메뉴 건너뛰기




Volumn 50, Issue 4, 2006, Pages 1470-1479

Sialidase fusion protein as a novel broad-spectrum inhibitor of influenza virus infection

Author keywords

[No Author keywords available]

Indexed keywords

DAS181 PROTEIN; HYBRID PROTEIN; SIALIC ACID; SIALIDASE; UNCLASSIFIED DRUG; VIRUS RECEPTOR;

EID: 33645765519     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/AAC.50.4.1470-1479.2006     Document Type: Article
Times cited : (206)

References (60)
  • 1
    • 0035047041 scopus 로고    scopus 로고
    • Comparative enzymology, biochemistry, and pathophysiology of human exo-α-sialidases (neuraminidases)
    • Achyuthan, K. E., and A. M. Achyuthan. 2001. Comparative enzymology, biochemistry, and pathophysiology of human exo-α-sialidases (neuraminidases). Comp. Biochem. Physiol. B Biochem. Mol. Biol. 129:29-64.
    • (2001) Comp. Biochem. Physiol. B Biochem. Mol. Biol. , vol.129 , pp. 29-64
    • Achyuthan, K.E.1    Achyuthan, A.M.2
  • 2
    • 0029103363 scopus 로고
    • Red cells bound to influenza virus N9 neuraminidase are not released by the N9 neuraminidase activity
    • Air, G. M., and W. G. Laver. 1995. Red cells bound to influenza virus N9 neuraminidase are not released by the N9 neuraminidase activity. Virology 211:278-284.
    • (1995) Virology , vol.211 , pp. 278-284
    • Air, G.M.1    Laver, W.G.2
  • 4
    • 0032037617 scopus 로고    scopus 로고
    • Adherence of Streptococcus pneumoniae to respiratory epithelial cells is inhibited by sialylated oligosaccharides
    • Barthelson, R., A. Mobasseri, D. Zopf, and P. Simon. 1998. Adherence of Streptococcus pneumoniae to respiratory epithelial cells is inhibited by sialylated oligosaccharides. Infect. Immun. 66:1439-1444.
    • (1998) Infect. Immun. , vol.66 , pp. 1439-1444
    • Barthelson, R.1    Mobasseri, A.2    Zopf, D.3    Simon, P.4
  • 8
    • 0015907266 scopus 로고
    • Substrate specificity of neuraminidases
    • Drzeniek, R. 1973. Substrate specificity of neuraminidases. Histochem. J. 5:271-290.
    • (1973) Histochem. J. , vol.5 , pp. 271-290
    • Drzeniek, R.1
  • 9
    • 0024605606 scopus 로고
    • Sialic acid is cleaved from glycoconjugates at the cell surface when influenza virus neuraminidases are expressed from recombinant vaccinia viruses
    • Els, M. C., W. G. Laver, and G. M. Air. 1989. Sialic acid is cleaved from glycoconjugates at the cell surface when influenza virus neuraminidases are expressed from recombinant vaccinia viruses. Virology 170:346-351.
    • (1989) Virology , vol.170 , pp. 346-351
    • Els, M.C.1    Laver, W.G.2    Air, G.M.3
  • 10
    • 0030998767 scopus 로고    scopus 로고
    • Specific binding of Haemophilus influenzae to minor gangliosides of human respiratory epithelial cells
    • Fakih, M. G., T. F. Murphy, M. A. Pattoli, and C. S. Berenson. 1997. Specific binding of Haemophilus influenzae to minor gangliosides of human respiratory epithelial cells. Infect. Immun. 65:1695-1700.
    • (1997) Infect. Immun. , vol.65 , pp. 1695-1700
    • Fakih, M.G.1    Murphy, T.F.2    Pattoli, M.A.3    Berenson, C.S.4
  • 11
    • 0029645872 scopus 로고
    • The three domains of a bacterial sialidase: A beta-propeller, an immunoglobulin module and a galactose-binding jelly-roll
    • Gaskell, A., S. Crennell, and G. Taylor. 1995. The three domains of a bacterial sialidase: a beta-propeller, an immunoglobulin module and a galactose-binding jelly-roll. Structure 3:1197-1205.
    • (1995) Structure , vol.3 , pp. 1197-1205
    • Gaskell, A.1    Crennell, S.2    Taylor, G.3
  • 12
    • 0003878326 scopus 로고
    • Academic Press, Inc., New York, N. Y.
    • Gottschalk, A. 1959. The Viruses. Academic Press, Inc., New York, N. Y.
    • (1959) The Viruses
    • Gottschalk, A.1
  • 13
    • 0020611458 scopus 로고
    • Effects of hexose starvation and the role of sialic acid in influenza virus release
    • Griffin, J. A., S. Basak, and R. W. Compans. 1983. Effects of hexose starvation and the role of sialic acid in influenza virus release. Virology 125:324-334.
    • (1983) Virology , vol.125 , pp. 324-334
    • Griffin, J.A.1    Basak, S.2    Compans, R.W.3
  • 14
    • 0023083855 scopus 로고
    • Complement activation by human lymphocytes from different lymphoid organs: Role of sialic acid and lack of relationship to electrical surface charge
    • Gutierrez, C., M. J. Martin, and K. A. Brown. 1987. Complement activation by human lymphocytes from different lymphoid organs: role of sialic acid and lack of relationship to electrical surface charge. Complement 4:99-109.
    • (1987) Complement , vol.4 , pp. 99-109
    • Gutierrez, C.1    Martin, M.J.2    Brown, K.A.3
  • 15
    • 0344200085 scopus 로고    scopus 로고
    • Quantitative glycohistochemical characterization of normal nasal mucosa, and of single as opposed to massive nasal polyps
    • Hassid, S., G. Choufani, N. Nagy, H. Kaltner, A. Danguy, H. J. Gabius, and R. Kiss. 1999. Quantitative glycohistochemical characterization of normal nasal mucosa, and of single as opposed to massive nasal polyps. Ann. Otol. Rhinol. Laryngol. 108:797-805.
    • (1999) Ann. Otol. Rhinol. Laryngol. , vol.108 , pp. 797-805
    • Hassid, S.1    Choufani, G.2    Nagy, N.3    Kaltner, H.4    Danguy, A.5    Gabius, H.J.6    Kiss, R.7
  • 16
    • 0022643732 scopus 로고
    • In vivo identification of sialic acid as the ocular receptor for Pseudomonas aeruginosa
    • Hazlett, L. D., M. Moon, and R. S. Berk. 1986. In vivo identification of sialic acid as the ocular receptor for Pseudomonas aeruginosa. Infect. Immun. 51:687-689.
    • (1986) Infect. Immun. , vol.51 , pp. 687-689
    • Hazlett, L.D.1    Moon, M.2    Berk, R.S.3
  • 18
    • 0002677020 scopus 로고    scopus 로고
    • Virus isolation and quantitation
    • B. W. J. Mahy and H. O. Kangro (ed.). Academic Press, Ltd., London, England
    • Hierholzer, J. C., and R. A. Killington. 1996. Virus isolation and quantitation, p. 25-46. In B. W. J. Mahy and H. O. Kangro (ed.), Virology methods manual. Academic Press, Ltd., London, England.
    • (1996) Virology Methods Manual , pp. 25-46
    • Hierholzer, J.C.1    Killington, R.A.2
  • 19
    • 0022653824 scopus 로고
    • Activation of the alternative complement pathway by mumps infected cells: Relationship to viral neuraminidase activity
    • Hirsch, R. L., J. S. Wolinsky, and J. A. Winkelstein. 1986. Activation of the alternative complement pathway by mumps infected cells: relationship to viral neuraminidase activity. Arch. Virol. 87:181-190.
    • (1986) Arch. Virol. , vol.87 , pp. 181-190
    • Hirsch, R.L.1    Wolinsky, J.S.2    Winkelstein, J.A.3
  • 20
    • 0033947283 scopus 로고    scopus 로고
    • Interspecies transmission and receptor recognition of influenza A viruses
    • Ito, T. 2000. Interspecies transmission and receptor recognition of influenza A viruses. Microbiol. Immunol. 44:423-430.
    • (2000) Microbiol. Immunol. , vol.44 , pp. 423-430
    • Ito, T.1
  • 24
    • 0031787323 scopus 로고    scopus 로고
    • Attachment of nontypable Haemophilus influenzae to human pharyngeal epithelial cells mediated by a ganglioside receptor
    • Kawakami, K., K. Ahmed, Y. Utsunomiya, N. Rikitomi, A. Hori, K. Oishi, and T. Nagatake. 1998. Attachment of nontypable Haemophilus influenzae to human pharyngeal epithelial cells mediated by a ganglioside receptor. Microbiol. Immunol. 42:697-702.
    • (1998) Microbiol. Immunol. , vol.42 , pp. 697-702
    • Kawakami, K.1    Ahmed, K.2    Utsunomiya, Y.3    Rikitomi, N.4    Hori, A.5    Oishi, K.6    Nagatake, T.7
  • 25
    • 0016311999 scopus 로고
    • On the transport of mucus and its rheologic simulants in ciliated systems
    • King, M., A. Gilboa, F. A. Meyer, and A. Silberberg. 1974. On the transport of mucus and its rheologic simulants in ciliated systems. Am. Rev. Respir. Dis. 110:740-745.
    • (1974) Am. Rev. Respir. Dis. , vol.110 , pp. 740-745
    • King, M.1    Gilboa, A.2    Meyer, F.A.3    Silberberg, A.4
  • 28
    • 0024514102 scopus 로고
    • Adherence of Pseudomonas aeruginosa to tracheal epithelium
    • Marcus, H., A. Austria, and N. R. Baker. 1989. Adherence of Pseudomonas aeruginosa to tracheal epithelium. Infect. Immun. 57:1050-1053.
    • (1989) Infect. Immun. , vol.57 , pp. 1050-1053
    • Marcus, H.1    Austria, A.2    Baker, N.R.3
  • 29
    • 1842585032 scopus 로고    scopus 로고
    • Human and avian influenza viruses target different cell types in cultures of human airway epithelium
    • Matrosovich, M. N., T. Y. Matrosovich, T. Gray, N. A. Roberts, and H. D. Klenk. 2004. Human and avian influenza viruses target different cell types in cultures of human airway epithelium. Proc. Natl. Acad. Sci. USA 101:4620-4624.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 4620-4624
    • Matrosovich, M.N.1    Matrosovich, T.Y.2    Gray, T.3    Roberts, N.A.4    Klenk, H.D.5
  • 30
    • 0037443951 scopus 로고    scopus 로고
    • Role of neuraminidase in lethal synergism between influenza virus and Streptococcus pneumoniae
    • McCullers, J. A., and K. C. Bartmess. 2003. Role of neuraminidase in lethal synergism between influenza virus and Streptococcus pneumoniae. J. Infect. Dis. 187:1000-1009.
    • (2003) J. Infect. Dis. , vol.187 , pp. 1000-1009
    • McCullers, J.A.1    Bartmess, K.C.2
  • 32
    • 0016800017 scopus 로고
    • On the role of sialic acid in the rheological properties of mucus
    • Meyer, F. A., M. King, and R. A. Gelman. 1975. On the role of sialic acid in the rheological properties of mucus. Biochim. Biophys. Acta 392:223-232.
    • (1975) Biochim. Biophys. Acta , vol.392 , pp. 223-232
    • Meyer, F.A.1    King, M.2    Gelman, R.A.3
  • 33
    • 0023879768 scopus 로고
    • Effect of gangliosides on activation of the alternative pathway of human complement
    • Michalek, M. T., E. G. Bremer, and C. Mold. 1988. Effect of gangliosides on activation of the alternative pathway of human complement. J. Immunol. 140:1581-1587.
    • (1988) J. Immunol. , vol.140 , pp. 1581-1587
    • Michalek, M.T.1    Bremer, E.G.2    Mold, C.3
  • 34
    • 0033405059 scopus 로고    scopus 로고
    • Expression of a novel human sialidase encoded by the NEU2 gene
    • Monti, E., A. Preti, C. Nesti, A. Ballabio, and G. Borsani. 1999. Expression of a novel human sialidase encoded by the NEU2 gene. Glycobiology 9:1313-1321.
    • (1999) Glycobiology , vol.9 , pp. 1313-1321
    • Monti, E.1    Preti, A.2    Nesti, C.3    Ballabio, A.4    Borsani, G.5
  • 35
    • 0034194259 scopus 로고    scopus 로고
    • Molecular mechanisms of target recognition in an innate immune system: Interactions among factor H, C3b, and target in the alternative pathway of human complement
    • Pangburn, M. K., K. L. Pangburn, V. Koistinen, S. Meri, and A. K. Sharma. 2000. Molecular mechanisms of target recognition in an innate immune system: interactions among factor H, C3b, and target in the alternative pathway of human complement. J. Immunol. 164:4742-4751.
    • (2000) J. Immunol. , vol.164 , pp. 4742-4751
    • Pangburn, M.K.1    Pangburn, K.L.2    Koistinen, V.3    Meri, S.4    Sharma, A.K.5
  • 36
    • 0842284589 scopus 로고    scopus 로고
    • Respiratory viruses predisposing to bacterial infections: Role of neuraminidase
    • Peltola, V. T., and J. A. McCullers. 2004. Respiratory viruses predisposing to bacterial infections: role of neuraminidase. Pediatr. Infect. Dis. J. 23:S87-S97.
    • (2004) Pediatr. Infect. Dis. J. , vol.23
    • Peltola, V.T.1    McCullers, J.A.2
  • 37
    • 22244471025 scopus 로고    scopus 로고
    • Influenza virus neuraminidase contributes to secondary bacterial pneumonia
    • Peltola, V. T., K. G. Murti, and J. A. McCullers. 2005. Influenza virus neuraminidase contributes to secondary bacterial pneumonia. J. Infect. Dis. 192:249-257.
    • (2005) J. Infect. Dis. , vol.192 , pp. 249-257
    • Peltola, V.T.1    Murti, K.G.2    McCullers, J.A.3
  • 38
    • 0018421350 scopus 로고
    • Fluorometric assay of neuraminidase with a sodium (4-methylumbelliferyl- α-D-N-acetylneuraminate) substrate
    • Potier, M., L. Mameli, M. Belisle, L. Dallaire, and S. B. Melancon. 1979. Fluorometric assay of neuraminidase with a sodium (4-methylumbelliferyl- α-D-N-acetylneuraminate) substrate. Anal. Biochem. 94:287-296.
    • (1979) Anal. Biochem. , vol.94 , pp. 287-296
    • Potier, M.1    Mameli, L.2    Belisle, M.3    Dallaire, L.4    Melancon, S.B.5
  • 39
    • 0020631367 scopus 로고
    • Evidence for mucins and sialic acid as receptors for Pseudomonas aeruginosa in the lower respiratory tract
    • Ramphal, R., and M. Pyle. 1983. Evidence for mucins and sialic acid as receptors for Pseudomonas aeruginosa in the lower respiratory tract. Infect. Immun. 41:339-344.
    • (1983) Infect. Immun. , vol.41 , pp. 339-344
    • Ramphal, R.1    Pyle, M.2
  • 40
    • 0021833148 scopus 로고
    • Further characterization of the tracheal receptor for Pseudomonas aeruginosa
    • Ramphal, R., and M. Pyle. 1985. Further characterization of the tracheal receptor for Pseudomonas aeruginosa. Eur. J. Clin. Microbiol. 4:160-162.
    • (1985) Eur. J. Clin. Microbiol. , vol.4 , pp. 160-162
    • Ramphal, R.1    Pyle, M.2
  • 41
    • 0023701143 scopus 로고
    • Intracellular trafficking of cell surface sialoglycoconjugates
    • Reichner, J. S., S. W. Whiteheart, and G. W. Hart. 1988. Intracellular trafficking of cell surface sialoglycoconjugates. J. Biol. Chem. 263:16316-16326.
    • (1988) J. Biol. Chem. , vol.263 , pp. 16316-16326
    • Reichner, J.S.1    Whiteheart, S.W.2    Hart, G.W.3
  • 42
    • 0024409183 scopus 로고
    • Assessment of signs of influenza illness in the ferret model
    • Reuman, P. D., S. Keely, and G. M. Schiff. 1989. Assessment of signs of influenza illness in the ferret model. J. Virol. Methods 24:27-34.
    • (1989) J. Virol. Methods , vol.24 , pp. 27-34
    • Reuman, P.D.1    Keely, S.2    Schiff, G.M.3
  • 43
    • 0026753576 scopus 로고
    • Comparison of adherence of Pseudomonas aeruginosa to respiratory epithelial cells from cystic fibrosis patients and healthy subjects
    • Saiman, L., G. Cacalano, D. Gruenert, and A. Prince. 1992. Comparison of adherence of Pseudomonas aeruginosa to respiratory epithelial cells from cystic fibrosis patients and healthy subjects. Infect. Immun. 60:2808-2814.
    • (1992) Infect. Immun. , vol.60 , pp. 2808-2814
    • Saiman, L.1    Cacalano, G.2    Gruenert, D.3    Prince, A.4
  • 44
    • 0020348005 scopus 로고
    • Chemistry, metabolism, and biological functions of sialic acids
    • Schauer, R. 1982. Chemistry, metabolism, and biological functions of sialic acids. Adv. Carbohydr. Chem. Biochem. 40:131-234.
    • (1982) Adv. Carbohydr. Chem. Biochem. , vol.40 , pp. 131-234
    • Schauer, R.1
  • 45
    • 3042824104 scopus 로고    scopus 로고
    • Acute infection with influenza virus enhances susceptibility to fatal pneumonia following Streptococcus pneumoniae infection in mice with chronic pulmonary colonization with Pseudomonas aeruginosa
    • Seki, M., Y. Higashiyama, K. Tomono, K. Yanagihara, H. Ohno, Y. Kaneko, K. Izumikawa, Y. Miyazaki, Y. Hirakata, Y. Mizuta, T. Tashiro, and S. Kohno. 2004. Acute infection with influenza virus enhances susceptibility to fatal pneumonia following Streptococcus pneumoniae infection in mice with chronic pulmonary colonization with Pseudomonas aeruginosa. Clin. Exp. Immunol. 137:35-40.
    • (2004) Clin. Exp. Immunol. , vol.137 , pp. 35-40
    • Seki, M.1    Higashiyama, Y.2    Tomono, K.3    Yanagihara, K.4    Ohno, H.5    Kaneko, Y.6    Izumikawa, K.7    Miyazaki, Y.8    Hirakata, Y.9    Mizuta, Y.10    Tashiro, T.11    Kohno, S.12
  • 46
    • 0024593476 scopus 로고
    • Structure and function of human amphiregulin: A member of the epidermal growth factor family
    • Shoyab, M., G. D. Plowman, V. L. McDonald, J. G. Bradley, and G. J. Todaro. 1989. Structure and function of human amphiregulin: a member of the epidermal growth factor family. Science 243:1074-1076.
    • (1989) Science , vol.243 , pp. 1074-1076
    • Shoyab, M.1    Plowman, G.D.2    McDonald, V.L.3    Bradley, J.G.4    Todaro, G.J.5
  • 49
    • 0036173555 scopus 로고    scopus 로고
    • Measles virus preferentially transduces the basolateral surface of well-differentiated human airway epithelia
    • Sinn, P. L., G. Williams, S. Vongpunsawad, R. Cattaneo, and P. B. McCray, Jr. 2002. Measles virus preferentially transduces the basolateral surface of well-differentiated human airway epithelia. J. Virol. 76:2403-2409.
    • (2002) J. Virol. , vol.76 , pp. 2403-2409
    • Sinn, P.L.1    Williams, G.2    Vongpunsawad, S.3    Cattaneo, R.4    McCray Jr., P.B.5
  • 51
    • 0023752476 scopus 로고
    • Lessons for human influenza from pathogenicity studies with ferrets
    • Smith, H., and C. Sweet. 1988. Lessons for human influenza from pathogenicity studies with ferrets. Rev. Infect. Dis. 10:55-75.
    • (1988) Rev. Infect. Dis. , vol.10 , pp. 55-75
    • Smith, H.1    Sweet, C.2
  • 52
    • 0033859822 scopus 로고    scopus 로고
    • Influenza virus infection of desialylated cells
    • Stray, S. J., R. D. Cummings, and G. M. Air. 2000. Influenza virus infection of desialylated cells. Glycobiology 10:649-658.
    • (2000) Glycobiology , vol.10 , pp. 649-658
    • Stray, S.J.1    Cummings, R.D.2    Air, G.M.3
  • 53
    • 0021397429 scopus 로고
    • Anaerobes as normal oral flora
    • Sutter, V. L. 1984. Anaerobes as normal oral flora. Rev. Infect. Dis. 6:S62-S66.
    • (1984) Rev. Infect. Dis. , vol.6
    • Sutter, V.L.1
  • 54
    • 0024673434 scopus 로고
    • Properties of sialidase isolated from Actinomyces viscosus DSM 43798
    • Teufel, M., P. Roggentin, and R. Schauer. 1989. Properties of sialidase isolated from Actinomyces viscosus DSM 43798. Biol. Chem. Hoppe-Seyler 370:435-443.
    • (1989) Biol. Chem. Hoppe-Seyler , vol.370 , pp. 435-443
    • Teufel, M.1    Roggentin, P.2    Schauer, R.3
  • 55
    • 0025787889 scopus 로고
    • Blocking of fimbria-mediated adherence of Haemophilus influenzae by sialyl gangliosides
    • van Alphen, L., L. Geelen-van den Broek, L. Blaas, M. van Ham, and J. Dankert. 1991. Blocking of fimbria-mediated adherence of Haemophilus influenzae by sialyl gangliosides. Infect. Immun. 59:4473-4477.
    • (1991) Infect. Immun. , vol.59 , pp. 4473-4477
    • Van Alphen, L.1    Geelen-Van Den Broek, L.2    Blaas, L.3    Van Ham, M.4    Dankert, J.5
  • 56
    • 0026842845 scopus 로고
    • Selectins and other mammalian sialic acid-binding lectins
    • Varki, A. 1992. Selectins and other mammalian sialic acid-binding lectins. Curr. Opin. Cell Biol. 4:257-266.
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 257-266
    • Varki, A.1
  • 57
    • 0030993576 scopus 로고    scopus 로고
    • Sialic acids as ligands in recognition phenomena
    • Varki, A. 1997. Sialic acids as ligands in recognition phenomena. FASEB J. 11:248-255.
    • (1997) FASEB J. , vol.11 , pp. 248-255
    • Varki, A.1
  • 58
    • 3142642823 scopus 로고    scopus 로고
    • Binding of influenza viruses to sialic acids: Reassortant viruses with A/NWS/33 hemagglutinin bind to α2,8-linked sialic acid
    • Wu, W., and G. M. Air. 2004. Binding of influenza viruses to sialic acids: reassortant viruses with A/NWS/33 hemagglutinin bind to α2,8-linked sialic acid. Virology 325:340-350.
    • (2004) Virology , vol.325 , pp. 340-350
    • Wu, W.1    Air, G.M.2
  • 59
    • 0027464115 scopus 로고
    • Complete nucleotide sequence of the Actinomyces viscosus T14V sialidase gene: Presence of a conserved repeating sequence among strains of Actinomyces spp
    • Yeung, M. K. 1993. Complete nucleotide sequence of the Actinomyces viscosus T14V sialidase gene: presence of a conserved repeating sequence among strains of Actinomyces spp. Infect. Immun. 61:109-116.
    • (1993) Infect. Immun. , vol.61 , pp. 109-116
    • Yeung, M.K.1
  • 60
    • 0036094947 scopus 로고    scopus 로고
    • Respiratory syncytial virus infection of human airway epithelial cells is polarized, specific to ciliated cells, and without obvious cytopathology
    • Zhang, L., M. E. Peeples, R. C. Boucher, P. L. Collins, and R. J. Pickles. 2002. Respiratory syncytial virus infection of human airway epithelial cells is polarized, specific to ciliated cells, and without obvious cytopathology. J. Virol. 76:5654-5666.
    • (2002) J. Virol. , vol.76 , pp. 5654-5666
    • Zhang, L.1    Peeples, M.E.2    Boucher, R.C.3    Collins, P.L.4    Pickles, R.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.