메뉴 건너뛰기




Volumn 218, Issue 1, 1996, Pages 127-133

Transfer of an esterase-resistant receptor analog to the surface of influenza C virions results in reduced infectivity due to aggregate formation

Author keywords

[No Author keywords available]

Indexed keywords

ESTERASE; SIALIC ACID DERIVATIVE; VIRUS GLYCOPROTEIN;

EID: 0343807503     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1996.0172     Document Type: Article
Times cited : (19)

References (30)
  • 1
    • 0028672847 scopus 로고
    • Sialic acid analogs and application for preparation of neoglycoconjugates
    • Brossmer, R., and Gross, H. J. (1994). Sialic acid analogs and application for preparation of neoglycoconjugates. Methods Enzymol. 247B, 153-176.
    • (1994) Methods Enzymol. , vol.247 B , pp. 153-176
    • Brossmer, R.1    Gross, H.J.2
  • 2
    • 0027158246 scopus 로고
    • A sialic acid analogue acting as a receptor determinant for binding but not for infection by influenza C virus
    • Brossmer, R., Isecke, R., and Herrler, G. (1993). A sialic acid analogue acting as a receptor determinant for binding but not for infection by influenza C virus. FEBS Lett. 323, 96-98.
    • (1993) FEBS Lett. , vol.323 , pp. 96-98
    • Brossmer, R.1    Isecke, R.2    Herrler, G.3
  • 3
    • 0014594355 scopus 로고
    • Effect of antibody to neuraminidase on the maturation and hemagglutinating activity of an influenza A2 virus
    • Compans, R. W., Dimmock, N. J., and Meier-Ewert, H. (1969). Effect of antibody to neuraminidase on the maturation and hemagglutinating activity of an influenza A2 virus. J. Virol. 4, 528-534.
    • (1969) J. Virol. , vol.4 , pp. 528-534
    • Compans, R.W.1    Dimmock, N.J.2    Meier-Ewert, H.3
  • 4
    • 0015452389 scopus 로고
    • Viral and bacterial neuraminidases
    • Drzeniek, R. (1972). Viral and bacterial neuraminidases. Curr. Top. Mirobiol. Immunol. 59, 35-74.
    • (1972) Curr. Top. Mirobiol. Immunol. , vol.59 , pp. 35-74
    • Drzeniek, R.1
  • 5
    • 0021751195 scopus 로고
    • Vesicular stomatitis virus infects and matures only through the basolateral surface of the polarized epithelial cell line, MDCK
    • Fuller, S. D., von Bonsdorff, C.-H., and Simons, K. (1984). Vesicular stomatitis virus infects and matures only through the basolateral surface of the polarized epithelial cell line, MDCK. Cell 38, 65-77.
    • (1984) Cell , vol.38 , pp. 65-77
    • Fuller, S.D.1    Von Bonsdorff, C.-H.2    Simons, K.3
  • 6
    • 0012464505 scopus 로고
    • Glycoproteins as influenza virus hemagglutinin inhibitors and as cellular virus receptors
    • (A. Gottschalk, Ed.), Elsevier, Amsterdam
    • Gottschalk, A., Belyavin, G., and Biddle, F. (1972). Glycoproteins as influenza virus hemagglutinin inhibitors and as cellular virus receptors. In "Glycoproteins: Their Composition, Structure and Function" (A. Gottschalk, Ed.), pp. 1082-1096. Elsevier, Amsterdam.
    • (1972) Glycoproteins: Their Composition, Structure and Function , pp. 1082-1096
    • Gottschalk, A.1    Belyavin, G.2    Biddle, F.3
  • 7
    • 0018575349 scopus 로고
    • A precursor glycoprotein in influenza C virus
    • Herrler, G., Compans, R. W., and Meier-Ewert, H. (1979). A precursor glycoprotein in influenza C virus. Virology 99, 49-56.
    • (1979) Virology , vol.99 , pp. 49-56
    • Herrler, G.1    Compans, R.W.2    Meier-Ewert, H.3
  • 8
    • 0023878766 scopus 로고
    • The glycoprotein of influenza C virus is the haemagglutinin, esterase and fusion factor
    • Herrler, G., Durkop, I., Becht, H., and Klenk, H. D. (1988). The glycoprotein of influenza C virus is the haemagglutinin, esterase and fusion factor. J. Gen. Virol. 69, 839-846.
    • (1988) J. Gen. Virol. , vol.69 , pp. 839-846
    • Herrler, G.1    Durkop, I.2    Becht, H.3    Klenk, H.D.4
  • 9
    • 0026708107 scopus 로고
    • A synthetic sialic acid analogue is recognized by influenza C virus as a receptor determinant but is resistant to the receptor-destroying enzyme
    • Herrler, G., Gross, H. J., Imhof, A., Brossmer, R., Milks, G., and Paulson, J. C. (1992). A synthetic sialic acid analogue is recognized by influenza C virus as a receptor determinant but is resistant to the receptor-destroying enzyme. J. Biol. Chem. 267, 12501-12505.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12501-12505
    • Herrler, G.1    Gross, H.J.2    Imhof, A.3    Brossmer, R.4    Milks, G.5    Paulson, J.C.6
  • 10
    • 0021945971 scopus 로고
    • Neuraminic acid is involved in the binding of influenza C virus to erythrocytes
    • Herrler, G., Rott, R., and Klenk, H.-D. (1985a). Neuraminic acid is involved in the binding of influenza C virus to erythrocytes. Virology 141, 144-147.
    • (1985) Virology , vol.141 , pp. 144-147
    • Herrler, G.1    Rott, R.2    Klenk, H.-D.3
  • 11
    • 0344036042 scopus 로고
    • The receptor-destroying enzyme of influenza C virus is neuraminate-O-acetylesterase
    • Herrler, G., Rott, R., Klenk, H. D., Muller, H. P., Shukla, A. K., and Schauer, R. (1985b). The receptor-destroying enzyme of influenza C virus is neuraminate-O-acetylesterase. EMBO J. 4, 1503-1506.
    • (1985) EMBO J. , vol.4 , pp. 1503-1506
    • Herrler, G.1    Rott, R.2    Klenk, H.D.3    Muller, H.P.4    Shukla, A.K.5    Schauer, R.6
  • 12
    • 0026199508 scopus 로고
    • 9-O-acetylated sialic acid, a receptor determinant for influenza C virus and coronaviruses
    • Herrler, G., Szepanski, S., and Schultze, B. (1991). 9-O-Acetylated sialic acid, a receptor determinant for influenza C virus and coronaviruses. Behring Inst. Mitt. 89, 177-184.
    • (1991) Behring Inst. Mitt. , vol.89 , pp. 177-184
    • Herrler, G.1    Szepanski, S.2    Schultze, B.3
  • 13
    • 0021944043 scopus 로고
    • Further studies on the role of neuraminidase and the mechanism of low pH dependence in influenza virus-induced membrane fusion
    • Huang, R. T. C., Dietsch, E., and Rott, R. (1985). Further studies on the role of neuraminidase and the mechanism of low pH dependence in influenza virus-induced membrane fusion. J. Gen. Virol. 66, 295-301.
    • (1985) J. Gen. Virol. , vol.66 , pp. 295-301
    • Huang, R.T.C.1    Dietsch, E.2    Rott, R.3
  • 14
    • 0019165295 scopus 로고
    • Function of neuraminidase in membrane fusion induced by myxoviruses
    • Huang, R. T. C., Rott, R., Wahn, K., Klenk, H.-D., and Kohama, T. (1980). Function of neuraminidase in membrane fusion induced by myxoviruses. Virology 107, 313-319.
    • (1980) Virology , vol.107 , pp. 313-319
    • Huang, R.T.C.1    Rott, R.2    Wahn, K.3    Klenk, H.-D.4    Kohama, T.5
  • 15
    • 0027261465 scopus 로고
    • Selection and characterization of a neuraminidase-minus mutant of influenza virus and its rescue by cloned neuraminidase genes
    • Liu, C., and Air, G. (1993). Selection and characterization of a neuraminidase-minus mutant of influenza virus and its rescue by cloned neuraminidase genes. Virology 194, 403-407.
    • (1993) Virology , vol.194 , pp. 403-407
    • Liu, C.1    Air, G.2
  • 16
    • 0028813628 scopus 로고
    • Influenza type A virus neuraminidase does not play a role in viral entry, replication, assembly, or budding
    • Liu, C., Eichelberger, M. C., Compans, R. W., and Air, G. M. (1995). Influenza type A virus neuraminidase does not play a role in viral entry, replication, assembly, or budding. J. Virol. 69, 1099-1106.
    • (1995) J. Virol. , vol.69 , pp. 1099-1106
    • Liu, C.1    Eichelberger, M.C.2    Compans, R.W.3    Air, G.M.4
  • 17
    • 0343589722 scopus 로고
    • Molecular analysis of influenza C virus
    • (B. W. J. Mahy and R. D. Barry, Eds.), Academic Press, New York
    • Meier-Ewert, H., Compans, R. W., Bishop, D. H. L., and Herrler, G. (1978). Molecular analysis of influenza C virus. In "Negative Strand Viruses and the Host Cell" (B. W. J. Mahy and R. D. Barry, Eds.), pp. 127-133. Academic Press, New York.
    • (1978) Negative Strand Viruses and the Host Cell , pp. 127-133
    • Meier-Ewert, H.1    Compans, R.W.2    Bishop, D.H.L.3    Herrler, G.4
  • 19
    • 0028828081 scopus 로고
    • Neuraminidase is essential for fowl plague virus hemagglutinin to show hemagglutinating activity
    • Ohuchi, M., Feldmann, A., Ohuchi, R., and Klenk, H.-D. (1995). Neuraminidase is essential for fowl plague virus hemagglutinin to show hemagglutinating activity. Virology 212, 77-83.
    • (1995) Virology , vol.212 , pp. 77-83
    • Ohuchi, M.1    Feldmann, A.2    Ohuchi, R.3    Klenk, H.-D.4
  • 20
    • 0017151109 scopus 로고
    • Inhibition of influenza virus replication in tissue culture by 2-deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid (FANA): Mechanism of action
    • Palese, P., and Compans, R. W. (1976). Inhibition of influenza virus replication in tissue culture by 2-deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid (FANA): Mechanism of action. J. Gen. Virol. 33, 159-163.
    • (1976) J. Gen. Virol. , vol.33 , pp. 159-163
    • Palese, P.1    Compans, R.W.2
  • 21
    • 0016272701 scopus 로고
    • Characterization of temperature-sensitive influenza virus mutants defective in neuraminidase
    • Palese, P., Tobita, K., Ueda, M., and Compans, R. W. (1974). Characterization of temperature-sensitive influenza virus mutants defective in neuraminidase. Virology 61, 397-410.
    • (1974) Virology , vol.61 , pp. 397-410
    • Palese, P.1    Tobita, K.2    Ueda, M.3    Compans, R.W.4
  • 22
    • 0023002952 scopus 로고
    • Influenza C virus uses 9-O-acetyl-N-acetylneuraminic acid as a high affinity receptor determinant for attachment to cells
    • Rogers, G. N., Herrler, G., Paulson, J. C., and Klenk, H.-D. (1986). Influenza C virus uses 9-O-acetyl-N-acetylneuraminic acid as a high affinity receptor determinant for attachment to cells. J. Biol. Chem. 261, 5947-5951.
    • (1986) J. Biol. Chem. , vol.261 , pp. 5947-5951
    • Rogers, G.N.1    Herrler, G.2    Paulson, J.C.3    Klenk, H.-D.4
  • 23
    • 0026085172 scopus 로고
    • The S protein of bovine coronavirus is a hemagglutinin recognizing 9-O-acetylated sialic acid as a receptor determinant
    • Schultze, B., Gross, H. J., Brossmer, R., and Herrler, G. (1991a). The S protein of bovine coronavirus is a hemagglutinin recognizing 9-O-acetylated sialic acid as a receptor determinant. J. Virol. 65, 6232-6237.
    • (1991) J. Virol. , vol.65 , pp. 6232-6237
    • Schultze, B.1    Gross, H.J.2    Brossmer, R.3    Herrler, G.4
  • 24
    • 0026023775 scopus 로고
    • Isolated HE-protein from hemagglutinating encephalomyelitis virus and bovine coronavirus has receptor-destroying and receptor-binding activity
    • Schultze, B., Wahn, K., Klenk, H. D., and Herrler, G. (1991b). Isolated HE-protein from hemagglutinating encephalomyelitis virus and bovine coronavirus has receptor-destroying and receptor-binding activity. Virology 180, 221-228.
    • (1991) Virology , vol.180 , pp. 221-228
    • Schultze, B.1    Wahn, K.2    Klenk, H.D.3    Herrler, G.4
  • 26
    • 0025770828 scopus 로고
    • Purification and characterization of alpha (2,6)-sialyltransferase from human liver
    • Sticher, U., Gross, H. J., and Brossmer, R. (1991). Purification and characterization of alpha (2,6)-sialyltransferase from human liver. Glycoconjugate J. 8, 45-54.
    • (1991) Glycoconjugate J. , vol.8 , pp. 45-54
    • Sticher, U.1    Gross, H.J.2    Brossmer, R.3
  • 27
    • 0027327591 scopus 로고
    • The receptor-destroying enzyme of influenza C virus is required for entry into target cells
    • Strobl, B., and Vlasak, R. (1993). The receptor-destroying enzyme of influenza C virus is required for entry into target cells. Virology 192, 679-682.
    • (1993) Virology , vol.192 , pp. 679-682
    • Strobl, B.1    Vlasak, R.2
  • 28
    • 0019455447 scopus 로고
    • Effects of various proteases on the glycoprotein composition and the infectivity of influenza C virus
    • Sugawara, K., Ohuchi, M., Nakamura, K., and Homma, M. (1981). Effects of various proteases on the glycoprotein composition and the infectivity of influenza C virus. Arch. Virol. 68, 147-151.
    • (1981) Arch. Virol. , vol.68 , pp. 147-151
    • Sugawara, K.1    Ohuchi, M.2    Nakamura, K.3    Homma, M.4
  • 29
    • 0023429281 scopus 로고
    • The influenza C virus glycoprotein (HE) exhibits receptor-binding (hemagglutinin) and receptor-destroying (esterase) activities
    • Vlasak, R., Krystal, M., Nacht, M., and Palese, P. (1987). The influenza C virus glycoprotein (HE) exhibits receptor-binding (hemagglutinin) and receptor-destroying (esterase) activities. Virology 160, 419-425.
    • (1987) Virology , vol.160 , pp. 419-425
    • Vlasak, R.1    Krystal, M.2    Nacht, M.3    Palese, P.4
  • 30
    • 0024543947 scopus 로고
    • Influenza C virus esterase: Analysis of catalytic site, inhibition, and possible function
    • Vlasak, R., Muster, T., Lauro, A. M., Powers, J. C., and Palese, P. (1989). Influenza C virus esterase: Analysis of catalytic site, inhibition, and possible function. J. Virol. 63, 2056-2562.
    • (1989) J. Virol. , vol.63 , pp. 2056-2562
    • Vlasak, R.1    Muster, T.2    Lauro, A.M.3    Powers, J.C.4    Palese, P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.