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Volumn 23, Issue 1-2, 2006, Pages 107-113

Gangliosides are not essential for influenza virus infection

Author keywords

Glycosphingolipid deficient cells; GM 95; Influenza virus; MEB 4; Serum free medium; TLC overlay assay

Indexed keywords

GANGLIOSIDE; SIALIC ACID; SIALOGLYCOPROTEIN; VIRUS RECEPTOR;

EID: 33645455932     PISSN: 02820080     EISSN: 15734986     Source Type: Journal    
DOI: 10.1007/s10719-006-5443-y     Document Type: Article
Times cited : (20)

References (30)
  • 1
    • 0000545033 scopus 로고
    • Interactions of animal viruses with cell surface receptors
    • edited by Conn M Academic Press, Orlando, FL
    • Paulson, J.C.: Interactions of animal viruses with cell surface receptors. In The receptors, edited by Conn M (Academic Press, Orlando, FL, 1985), vol. 2, pp. 131-219
    • (1985) The Receptors , vol.2 , pp. 131-219
    • Paulson, J.C.1
  • 2
    • 0002044965 scopus 로고
    • Sialic acid as receptor determinant of ortho- and paramyxoviruses
    • Rosenberg A (Eds.) Plenum, New York
    • Herrler, G., Hausmann, J., Klenk, H-D: Sialic acid as receptor determinant of ortho- and paramyxoviruses. In: Rosenberg A (Eds.) Biology of the sialic acids, (Plenum, New York, 1995), pp. 315-336
    • (1995) Biology of the Sialic Acids , pp. 315-336
    • Herrler, G.1    Hausmann, J.2    Klenk, H.-D.3
  • 3
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • Skehel, J.J., Wiley, D.C.: Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu Rev Biochem 69, 531-69 (2000)
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 4
    • 0020348005 scopus 로고
    • Chemistry, metabolism, and biological functions of sialic acids
    • Schauer, R.: Chemistry, metabolism, and biological functions of sialic acids. Adv Carbohydr Chem Biochem 40, 131-234 (1982)
    • (1982) Adv. Carbohydr. Chem. Biochem. , vol.40 , pp. 131-234
    • Schauer, R.1
  • 5
    • 0002867950 scopus 로고
    • Biochemistry and role of sialic acids
    • edited by Rosenberg A Plenum, New York
    • Schauer, R., Kelm, S., Schröder, C., Miller, E.: Biochemistry and role of sialic acids. In Biology of the sialic acids, edited by Rosenberg A (Plenum, New York, 1995), pp. 7-67
    • (1995) Biology of the Sialic Acids , pp. 7-67
    • Schauer, R.1    Kelm, S.2    Schröder, C.3    Miller, E.4
  • 6
    • 0020009821 scopus 로고
    • Gangliosides: Structure, isolation, and analysis
    • Ledeen, R.W., Yu, R.K.: Gangliosides: Structure, isolation, and analysis. Meth Enzymol 83, 139-91 (1982)
    • (1982) Meth. Enzymol. , vol.83 , pp. 139-191
    • Ledeen, R.W.1    Yu, R.K.2
  • 7
    • 0028133152 scopus 로고
    • Gangliosides as influenza virus receptors. Variation of influenza viruses and their recognition of the receptor sialo-sugar chains
    • Suzuki, Y.: Gangliosides as influenza virus receptors. Variation of influenza viruses and their recognition of the receptor sialo-sugar chains. Progr Lipid Res 33, 429-57 (1994)
    • (1994) Progr. Lipid. Res. , vol.33 , pp. 429-457
    • Suzuki, Y.1
  • 10
    • 0023638370 scopus 로고
    • The surface receptor is a major de terminant of the cell tropism of influenza C virus
    • Herrler, G., Klenk, H-D: The surface receptor is a major de terminant of the cell tropism of influenza C virus. Virology 159, 102-8 (1987)
    • (1987) Virology , vol.159 , pp. 102-108
    • Herrler, G.1    Klenk, H.-D.2
  • 11
    • 0001927825 scopus 로고
    • Clinical influenza virus and the embryonated hen's eggs
    • Robertson, J.S.: Clinical influenza virus and the embryonated hen's eggs. Rev Med Virol 3, 97-106 (1993)
    • (1993) Rev. Med. Virol. , vol.3 , pp. 97-106
    • Robertson, J.S.1
  • 12
    • 0033526523 scopus 로고    scopus 로고
    • Effects of egg-adaptation on the receptor-binding properties of human influenza viruses
    • Gambaryan, A.S., Robertson, J.S., Matrosovich, M.N.: Effects of egg-adaptation on the receptor-binding properties of human influenza viruses. Virology 258, 232-9 (1999)
    • (1999) Virology , vol.258 , pp. 232-239
    • Gambaryan, A.S.1    Robertson, J.S.2    Matrosovich, M.N.3
  • 13
    • 0030748536 scopus 로고    scopus 로고
    • Avian influenza A viruses differ from human viruses by recognition of sialyloligosaccharides and gangliosides and by a higher conservation of the HA receptor-binding site
    • Matrosovich, M.N., Gambaryan, A.S., Teneberg, S., Piskarev, V.E., Yamnikova, S.S., Lvov, D.K., Robertson, J.S., Karlsson, K-A: Avian influenza A viruses differ from human viruses by recognition of sialyloligosaccharides and gangliosides and by a higher conservation of the HA receptor-binding site. Virology 233, 224-34 (1997)
    • (1997) Virology , vol.233 , pp. 224-234
    • Matrosovich, M.N.1    Gambaryan, A.S.2    Teneberg, S.3    Piskarev, V.E.4    Yamnikova, S.S.5    Lvov, D.K.6    Robertson, J.S.7    Karlsson, K.-A.8
  • 14
    • 0033789373 scopus 로고    scopus 로고
    • A strain of human influenza A virus binds to extended but not short gangliosides as assayed by thin-layer chromatography overlay
    • Miller-Podraza, H., Johansson, L., Johansson, P., Matrosovich, M., Karlsson, K-A: A strain of human influenza A virus binds to extended but not short gangliosides as assayed by thin-layer chromatography overlay. Glycobiology 10, 975-82 (2000)
    • (2000) Glycobiology , vol.10 , pp. 975-982
    • Miller-Podraza, H.1    Johansson, L.2    Johansson, P.3    Matrosovich, M.4    Karlsson, K.-A.5
  • 15
    • 0141789590 scopus 로고    scopus 로고
    • Differences between influenza virus receptors on target cells of duck and chicken and receptor specificity of the 1997 H5N1 chicken and human influenza viruses from Hong Kong
    • Gambaryan, A.S., Tuzikov, A.B., Bovin, N.V., Yamnikova, S.S., Lvov, D.K., Webster, R.G.: Matrosovich MN, Differences between influenza virus receptors on target cells of duck and chicken and receptor specificity of the 1997 H5N1 chicken and human influenza viruses from Hong Kong. Avian. Dis. 47, 1154-60 (2003)
    • (2003) Avian. Dis. , vol.47 , pp. 1154-1160
    • Gambaryan, A.S.1    Tuzikov, A.B.2    Bovin, N.V.3    Yamnikova, S.S.4    Lvov, D.K.5    Webster, R.G.6    Matrosovich, M.N.7
  • 16
    • 0017804579 scopus 로고
    • Intestinal influenza: Replication and characterization of influenza viruses in ducks
    • Webster, R.G., Yakhno, M., Hinshaw, V.S., Bean, W.J., Murti, K.G.: Intestinal influenza: replication and characterization of influenza viruses in ducks. Virology 84, 268-78 (1978)
    • (1978) Virology , vol.84 , pp. 268-278
    • Webster, R.G.1    Yakhno, M.2    Hinshaw, V.S.3    Bean, W.J.4    Murti, K.G.5
  • 17
    • 0035208265 scopus 로고    scopus 로고
    • Entry of influenza virus into a glycosphingolipid-deficient mouse skin fibroblast cell line
    • Ablan, S., Rawat, S.S., Blumenthal, R., Puri, A.: Entry of influenza virus into a glycosphingolipid-deficient mouse skin fibroblast cell line. Arch. Virol. 146, 2227-38 (2001)
    • (2001) Arch. Virol. , vol.146 , pp. 2227-2238
    • Ablan, S.1    Rawat, S.S.2    Blumenthal, R.3    Puri, A.4
  • 19
    • 0027179047 scopus 로고
    • A review and predictive models of ganglioside uptake by biological membranes
    • Saqr, H.E., Pearl, D.K., Yates, A.J.: A review and predictive models of ganglioside uptake by biological membranes. J Neurochem 61, 395-411 (1993)
    • (1993) J. Neurochem. , vol.61 , pp. 395-411
    • Saqr, H.E.1    Pearl, D.K.2    Yates, A.J.3
  • 21
    • 0026719676 scopus 로고
    • Structural determination of gangliosides that bind to influenza A, B, and C viruses by an improved binding assay: Strain-specific receptor epitopes in sialo-sugar chains
    • Suzuki, Y., Nakao, T., Ito, T., Watanabe, N., Toda, Y., Xu, G., Suzuki, T., Kobayashi, T., Kimura, Y., Yamada, A.: Structural determination of gangliosides that bind to influenza A, B, and C viruses by an improved binding assay: strain-specific receptor epitopes in sialo-sugar chains. Virology 189, 121-31 (1992)
    • (1992) Virology , vol.189 , pp. 121-131
    • Suzuki, Y.1    Nakao, T.2    Ito, T.3    Watanabe, N.4    Toda, Y.5    Xu, G.6    Suzuki, T.7    Kobayashi, T.8    Kimura, Y.9    Yamada, A.10
  • 22
    • 11144239774 scopus 로고    scopus 로고
    • Influenza virus entry and infection require host cell N-linked glycoprotein
    • USA
    • Chu, V.C., Whittaker, G.R.: Influenza virus entry and infection require host cell N-linked glycoprotein. Proc. Natl. Acad. Sci. USA 101, 18153-8 (2004)
    • (2004) Proc. Natl. Acad. Sci. , vol.101 , pp. 18153-18158
    • Chu, V.C.1    Whittaker, G.R.2
  • 23
    • 0038314400 scopus 로고    scopus 로고
    • Virus entry, assembly, budding, and membrane rafts
    • Chazal, N., Gerlier, D.: Virus entry, assembly, budding, and membrane rafts. Microbiol Mol Biol Rev 67, 226-37 (2003)
    • (2003) Microbiol. Mol. Biol. Rev. , vol.67 , pp. 226-237
    • Chazal, N.1    Gerlier, D.2
  • 24
    • 7444272134 scopus 로고    scopus 로고
    • The role of lipid microdomains in virus biology
    • Nayak, D.P., Hui, E.K.: The role of lipid microdomains in virus biology. Subcell Biochem. 37, 443-91 (2004)
    • (2004) Subcell Biochem. , vol.37 , pp. 443-491
    • Nayak, D.P.1    Hui, E.K.2
  • 25
    • 0016679968 scopus 로고
    • Activation of influenza A viruses by trypsin treatment
    • Klenk, H-D, Rott, R., Orlich, M., Blodorn, J.: Activation of influenza A viruses by trypsin treatment. Virology 68, 426-39 (1975)
    • (1975) Virology , vol.68 , pp. 426-439
    • Klenk, H.-D.1    Rott, R.2    Orlich, M.3    Blodorn, J.4
  • 26
    • 0028123337 scopus 로고
    • Host cell proteases controlling virus pathogenicity
    • Klenk, H-D, Garten, W.: Host cell proteases controlling virus pathogenicity. Trends Microbiol 2, 39-43 (1994)
    • (1994) Trends Microbiol. , vol.2 , pp. 39-43
    • Klenk, H.-D.1    Garten, W.2
  • 27
    • 0015588595 scopus 로고
    • Proteolytic cleavage of the hemagglutinin polypeptide of influenza virus. Function of the uncleaved polypeptide HA
    • Lazarowitz, S.G., Compans, R.W., Choppin, P.W.: Proteolytic cleavage of the hemagglutinin polypeptide of influenza virus. Function of the uncleaved polypeptide HA. Virology 52, 199-212 (1973)
    • (1973) Virology , vol.52 , pp. 199-212
    • Lazarowitz, S.G.1    Compans, R.W.2    Choppin, P.W.3
  • 28
    • 0032544055 scopus 로고    scopus 로고
    • A novel mechanism for the acquisition of virulence by a human influenza A virus
    • USA
    • Goto, H., Kawaoka, Y.: A novel mechanism for the acquisition of virulence by a human influenza A virus. Proc. Natl. Acad. Sci. USA 95, 10224-8 (1998)
    • (1998) Proc. Natl. Acad. Sci. , vol.95 , pp. 10224-10228
    • Goto, H.1    Kawaoka, Y.2
  • 29
    • 0033607680 scopus 로고    scopus 로고
    • Glycosphingolipids are not essential for formation of detergent-resistant membrane rafts in melanoma cells. Methylbeta-cyclodextrin does not affect cell surface transport of a GPI-anchored protein
    • Ostermeyer, A.G., Beckrich, B.T., Ivarson, K.A., Grove, K.E., Brown, D.A.: Glycosphingolipids are not essential for formation of detergent-resistant membrane rafts in melanoma cells. methylbeta-cyclodextrin does not affect cell surface transport of a GPI-anchored protein. J. Biol. Chem. 274, 34459-66 (1999)
    • (1999) J. Biol. Chem. , vol.274 , pp. 34459-34466
    • Ostermeyer, A.G.1    Beckrich, B.T.2    Ivarson, K.A.3    Grove, K.E.4    Brown, D.A.5
  • 30
    • 0034534267 scopus 로고    scopus 로고
    • Lipid membrane domains in cell surface and vacuolar systems
    • Kobayashi, T., Hirabayashi, Y.: Lipid membrane domains in cell surface and vacuolar systems. Glycoconj. J. 17, 163-71 (2000)
    • (2000) Glycoconj. J. , vol.17 , pp. 163-171
    • Kobayashi, T.1    Hirabayashi, Y.2


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