메뉴 건너뛰기




Volumn 70, Issue 3, 1996, Pages 1818-1827

Characterization of mutants of influenza A virus selected with the neuraminidase inhibitor 4-guanidino-Neu5Ac2en

Author keywords

[No Author keywords available]

Indexed keywords

SIALIDASE INHIBITOR;

EID: 0030028671     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.70.3.1818-1827.1996     Document Type: Article
Times cited : (197)

References (34)
  • 1
    • 0017411851 scopus 로고
    • Amantadine-resistance as a genetic marker for influenza viruses
    • Appleyard, G. 1977. Amantadine-resistance as a genetic marker for influenza viruses. J. Gen. Virol. 36:249-255.
    • (1977) J. Gen. Virol. , vol.36 , pp. 249-255
    • Appleyard, G.1
  • 3
    • 0018979049 scopus 로고
    • Electrophorctic analysis of iodine-labeled influenza virus RNA segments
    • Bean, W. J., G. Sriram, and R. G. Webster. 1980. Electrophorctic analysis of iodine-labeled influenza virus RNA segments. Anal Biochem. 102:228-232
    • (1980) Anal Biochem. , vol.102 , pp. 228-232
    • Bean, W.J.1    Sriram, G.2    Webster, R.G.3
  • 4
    • 0024348490 scopus 로고
    • Biological potential of amantadine-resistant influenza A virus in an avian model
    • Bean, W. J., S. C. Threlkeld, and R. G. Webster. 1989. Biological potential of amantadine-resistant influenza A virus in an avian model. J. Infect. Dis 159:1050-1056.
    • (1989) J. Infect. Dis , vol.159 , pp. 1050-1056
    • Bean, W.J.1    Threlkeld, S.C.2    Webster, R.G.3
  • 5
    • 9044242047 scopus 로고
    • Crystalline antigen from ihe influenza virus envelope
    • Brand, C. M., and J. J. Skehel. 1972. Crystalline antigen from ihe influenza virus envelope. Nature (London) 238:366-373.
    • (1972) Nature (London) , vol.238 , pp. 366-373
    • Brand, C.M.1    Skehel, J.J.2
  • 6
    • 84958058579 scopus 로고
    • Mucin and mucoids in relation to influenza virus action IV. Inhibition by purified mucoid of infection and haemagglutinin with the virus strain WSE
    • Burnet, F. M. 1948. Mucin and mucoids in relation to influenza virus action IV. Inhibition by purified mucoid of infection and haemagglutinin with the virus strain WSE. Aust. J. Exp. Biol. Med Sci 26:381-387
    • (1948) Aust. J. Exp. Biol. Med Sci , vol.26 , pp. 381-387
    • Burnet, F.M.1
  • 8
    • 0002834361 scopus 로고
    • Neuraminidase: Enzyme and antigen
    • R. M. Krug (ed). Plenum Press, NY
    • Colman, P. M. 1989 Neuraminidase: enzyme and antigen. p 175-218. In R. M. Krug (ed). The influenza viruses. Plenum Press, NY
    • (1989) The Influenza Viruses , pp. 175-218
    • Colman, P.M.1
  • 9
    • 0028113435 scopus 로고
    • Influenza virus neuraminidase: Structure. antibodies. and inhibitors
    • Review
    • Colman, P. M. 1994. Influenza virus neuraminidase: structure. antibodies. and inhibitors. Protein Sci. 3:1687-1696. (Review.)
    • (1994) Protein Sci. , vol.3 , pp. 1687-1696
    • Colman, P.M.1
  • 10
    • 0020633096 scopus 로고
    • Structure of the catalytic and antigenic sites in influenza virus neuraminidase
    • Colman, P. M., J. N. Varghese, and W. G. Laver. 1983. Structure of the catalytic and antigenic sites in influenza virus neuraminidase Nature (London) 303:41-44.
    • (1983) Nature (London) , vol.303 , pp. 41-44
    • Colman, P.M.1    Varghese, J.N.2    Laver, W.G.3
  • 11
    • 77049143386 scopus 로고
    • The determination of enzyme inhibitor constants
    • Dixon, M. 1953. The determination of enzyme inhibitor constants. Biochem J. 55:170-171.
    • (1953) Biochem J. , vol.55 , pp. 170-171
    • Dixon, M.1
  • 12
    • 0020611458 scopus 로고
    • Effect of hevose starvation and the role of sialic acid in influenza virus release
    • Griffin, J. A., S. Basak, and R. W. Compans. 1983 Effect of hevose 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
  • 13
    • 0029550466 scopus 로고
    • 2,3-Didehydro-2,4-dideoxy-guanidino-N-acetyl-D-neuraminic acid (4-guanidino-Neu5Ac2en) is a slow, binding inhibitor of sialidase from both influenza A virus and influenza B virus
    • Hart, G. J., and R. C. Bethell. 1995. 2,3-Didehydro-2,4-dideoxy-guanidino-N-acetyl-D-neuraminic acid (4-guanidino-Neu5Ac2en) is a slow, binding inhibitor of sialidase from both influenza A virus and influenza B virus. Biochem. Mol. Biol. Int 36:695-703.
    • (1995) Biochem. Mol. Biol. Int , vol.36 , pp. 695-703
    • Hart, G.J.1    Bethell, R.C.2
  • 14
    • 0024819536 scopus 로고
    • Emergence and apparent transmission of rimandine-resistant influenza A virus in families
    • Hayden, F. G., R. B. Belshe, R. D. Clover, A. J. Hay, M. G. Oakes, and W. Soo. 1989. Emergence and apparent transmission of rimandine-resistant influenza A virus in families N. Engl. J. Med. 321:1696-1702
    • (1989) N. Engl. J. Med. , vol.321 , pp. 1696-1702
    • Hayden, F.G.1    Belshe, R.B.2    Clover, R.D.3    Hay, A.J.4    Oakes, M.G.5    Soo, W.6
  • 15
    • 0018875646 scopus 로고
    • Ploquo inhibition assay for drug susceptibility testing of influenza viruses
    • Hayden, F. G., K. M. Cote, and R. G. Douglas, Jr. 1980. Ploquo inhibition assay for drug susceptibility testing of influenza viruses. Antimicrob Agents Chemother. 17:865-870.
    • (1980) Antimicrob Agents Chemother. , vol.17 , pp. 865-870
    • Hayden, F.G.1    Cote, K.M.2    Douglas Jr., R.G.3
  • 16
    • 0344597456 scopus 로고
    • Clinical and epidermological importance of influenza A viruses resistant to amantadine and rimantadine
    • C. Hannoun, A. P Kendal, H. D. Klenk, and F. L. Ruben (ed.), Excerpta Medica, Amsterdam
    • Hayden, F. G., and R. B. Couch. 1993. Clinical and epidermological importance of influenza A viruses resistant to amantadine and rimantadine, p. 333-342. In C. Hannoun, A. P Kendal, H. D. Klenk, and F. L. Ruben (ed.), Options for the control of influenza II. Excerpta Medica, Amsterdam.
    • (1993) Options for the Control of Influenza II , pp. 333-342
    • Hayden, F.G.1    Couch, R.B.2
  • 17
    • 0027287318 scopus 로고
    • Inhibition of sialidases from viral, bacterial and mammalian sources by analogues of 2-deoxy-2,3-didehydro-N-acetylneuraminic acid modified at the C-4 position
    • Holzer, C. T., M. von Itzstein, B. Jin, M. S. Pegg, W. P. Stewart, and W.-Y. Wu. 1993 Inhibition of sialidases from viral, bacterial and mammalian sources by analogues of 2-deoxy-2,3-didehydro-N-acetylneuraminic acid modified at the C-4 position. Glycoconjugate J. 10:40-44.
    • (1993) Glycoconjugate J. , vol.10 , pp. 40-44
    • Holzer, C.T.1    Von Itzstein, M.2    Jin, B.3    Pegg, M.S.4    Stewart, W.P.5    Wu, W.-Y.6
  • 18
    • 0018177170 scopus 로고
    • Effects of sialylation of influenza virions on their interactions with host cells and erythrocytes
    • Lakshmi, M. V., and I. T. Schulze, 1978. Effects of sialylation of influenza virions on their interactions with host cells and erythrocytes. Virology 88:314-324.
    • (1978) Virology , vol.88 , pp. 314-324
    • Lakshmi, M.V.1    Schulze, I.T.2
  • 19
    • 0028813628 scopus 로고
    • Influenza type A virus neurammidase does not play a role in viral entry, replication, assembly, or budding
    • Liu, C., M. C. Eichelberger, R. W. Comparts, and G. M. Air. 1995. Influenza type A virus neurammidase 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    Comparts, R.W.3    Air, G.M.4
  • 21
    • 0019814443 scopus 로고
    • Infectious entry pathway of influenza virus in a canine kidney cell line
    • Matlin, K. S., H. Reggio, A. Helenius, and K. Simons. 1981. Infectious entry pathway of influenza virus in a canine kidney cell line. J. Cell Biol. 91:601-613
    • (1981) J. Cell Biol. , vol.91 , pp. 601-613
    • Matlin, K.S.1    Reggio, H.2    Helenius, A.3    Simons, K.4
  • 22
    • 0014931976 scopus 로고
    • In vivo selection of an influenza A2 strain resistant to amantadine
    • Oxford, J. S., L. S. Logan, and C. W. Potter. 1970. In vivo selection of an influenza A2 strain resistant to amantadine. Nature (London) 226:82-83.
    • (1970) Nature (London) , vol.226 , pp. 82-83
    • Oxford, J.S.1    Logan, L.S.2    Potter, C.W.3
  • 23
    • 0017151109 scopus 로고
    • Inhibition of influenza virus replication in tissue culture by 2-deoxy-2,3-dehydro-N-trifluoro-acetyl-neuraminic acid (FANA): Mechanism of action
    • Palese, P., and R. W. Compans. 1976. Inhibition of influenza virus replication in tissue culture by 2-deoxy-2,3-dehydro-N-trifluoro-acetyl-neuraminic 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
  • 24
    • 0000225764 scopus 로고
    • Inhibitors of viral neuraminidase as potential antiviral drugs
    • J. S. Oxford (ed.), CRC Press. Inc, Cleveland
    • Palese, P., and J. L. Schulman. 1977. Inhibitors of viral neuraminidase as potential antiviral drugs, p. 189-205. In J. S. Oxford (ed.), Chemoprophylaxis and virus infections of the respiratory tract. CRC Press. Inc, Cleveland.
    • (1977) Chemoprophylaxis and Virus Infections of the Respiratory Tract , pp. 189-205
    • Palese, P.1    Schulman, J.L.2
  • 25
    • 0016272701 scopus 로고
    • Characterization of temperature sensitive influenza virus mutants defective in neuraminidase
    • Palese, P., K. Tobita, M. Ueda, and R. W. Compans. 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
  • 26
    • 0022477122 scopus 로고
    • Measurement of the mutation rates of animal viruses: Influenza A virus and poliovirus type 1
    • Parvin, J. D., A. Moscona, W. T. Pan, J. M. Leider, and P. Palese. 1986. Measurement of the mutation rates of animal viruses: influenza A virus and poliovirus type 1. J. Virol. 59:377-383.
    • (1986) J. Virol. , vol.59 , pp. 377-383
    • Parvin, J.D.1    Moscona, A.2    Pan, W.T.3    Leider, J.M.4    Palese, P.5
  • 27
    • 0027981472 scopus 로고
    • Inhibition of influenza virus replication in mice by GG167 (4-guanidmo-2,4-dideoxy-2,3-dehydro-N-acetylneurarminic acid) is consistent with extracellular activity of viral neuraminidase (sialidase)
    • Ryan, D. M., J. Ticehurst, M. H. Dempsey, and C. R. Penn. 1994. Inhibition of influenza virus replication in mice by GG167 (4-guanidmo-2,4-dideoxy-2,3-dehydro-N-acetylneurarminic acid) is consistent with extracellular activity of viral neuraminidase (sialidase). Antimicrob. Agents Chemother. 38:2270-2275
    • (1994) Antimicrob. Agents Chemother. , vol.38 , pp. 2270-2275
    • Ryan, D.M.1    Ticehurst, J.2    Dempsey, M.H.3    Penn, C.R.4
  • 29
    • 0020626583 scopus 로고
    • Evidence for host-cell selection of influenza virus antigenic variants
    • Schild, G. C., J. S. Oxford, J. C. de Jong, and R. G. Webster. 1983. Evidence for host-cell selection of influenza virus antigenic variants Nature (London) 303:706-709.
    • (1983) Nature (London) , vol.303 , pp. 706-709
    • Schild, G.C.1    Oxford, J.S.2    De Jong, J.C.3    Webster, R.G.4
  • 30
    • 0016433781 scopus 로고
    • Susceptibility of different strains of influenza A virus to the inhibitory effects of 2-deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid (FANA)
    • Schulman, J. L., and P. Palese. 1975. Susceptibility of different strains of influenza A virus to the inhibitory effects of 2-deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid (FANA). Virology 63:98-104
    • (1975) Virology , vol.63 , pp. 98-104
    • Schulman, J.L.1    Palese, P.2
  • 31
    • 0027967179 scopus 로고
    • Inhibition of the growth of influenza viruses in vitro by 4-guanidino-2,4-dideoxy-N-acetylneuraminic acid
    • Thomas, G. P., M. Forsyth, C. R. Penn, and J. W. McCauley. 1994. Inhibition of the growth of influenza viruses in vitro by 4-guanidino-2,4-dideoxy-N-acetylneuraminic acid. Antivir. Res. 24:351-356.
    • (1994) Antivir. Res. , vol.24 , pp. 351-356
    • Thomas, G.P.1    Forsyth, M.2    Penn, C.R.3    McCauley, J.W.4
  • 33
    • 0019890491 scopus 로고
    • Structure of the hemagglutinin membrane glycoprotein of influenza virus at 3Å resolution
    • Wilson, I. A., J. J. Skehel, and D. C. Wiley. 1981. Structure of the hemagglutinin membrane glycoprotein of influenza virus at 3Å resolution. Nature (London) 289:366-373.
    • (1981) Nature (London) , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 34
    • 0027162942 scopus 로고
    • 4-Guanidino-2,4-dideoxy-2,3-dehydro-N-acetylneuraminic acid is a highly effective inhibitor both of the sialidase (neuraminidase) and of growth of a wide range of influenza A and B viruses in vitro
    • Woods, J. M., R. C. Bethell, J. A. V. Coates, N. Healy, S. A. Hiscox, B. A. Pearson, D. M. Ryan, J. Ticehurst, J. Tilling, S. M. Walcott, and C. R. Penn. 1993. 4-Guanidino-2,4-dideoxy-2,3-dehydro-N-acetylneuraminic acid is a highly effective inhibitor both of the sialidase (neuraminidase) and of growth of a wide range of influenza A and B viruses in vitro. Antimicrob. Agents Chemother. 37:1473-1479.
    • (1993) Antimicrob. Agents Chemother. , vol.37 , pp. 1473-1479
    • Woods, J.M.1    Bethell, R.C.2    Coates, J.A.V.3    Healy, N.4    Hiscox, S.A.5    Pearson, B.A.6    Ryan, D.M.7    Ticehurst, J.8    Tilling, J.9    Walcott, S.M.10    Penn, C.R.11


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.