030947592 scopus 로고    scopus 로고
    • Role of the extracellular domain of human herpesvirus 7 glycoprotein B in virus binding to cell surface heparan sulfate proteoglycans
    • Secchiero, P., D. Sund, A. L. De Vico, R. W. Crowley, M. S. Reitz, Jr., G. Zauli, P. Lusso, and R. C. Gallo. 1997. Role of the extracellular domain of human herpesvirus 7 glycoprotein B in virus binding to cell surface heparan sulfate proteoglycans. J. Virol. 71:4571-4580.
    • (1997) J. Virol. , vol.71 , pp. 4571-4580
    • Secchiero, P.1    Sund, D.2    De Vico, A.L.3    Crowley, R.W.4    Reitz M.S., Jr.5    Zauli, G.6    Lusso, P.7    Gallo, R.C.8
  • 61
    • 0034003827 scopus 로고    scopus 로고
    • Identification and analysis of a novel heparin-binding glycoprotein encoded by human herpesvirus 7
    • Skrincosky, D., P. Hocknell, L. Whetter, P. Secchiero, B. Chandran, and S. Dewhurst. 2000. Identification and analysis of a novel heparin-binding glycoprotein encoded by human herpesvirus 7. J. Virol. 74:4530-4540.
    • (2000) J. Virol. , vol.74 , pp. 4530-4540
    • Skrincosky, D.1    Hocknell, P.2    Whetter, L.3    Secchiero, P.4    Chandran, B.5    Dewhurst, S.6
  • 62
    • 0031906147 scopus 로고    scopus 로고
    • Membrane-associated heparan sulfate proteoglycan is a receptor for adeno-associated virus type 2 virions
    • Summerford, C., and R. J. Samulski. 1998. Membrane-associated heparan sulfate proteoglycan is a receptor for adeno-associated virus type 2 virions. J. Virol. 72:1438-1445.
    • (1998) J. Virol. , vol.72 , pp. 1438-1445
    • Summerford, C.1    Samulski, R.J.2
  • 63
    • 0031183514 scopus 로고    scopus 로고
    • Virus entry: Two receptors are better than one
    • Tufaro, F. 1997. Virus entry: two receptors are better than one. Trends Microbiol. 5:257-260.
    • (1997) Trends Microbiol. , vol.5 , pp. 257-260
    • Tufaro, F.1
  • 64
    • 0033959545 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans on the cell surface: Versatile coordinators of cellular functions
    • Tumova, S., A. Woods, and J. R. Couchman. 2000. Heparan sulfate proteoglycans on the cell surface: versatile coordinators of cellular functions. Int. J. Biochem. Cell Biol. 32:269-288.
    • (2000) Int. J. Biochem. Cell Biol. , vol.32 , pp. 269-288
    • Tumova, S.1    Woods, A.2    Couchman, J.R.3
  • 67
    • 0345411634 scopus 로고    scopus 로고
    • Identification of functional domains in the 14-kilodalton envelope protein (A27L) of vaccinia virus
    • Vázquez, M.-I., and M. Esteban. 1999. Identification of functional domains in the 14-kilodalton envelope protein (A27L) of vaccinia virus. J. Virol. 73:9098-9109.
    • (1999) J. Virol. , vol.73 , pp. 9098-9109
    • Vázquez, M.-I.1    Esteban, M.2
  • 68
    • 0028785280 scopus 로고
    • The flavivirus 3′-noncoding region: Extensive size heterogeneity independent of evolutionary relationships among strains of tick-borne encephalitis virus
    • Wallner, G., C. W. Mandl, C. Kunz, and F. X. Heinz. 1995. The flavivirus 3′-noncoding region: extensive size heterogeneity independent of evolutionary relationships among strains of tick-borne encephalitis virus. Virology 213:169-178.
    • (1995) Virology , vol.213 , pp. 169-178
    • Wallner, G.1    Mandl, C.W.2    Kunz, C.3    Heinz, F.X.4
  • 69
    • 0029986085 scopus 로고    scopus 로고
    • Characterization and complete genome sequences of high- and low-virulence variants of tick-borne encephalitis virus
    • Wallner, G., C. W. Mandl, M. Ecker, H. Holzmann, K. Stiasny, C. Kunz, and F. X.Heinz. 1996. Characterization and complete genome sequences of high- and low-virulence variants of tick-borne encephalitis virus. J. Gen. Virol. 77:1035-1042.
    • (1996) J. Gen. Virol. , vol.77 , pp. 1035-1042
    • Wallner, G.1    Mandl, C.W.2    Ecker, M.3    Holzmann, H.4    Stiasny, K.5    Kunz, C.6    Heinz, F.X.7
  • 70
    • 0024497174 scopus 로고
    • Initial interaction of herpes simplex virus with cells is binding to heparan sulfate
    • WuDunn, D., and D. Spear. 1989. Initial interaction of herpes simplex virus with cells is binding to heparan sulfate. J. Virol. 63:52-58.
    • (1989) J. Virol. , vol.63 , pp. 52-58
    • WuDunn, D.1    Spear, D.2


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