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Volumn 81, Issue 1, 2007, Pages 261-271

Identification of linear heparin-binding peptides derived from human respiratory syncytial virus fusion glycoprotein that inhibit infectivity

Author keywords

[No Author keywords available]

Indexed keywords

AGAROSE; GLYCOSAMINOGLYCAN; HEPARAN SULFATE; HEPARIN; HEPARIN BINDING PROTEIN; PROTEINASE; SODIUM CHLORATE; VIRUS FUSION PROTEIN;

EID: 33845745776     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.01226-06     Document Type: Article
Times cited : (45)

References (65)
  • 1
    • 0033778942 scopus 로고    scopus 로고
    • Proteoglycans in the developing brain: New conceptual insights for old proteins
    • Bandtlow, C. E., and D. R. Zimmerman. 2000. Proteoglycans in the developing brain: new conceptual insights for old proteins. Physiol. Rev. 80:1267-1290.
    • (2000) Physiol. Rev. , vol.80 , pp. 1267-1290
    • Bandtlow, C.E.1    Zimmerman, D.R.2
  • 2
    • 0034805904 scopus 로고    scopus 로고
    • Blocking intercellular adhesion molecule-1 on human epithelial cells decreases respiratory syncytial virus infection
    • Behera, A. K., H. Matsuse, M. Kumar, X. Kong, R. F. Lockely, and S. S. Mohapatra. 2001. Blocking intercellular adhesion molecule-1 on human epithelial cells decreases respiratory syncytial virus infection. Biochem. Biophys. Res. Commun. 280:188-195.
    • (2001) Biochem. Biophys. Res. Commun. , vol.280 , pp. 188-195
    • Behera, A.K.1    Matsuse, H.2    Kumar, M.3    Kong, X.4    Lockely, R.F.5    Mohapatra, S.S.6
  • 3
    • 24644432375 scopus 로고    scopus 로고
    • Herpes simplex virus glycoprotein B binds to cell surfaces independently of heparan sulfate and blocks virus entry
    • Bender, F. C., J. C. Whitbeck, H. Lou, G. H. Cohen, and R. J. Eisenberg. 2005. Herpes simplex virus glycoprotein B binds to cell surfaces independently of heparan sulfate and blocks virus entry. J. Virol. 79:11588-11597.
    • (2005) J. Virol. , vol.79 , pp. 11588-11597
    • Bender, F.C.1    Whitbeck, J.C.2    Lou, H.3    Cohen, G.H.4    Eisenberg, R.J.5
  • 4
    • 0025705858 scopus 로고
    • Syndecan, a developmentally regulated cell surface proteoglycan that binds extracellular matrix and growth factors
    • Bernfleld, M., and R. D. Sanderson. 1990. Syndecan, a developmentally regulated cell surface proteoglycan that binds extracellular matrix and growth factors. Philos. Trans. R. Soc. Lond. B Biol. Sci. 327:171-186.
    • (1990) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.327 , pp. 171-186
    • Bernfleld, M.1    Sanderson, R.D.2
  • 5
    • 0031870745 scopus 로고    scopus 로고
    • Heparin-like structure on respiratory syncytial virus are involved in its infectivity in vitro
    • Bourgeois, C., J. B. Bour, K. Lidholt, C. Gauthray, and P. Pothier. 1998. Heparin-like structure on respiratory syncytial virus are involved in its infectivity in vitro. J. Virol. 72:7221-7227.
    • (1998) J. Virol. , vol.72 , pp. 7221-7227
    • Bourgeois, C.1    Bour, J.B.2    Lidholt, K.3    Gauthray, C.4    Pothier, P.5
  • 6
    • 0026072631 scopus 로고
    • Syndecan, a cell surface proteoglycan, exhibits a molecular polymorphism during lung development
    • Brauker, J. H., M. S. Trautman, and M. Bernfield. 1991. Syndecan, a cell surface proteoglycan, exhibits a molecular polymorphism during lung development. Dev. Biol. 147:285-292.
    • (1991) Dev. Biol. , vol.147 , pp. 285-292
    • Brauker, J.H.1    Trautman, M.S.2    Bernfield, M.3
  • 7
    • 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
  • 8
    • 0024584913 scopus 로고
    • Molecular modeling of protein-glycosaminoglycan interactions
    • Cardin, A. D., and H. J. 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.2
  • 9
    • 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
  • 10
    • 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
  • 11
    • 0021742698 scopus 로고
    • Nucleotide sequence of the gene encoding the fusion (F) glycoprotein of human respiratory syncytial virus
    • Collins, P. L., Y. T. Huang, and G. W. Wertz. 1984. Nucleotide sequence of the gene encoding the fusion (F) glycoprotein of human respiratory syncytial virus. Proc. Natl. Acad. Sci. USA 81:7683-7687.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 7683-7687
    • Collins, P.L.1    Huang, Y.T.2    Wertz, G.W.3
  • 12
    • 0000089226 scopus 로고    scopus 로고
    • Respiratory syncytial virus
    • B. N. Fields, D. M. Knipe, P. M. Howley, et al (ed.). Lippincott-Raven, Philadelphia, PA
    • Collins, P. L., K. McIntosh, and R. M. Chanock. 1996. Respiratory syncytial virus, p. 1313-1351. In B. N. Fields, D. M. Knipe, P. M. Howley, et al (ed.), Fields virology, vol. 1, 3rd ed. Lippincott-Raven, Philadelphia, PA.
    • (1996) Fields Virology, Vol. 1, 3rd Ed. , pp. 1313-1351
    • Collins, P.L.1    McIntosh, K.2    Chanock, R.M.3
  • 13
    • 0026787022 scopus 로고
    • Binding of vitronectin-thrombin-antithrombin III complex to human endothelial cells is mediated by the heparin binding site of vitronectin
    • de Boer, H. C., K. T. Preissner, B. N. Bouma, and P. G. de Groot. 1992. Binding of vitronectin-thrombin-antithrombin III complex to human endothelial cells is mediated by the heparin binding site of vitronectin. J. Biol. Chem. 267:2264-2268.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2264-2268
    • De Boer, H.C.1    Preissner, K.T.2    Bouma, B.N.3    De Groot, P.G.4
  • 14
    • 27644485016 scopus 로고    scopus 로고
    • Murine coronavirus with an extended host range uses heparan sulfate as an entry receptor
    • de Haan, C. A., Z. Li, E. te Lintelo, B. J. Bosch, B. J. Haijema, and P. J. Rottier. 2005. Murine coronavirus with an extended host range uses heparan sulfate as an entry receptor. J. Virol. 79:14451-14456.
    • (2005) J. Virol. , vol.79 , pp. 14451-14456
    • De Haan, C.A.1    Li, Z.2    Te Lintelo, E.3    Bosch, B.J.4    Haijema, B.J.5    Rottier, P.J.6
  • 15
    • 0022445670 scopus 로고
    • Rapid colorimetric assay for cell growth and survival. Modifications to the tetrazolium dye procedure giving improved sensitivity and reliability
    • Denizot, F., and R. Lang. 1986. Rapid colorimetric assay for cell growth and survival. Modifications to the tetrazolium dye procedure giving improved sensitivity and reliability. J. Immunol. Methods 89:271-277.
    • (1986) J. Immunol. Methods , vol.89 , pp. 271-277
    • Denizot, F.1    Lang, R.2
  • 16
    • 1842457772 scopus 로고    scopus 로고
    • The soluble form of human respiratory syncytial virus attachment protein differs from the membrane-bound form in its oligomeric state but is still capable of binding to cell surface proteoglycans
    • Escribano-Romero, E., J. Rawling, B. Garcia-Barreno, and J. A. Melero. 2004. The soluble form of human respiratory syncytial virus attachment protein differs from the membrane-bound form in its oligomeric state but is still capable of binding to cell surface proteoglycans. J. Virol. 78:3524-3532.
    • (2004) J. Virol. , vol.78 , pp. 3524-3532
    • Escribano-Romero, E.1    Rawling, J.2    Garcia-Barreno, B.3    Melero, J.A.4
  • 17
    • 0022999371 scopus 로고
    • Sulfate transport-deficient mutants of Chinese hamster ovary cells. Sulfation of glycosaminoglycans dependent on cysteine
    • Esko, J. D., A. Elgavish, T. Prasthofer, W. H. Taylor, and J. L. Weinke. 1986. Sulfate transport-deficient mutants of Chinese hamster ovary cells. Sulfation of glycosaminoglycans dependent on cysteine. J. Biol. Chem. 261:15725-15733.
    • (1986) J. Biol. Chem. , vol.261 , pp. 15725-15733
    • Esko, J.D.1    Elgavish, A.2    Prasthofer, T.3    Taylor, W.H.4    Weinke, J.L.5
  • 18
    • 2142854239 scopus 로고
    • Animal cell mutants defective in glycosaminoglycan biosynthesis
    • Esko, J. D., T. E. Stewart, and W. H. Taylor. 1985. Animal cell mutants defective in glycosaminoglycan biosynthesis. Proc. Natl. Acad. Sci. USA 82:3197-3207.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 3197-3207
    • Esko, J.D.1    Stewart, T.E.2    Taylor, W.H.3
  • 19
    • 0033918951 scopus 로고    scopus 로고
    • The fusion glycoprotein of human respiratory syncytial virus facilitates virus attachment and infectivity via an interaction with cellular heparan sulfate
    • Feldman, S. A., S. Audet, and J. A. Beeler. 2000. The fusion glycoprotein of human respiratory syncytial virus facilitates virus attachment and infectivity via an interaction with cellular heparan sulfate. J. Virol. 74:6442-6447.
    • (2000) J. Virol. , vol.74 , pp. 6442-6447
    • Feldman, S.A.1    Audet, S.2    Beeler, J.A.3
  • 20
    • 0032798395 scopus 로고    scopus 로고
    • Identification of a linear heparin binding domain for human respiratory syncytial virus attachment glycoprotein G
    • Feldman, 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
    • Feldman, S.A.1    Hendry, R.M.2    Beeler, J.A.3
  • 21
    • 0022196484 scopus 로고
    • Kinetics of synthesis of respiratory syncytial virus glycoproteins
    • Fernie, B. F., G. Dapolito, P. J. Cote, Jr., and J. L. Gerin. 1985. Kinetics of synthesis of respiratory syncytial virus glycoproteins. J. Gen. Virol. 66:1983-1990.
    • (1985) J. Gen. Virol. , vol.66 , pp. 1983-1990
    • Fernie, B.F.1    Dapolito, G.2    Cote Jr., P.J.3    Gerin, J.L.4
  • 22
    • 0032759064 scopus 로고    scopus 로고
    • Surfactant protein A binds to the fusion glycoprotein of respiratory syncytial virus and neutralizes virion infectivity
    • Ghildyal, R., C. Hartley, A. Varrasso, J. Meanger, D. R. Voelker, E. M. Anders, and J. Mills. 1999. Surfactant protein A binds to the fusion glycoprotein of respiratory syncytial virus and neutralizes virion infectivity. J. Infect. Dis. 180:2009-2013.
    • (1999) J. Infect. Dis. , vol.180 , pp. 2009-2013
    • Ghildyal, R.1    Hartley, C.2    Varrasso, A.3    Meanger, J.4    Voelker, D.R.5    Anders, E.M.6    Mills, J.7
  • 23
    • 0026657822 scopus 로고
    • Mammalian subtilisin-related proteinases in cleavage activation of the paramyxovirus fusion glycoprotein: Superiority of furin/PACE to PC2 or PC1/PC3
    • Gotoh, B., Y. Ohnishi, N. M. Inocencio, E. Esaki, K. Nakayama, P. J. Barr, G. Thomas, and Y. Nagai. 1992. Mammalian subtilisin-related proteinases in cleavage activation of the paramyxovirus fusion glycoprotein: superiority of furin/PACE to PC2 or PC1/PC3. J. Virol. 66:6391-6397.
    • (1992) J. Virol. , vol.66 , pp. 6391-6397
    • Gotoh, B.1    Ohnishi, Y.2    Inocencio, N.M.3    Esaki, E.4    Nakayama, K.5    Barr, P.J.6    Thomas, G.7    Nagai, Y.8
  • 24
    • 0020658446 scopus 로고
    • Respiratory syncytial virus polypeptides. III. The envelope-associated proteins
    • Gruber, C., and S. Levine. 1983. Respiratory syncytial virus polypeptides. III. The envelope-associated proteins. J. Gen. Virol. 64:825-832.
    • (1983) J. Gen. Virol. , vol.64 , pp. 825-832
    • Gruber, C.1    Levine, S.2
  • 25
    • 0034608222 scopus 로고    scopus 로고
    • Iduronic acid-containing glycosaminoglycans on target cells are required for efficient respiratory syncytial virus infection
    • Hallak, L. K., P. L. Collins, W. Knudson, and M. E. Peeples. 2000. Iduronic acid-containing glycosaminoglycans on target cells are required for efficient respiratory syncytial virus infection. Virology 271:264-275.
    • (2000) Virology , vol.271 , pp. 264-275
    • Hallak, L.K.1    Collins, P.L.2    Knudson, W.3    Peeples, M.E.4
  • 26
    • 0033766989 scopus 로고    scopus 로고
    • Glycosaminoglycan sulfation requirements for respiratory syncytial virus infection
    • Hallak, L. K., D. Spillmann, P. L. Collins, and M. E. Peeples. 2000. Glycosaminoglycan sulfation requirements for respiratory syncytial virus infection. J. Virol. 74:10508-10513.
    • (2000) J. Virol. , vol.74 , pp. 10508-10513
    • Hallak, L.K.1    Spillmann, D.2    Collins, P.L.3    Peeples, M.E.4
  • 27
    • 0141502423 scopus 로고    scopus 로고
    • Binding and entry of respiratory syncytial virus into host cells and initiation of the innate immune response
    • Harris, J., and D. Werling. 2003. Binding and entry of respiratory syncytial virus into host cells and initiation of the innate immune response. Cell. Microbiol. 5:671-680.
    • (2003) Cell. Microbiol. , vol.5 , pp. 671-680
    • Harris, J.1    Werling, D.2
  • 28
    • 0028904761 scopus 로고
    • Role of basic residues in the proteolytic activation of Sendai virus fusion glycoprotein
    • Heminaway, B. R., Y. Yang, Y. Tanaka, M. Panin, Y. T. Huang, and M. S. Galinski. 1995. Role of basic residues in the proteolytic activation of Sendai virus fusion glycoprotein. Virus Res. 36:15-35.
    • (1995) Virus Res. , vol.36 , pp. 15-35
    • Heminaway, B.R.1    Yang, Y.2    Tanaka, Y.3    Panin, M.4    Huang, Y.T.5    Galinski, M.S.6
  • 30
    • 0034060308 scopus 로고    scopus 로고
    • Lung surfactant protein a provides a route of entry for respiratory syncytial virus into host cells
    • Hickling, T. P., R. Malhotra, H. Bright, W. McDowell, E. D. Blair, and R. B. Sim. 2000. Lung surfactant protein A provides a route of entry for respiratory syncytial virus into host cells. Viral Immunol. 13:125-135.
    • (2000) Viral Immunol. , vol.13 , pp. 125-135
    • Hickling, T.P.1    Malhotra, R.2    Bright, H.3    McDowell, W.4    Blair, E.D.5    Sim, R.B.6
  • 31
    • 0016710378 scopus 로고
    • Content and synthesis of glycosaminoglycans in the developing lung
    • Horwitz, A. L., and R. C. Crystal. 1975. Content and synthesis of glycosaminoglycans in the developing lung. J. Clin. Investig. 56:1312-1318.
    • (1975) J. Clin. Investig. , vol.56 , pp. 1312-1318
    • Horwitz, A.L.1    Crystal, R.C.2
  • 32
    • 0031661314 scopus 로고    scopus 로고
    • Cell surface proteoglycans are necessary for A27L protein-mediated cell fusion: Identification of the N-terminal region of A27L protein as the glycosaminoglycan-binding domain
    • Hsiao, J. C., C. S. Chung, and W. Chang. 1998. Cell surface proteoglycans are necessary for A27L protein-mediated cell fusion: identification of the N-terminal region of A27L protein as the glycosaminoglycan-binding domain. J. Virol. 72:8374-8379.
    • (1998) J. Virol. , vol.72 , pp. 8374-8379
    • Hsiao, J.C.1    Chung, C.S.2    Chang, W.3
  • 33
    • 0007466688 scopus 로고
    • Virus assay, neutralization test, and antiviral assay
    • V. F. Chan (ed.). Yale University Press, New Haven, CT
    • Hsiung, G. D. 1994. Virus assay, neutralization test, and antiviral assay, p. 46. In V. F. Chan (ed.), Hsiung's diagnostic virology. Yale University Press, New Haven, CT.
    • (1994) Hsiung's Diagnostic Virology , pp. 46
    • Hsiung, G.D.1
  • 35
    • 0035109550 scopus 로고    scopus 로고
    • Recombinant bovine respiratory syncytial virus with deletions of the G or SH genes: G and F proteins bind heparin
    • Karger, A., U. Schmidt, and U. J. Buchholz. 2001. Recombinant bovine respiratory syncytial virus with deletions of the G or SH genes: G and F proteins bind heparin. J. Gen. Virol. 82:631-640.
    • (2001) J. Gen. Virol. , vol.82 , pp. 631-640
    • Karger, A.1    Schmidt, U.2    Buchholz, U.J.3
  • 36
  • 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. Streckert. 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    Streckert, H.J.2
  • 39
    • 29144460894 scopus 로고    scopus 로고
    • Paramyxovirus membrane fusion: Lessons from the F and HN atomic structures
    • Lamb, R. A., R. G. Paterson, and T. S. Jardetzky. 2006. Paramyxovirus membrane fusion: lessons from the F and HN atomic structures. Virology 344:30-37.
    • (2006) Virology , vol.344 , pp. 30-37
    • Lamb, R.A.1    Paterson, R.G.2    Jardetzky, T.S.3
  • 40
    • 0032502692 scopus 로고    scopus 로고
    • Structural homology of the central conserved region of the attachment protein G or respiratory syncytial virus with the fourth subdomain of 55-kDa tumor necrosis factor receptor
    • Langedijk, J. P., B. L. de Groot, H. J. Berendsen, and J. T. van Oirschot. 1998. Structural homology of the central conserved region of the attachment protein G or respiratory syncytial virus with the fourth subdomain of 55-kDa tumor necrosis factor receptor. Virology 243:293-302.
    • (1998) Virology , vol.243 , pp. 293-302
    • Langedijk, J.P.1    De Groot, B.L.2    Berendsen, H.J.3    Van Oirschot, J.T.4
  • 41
    • 3242705779 scopus 로고    scopus 로고
    • Common e protein determinants for attenuation of glycosaminoglycan- binding variants of Japanese encephalitis and West Nile viruses
    • Lee, E., R. A. Hall, and M. Lobigs. 2004. Common E protein determinants for attenuation of glycosaminoglycan-binding variants of Japanese encephalitis and West Nile viruses. J. Virol. 78:8271-8280.
    • (2004) J. Virol. , vol.78 , pp. 8271-8280
    • Lee, E.1    Hall, R.A.2    Lobigs, M.3
  • 42
    • 0023275087 scopus 로고
    • Demonstration the glycoprotein G is the attachment protein of respiratory syncytial virus
    • Levine, S., R. Klaiber-Franco, and P. R. Paradiso. 1987. Demonstration the glycoprotein G is the attachment protein of respiratory syncytial virus. J. Gen. Virol. 68:2521-2524.
    • (1987) J. Gen. Virol. , vol.68 , pp. 2521-2524
    • Levine, S.1    Klaiber-Franco, R.2    Paradiso, P.R.3
  • 44
    • 0037297758 scopus 로고    scopus 로고
    • Isolation and characterisation of potential respiratory syncytial virus receptor(s) on epithelial cells
    • Malhotra, R., M. Ward, H. Bright, R. Priest, M. R. Foster, M. Hurle, E. Blair, and M. Bird. 2003. Isolation and characterisation of potential respiratory syncytial virus receptor(s) on epithelial cells. Microbes Infect. 5:123-133.
    • (2003) Microbes Infect. , vol.5 , pp. 123-133
    • Malhotra, R.1    Ward, M.2    Bright, H.3    Priest, R.4    Foster, M.R.5    Hurle, M.6    Blair, E.7    Bird, M.8
  • 45
    • 0033766518 scopus 로고    scopus 로고
    • Binding of human respiratory syncytial virus to cells: Implication of sulfated cell surface proteoglycans
    • Martinez, I., and J. A. Melero. 2000. Binding of human respiratory syncytial virus to cells: implication of sulfated cell surface proteoglycans. J. Gen. Virol. 81:2715-2722.
    • (2000) J. Gen. Virol. , vol.81 , pp. 2715-2722
    • Martinez, I.1    Melero, J.A.2
  • 46
    • 0034086980 scopus 로고    scopus 로고
    • The core of the respiratory syncytial virus fusion protein is a trimeric coiled coil
    • Matthews, J. M., T. F. Young, S. P. Tucker, and J. P. Mackay. 2000. The core of the respiratory syncytial virus fusion protein is a trimeric coiled coil. J. Virol. 74:5911-5920.
    • (2000) J. Virol. , vol.74 , pp. 5911-5920
    • Matthews, J.M.1    Young, T.F.2    Tucker, S.P.3    Mackay, J.P.4
  • 47
    • 0026028044 scopus 로고
    • Purification of human respiratory syncytial virus: Superiority of sucrose gradient over percoll, renografin and metrizamide gradients
    • Mbiguino, A., and J. Menezes. 1991. Purification of human respiratory syncytial virus: superiority of sucrose gradient over percoll, renografin and metrizamide gradients. J. Virol. Methods 31:161-170.
    • (1991) J. Virol. Methods , vol.31 , pp. 161-170
    • Mbiguino, A.1    Menezes, J.2
  • 48
    • 0018069751 scopus 로고
    • Sulfated glycosaminoglycans of cells grown in culture: Dermatan sulfate disappearance in successive fibroblast subcultures
    • Mourao, P. A., and G. M. Machado-Santelli. 1978. Sulfated glycosaminoglycans of cells grown in culture: dermatan sulfate disappearance in successive fibroblast subcultures. Cell Diff. 7:367-374.
    • (1978) Cell Diff. , vol.7 , pp. 367-374
    • Mourao, P.A.1    Machado-Santelli, G.M.2
  • 49
    • 0017113513 scopus 로고
    • Proteolytic cleavage of the viral glycoproteins and its significance for the virulence of Newcastle disease virus
    • Nagai, Y., H. D. Klenk, and R. Rott. 1976. Proteolytic cleavage of the viral glycoproteins and its significance for the virulence of Newcastle disease virus. Virology 72:494-508.
    • (1976) Virology , vol.72 , pp. 494-508
    • Nagai, Y.1    Klenk, H.D.2    Rott, R.3
  • 50
    • 0032816403 scopus 로고    scopus 로고
    • RhoA interacts with the fusion glycoprotein of respiratory syncytial virus and facilitates virus-induced syncytium formation
    • Pastey, M., J. E. Crowe, Jr., and B. S. Graham. 1999. RhoA interacts with the fusion glycoprotein of respiratory syncytial virus and facilitates virus-induced syncytium formation. J. Virol. 73:7262-7270.
    • (1999) J. Virol. , vol.73 , pp. 7262-7270
    • Pastey, M.1    Crowe Jr., J.E.2    Graham, B.S.3
  • 51
    • 0033963230 scopus 로고    scopus 로고
    • A RhoA-derived peptide inhibits syncytium formation induced by respiratory syncytial virus and parainfluenza virus type 3
    • Pastey, M., T. Gower, P. Spearman, J. Crowe, and B. Graham. 2000. A RhoA-derived peptide inhibits syncytium formation induced by respiratory syncytial virus and parainfluenza virus type 3. Nat. Med. 6:35-40.
    • (2000) Nat. Med. , vol.6 , pp. 35-40
    • Pastey, M.1    Gower, T.2    Spearman, P.3    Crowe, J.4    Graham, B.5
  • 53
    • 14744274494 scopus 로고    scopus 로고
    • Differential role for TLR3 in respiratory syncytial virus-induced chemokine expression
    • Rudd, B. D., E. Burstein, C. S. Duckett, X. Li, and N. W. Lukacs. 2005. Differential role for TLR3 in respiratory syncytial virus-induced chemokine expression. J. Virol. 79:3350-3357.
    • (2005) J. Virol. , vol.79 , pp. 3350-3357
    • Rudd, B.D.1    Burstein, E.2    Duckett, C.S.3    Li, X.4    Lukacs, N.W.5
  • 54
    • 1842291716 scopus 로고
    • Molecular polymorphism of a cell surface proteoglycan: Distinct structures on simple and stratified epithelia
    • Sanderson, R. D., and M. Bernfield. 1988. Molecular polymorphism of a cell surface proteoglycan: distinct structures on simple and stratified epithelia. Proc. Natl. Acad. Sci. USA 85:9562-9566.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 9562-9566
    • Sanderson, R.D.1    Bernfield, M.2
  • 56
    • 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
  • 57
    • 0036060278 scopus 로고    scopus 로고
    • Respiratory syncytial virus with the fusion protein as its only viral glycoprotein is less dependent of cellular glycosaminoglycans for attachment than complete virus
    • Techaarpornkul, S., P. L. Collins, and M. E. Peeples. 2002. Respiratory syncytial virus with the fusion protein as its only viral glycoprotein is less dependent of cellular glycosaminoglycans for attachment than complete virus. Virology 294:296-304.
    • (2002) Virology , vol.294 , pp. 296-304
    • Techaarpornkul, S.1    Collins, P.L.2    Peeples, M.E.3
  • 58
    • 0036100265 scopus 로고    scopus 로고
    • The central conserved cystine noose of the attachment G protein of human respiratory syncytial virus is not required for efficient viral infection in vitro or in vivo
    • Teng, M. N., and P. L. Collins. 2002. The central conserved cystine noose of the attachment G protein of human respiratory syncytial virus is not required for efficient viral infection in vitro or in vivo. J. Virol. 76:6164-6171.
    • (2002) J. Virol. , vol.76 , pp. 6164-6171
    • Teng, M.N.1    Collins, P.L.2
  • 59
    • 0035950607 scopus 로고    scopus 로고
    • Contribution of the respiratory syncytial virus G glycoprotein and its secreted and membrane-bound forms to virus replication in vitro and in vivo
    • Teng, M. N., S. S. Whitehead, and P. L. Collins. 2001. Contribution of the respiratory syncytial virus G glycoprotein and its secreted and membrane-bound forms to virus replication in vitro and in vivo. Virology 289:283-296.
    • (2001) Virology , vol.289 , pp. 283-296
    • Teng, M.N.1    Whitehead, S.S.2    Collins, P.L.3
  • 60
    • 0023235834 scopus 로고
    • Structural comparison of the cleavage-activation site of the fusion glycoprotein between virulent and avirulent strains of Newcastle disease virus
    • Toyoda, T., T. Sakaguchi, K. Imai, N. M. Inocencio, B. Gotoh, M. Hamaguchi, and Y. Nagai. 1987. Structural comparison of the cleavage-activation site of the fusion glycoprotein between virulent and avirulent strains of Newcastle disease virus. Virology 158:242-247.
    • (1987) Virology , vol.158 , pp. 242-247
    • Toyoda, T.1    Sakaguchi, T.2    Imai, K.3    Inocencio, N.M.4    Gotoh, B.5    Hamaguchi, M.6    Nagai, Y.7
  • 62
    • 0029153549 scopus 로고
    • Cellular receptor structures for pseudorabies virus are blocked by antithrombin III
    • Voigt, A., D. Sawitzky, H. Zeichhardt, and K. O. Habermehl. 1995. Cellular receptor structures for pseudorabies virus are blocked by antithrombin III. Med. Microbiol. Immunol. 184:97-103.
    • (1995) Med. Microbiol. Immunol. , vol.184 , pp. 97-103
    • Voigt, A.1    Sawitzky, D.2    Zeichhardt, H.3    Habermehl, K.O.4
  • 63
    • 0024497174 scopus 로고
    • Initial interaction of herpes simplex virus with cells is binding to heparan sulfate
    • WuDunn, D., and P. G. 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, P.G.2
  • 64
    • 0034687711 scopus 로고    scopus 로고
    • Structural characterization of the human respiratory syncytial virus fusion protein core
    • Zhao, X., M. Singh, V. N. Malashkevich, and P. S. Kim. 2000. Structural characterization of the human respiratory syncytial virus fusion protein core. Proc. Natl. Acad. Sci. USA 97:14172-14177.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 14172-14177
    • Zhao, X.1    Singh, M.2    Malashkevich, V.N.3    Kim, P.S.4
  • 65
    • 0035943659 scopus 로고    scopus 로고
    • Proteolytic activation of respiratory syncytial virus fusion protein
    • Zimmer, G., L. Budz, and G. Herrler. 2001. Proteolytic activation of respiratory syncytial virus fusion protein. J. Biol. Chem. 276:31642-31650.
    • (2001) J. Biol. Chem. , vol.276 , pp. 31642-31650
    • Zimmer, G.1    Budz, L.2    Herrler, G.3


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