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Volumn 226, Issue 1, 1996, Pages 66-76

Characterization of a hemagglutinin-specific inhibitor of influenza A virus

Author keywords

[No Author keywords available]

Indexed keywords

ANTIVIRUS AGENT; BMY 27709; HEMAGGLUTININ; UNCLASSIFIED DRUG;

EID: 0030560967     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1996.0628     Document Type: Article
Times cited : (74)

References (56)
  • 1
    • 0024827395 scopus 로고
    • The neuraminidase of influenza virus
    • Air, G., and Laver, W. G. (1989). The neuraminidase of influenza virus. Proteins 6, 341-356.
    • (1989) Proteins , vol.6 , pp. 341-356
    • Air, G.1    Laver, W.G.2
  • 2
    • 0002947563 scopus 로고
    • Growth, purification and titration on influenza viruses
    • B. W. J. Mahy, Ed., IRL Press, Oxford, UK
    • Barrett, T., and Inglis, S. C. (1985). Growth, purification and titration on influenza viruses. In "Virology: A Practical Approach" (B. W. J. Mahy, Ed.), pp. 119-150. IRL Press, Oxford, UK.
    • (1985) Virology: A Practical Approach , pp. 119-150
    • Barrett, T.1    Inglis, S.C.2
  • 3
    • 0027523625 scopus 로고
    • Inhibition of the fusion-inducing conformational change of influenza hemagglutinin by benzoquinones and hydroquinones
    • Bodian, D. L., Yamasaki, R. B., Stearns, R. L., Steven, J. F., White, J. M., and Kuntz, I. D. (1993). Inhibition of the fusion-inducing conformational change of influenza hemagglutinin by benzoquinones and hydroquinones. Biochemistry 32, 2967-2978.
    • (1993) Biochemistry , vol.32 , pp. 2967-2978
    • Bodian, D.L.1    Yamasaki, R.B.2    Stearns, R.L.3    Steven, J.F.4    White, J.M.5    Kuntz, I.D.6
  • 4
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough, P. A., Hughson, F. M., Skehel, J. J., and Wiley, D. C. (1994). Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 371, 37-43.
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 5
    • 0027253445 scopus 로고
    • A spring-loaded mechanism for the conformational change of influenza hemagglutinin
    • Carr, C. M., and. Kim, P. S. (1993). A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell 73, 823-832.
    • (1993) Cell , vol.73 , pp. 823-832
    • Carr, C.M.1    Kim, P.S.2
  • 6
    • 0028089983 scopus 로고
    • Flu virus invasion: Halfway there
    • Carr, C. M., and Kim, P. S. (1994). Flu Virus Invasion: Halfway There. Science 266, 234-236.
    • (1994) Science , vol.266 , pp. 234-236
    • Carr, C.M.1    Kim, P.S.2
  • 7
    • 0027128105 scopus 로고
    • Outbreak of influenza A in a nursing home - New York, December 1991-January 1992
    • Centers for Disease Control. (1992). Outbreak of Influenza A in a nursing home - New York, December 1991-January 1992. Morbid. Mortal. Weekly Rep. 41, 129-131.
    • (1992) Morbid. Mortal. Weekly Rep. , vol.41 , pp. 129-131
  • 9
    • 0002834361 scopus 로고
    • Neuraminidase, enzyme and antigen
    • R. M. Krug, Ed., Plenum Press, NY
    • Colman, P. M. (1989). Neuraminidase, enzyme and antigen. In "The Influenza Viruses" (R. M. Krug, Ed.), pp. 175-218. Plenum Press, NY.
    • (1989) The Influenza Viruses , pp. 175-218
    • Colman, P.M.1
  • 10
    • 0028113435 scopus 로고
    • Influenza virus neuraminidase: Structure, antibodies, and inhibitors
    • Colman, P. M. (1994). Influenza virus neuraminidase: Structure, Antibodies, and Inhibitors. Protein Sci. 3, 1687-1696.
    • (1994) Protein Sci. , vol.3 , pp. 1687-1696
    • Colman, P.M.1
  • 11
    • 0025314308 scopus 로고
    • Introduction of site specific mutations into the genome of influenza virus
    • Enami, M., Luytjes, W., Krystal, M., and Palese, P. (1990). Introduction of site specific mutations into the genome of influenza virus. Proc. Nat. Acad. Sci. USA 87, 3802-3805.
    • (1990) Proc. Nat. Acad. Sci. USA , vol.87 , pp. 3802-3805
    • Enami, M.1    Luytjes, W.2    Krystal, M.3    Palese, P.4
  • 12
    • 0025850680 scopus 로고
    • High-efficiency formation of influenza virus transfectants
    • Enami, M., and Palese, P. (1991). High-efficiency formation of influenza virus transfectants. J. Virol. 65, 2711-2713.
    • (1991) J. Virol. , vol.65 , pp. 2711-2713
    • Enami, M.1    Palese, P.2
  • 13
    • 0002988267 scopus 로고
    • The action of amantadine against influenza A viruses; inhibition of the M2 ion channel protein
    • Hay., A. J. (1992). The action of amantadine against influenza A viruses; inhibition of the M2 ion channel protein. Semin. Virol. 3, 21-30.
    • (1992) Semin. Virol. , vol.3 , pp. 21-30
    • Hay, A.J.1
  • 14
    • 0024819536 scopus 로고
    • Emergence and apparent transmission of rimantadine-resistant influenza A virus in families
    • Hayden, F. G., Belshe, R. B., Glover, R. D., Hay, A. J., Oakes, M. G., and Soo, W. (1989). Emergence and apparent transmission of rimantadine-resistant influenza A virus in families. N. Engl. J. Med. 321 (25), 1696-1702.
    • (1989) N. Engl. J. Med. , vol.321 , Issue.25 , pp. 1696-1702
    • Hayden, F.G.1    Belshe, R.B.2    Glover, R.D.3    Hay, A.J.4    Oakes, M.G.5    Soo, W.6
  • 15
    • 0030032258 scopus 로고    scopus 로고
    • Safety and efficacy of the neuraminidase inhibitor GG-167 in experimental human influenza
    • Hayden, F., Treanor, J. J., Betts, R. F., Lobo, M., Esinhart, J., and Hussey, E. (1996). Safety and efficacy of the neuraminidase inhibitor GG-167 in experimental human influenza. J. Am. Med. Assoc. 275, 295-299.
    • (1996) J. Am. Med. Assoc. , vol.275 , pp. 295-299
    • Hayden, F.1    Treanor, J.J.2    Betts, R.F.3    Lobo, M.4    Esinhart, J.5    Hussey, E.6
  • 16
    • 0030007129 scopus 로고    scopus 로고
    • Anti-influenza virus activities of 4-substituted 2,4-dioxobutanoic acid inhibitors
    • Hastings, J. C., Selnick, H., Wolanski, B., and Tomassini, J. E. (1996). Anti-influenza virus activities of 4-substituted 2,4-dioxobutanoic acid inhibitors. Antimicrob. Agents Chemother. 40, 1304-1307.
    • (1996) Antimicrob. Agents Chemother. , vol.40 , pp. 1304-1307
    • Hastings, J.C.1    Selnick, H.2    Wolanski, B.3    Tomassini, J.E.4
  • 17
    • 0026664025 scopus 로고
    • Unpacking the incoming influenza virus
    • Helenius, A. (1992). Unpacking the incoming influenza virus. Cell 69, 577-578.
    • (1992) Cell , vol.69 , pp. 577-578
    • Helenius, A.1
  • 19
    • 0019400775 scopus 로고
    • Complete sequence analysis shows that the hemagglutinins of the H1 and H2 subtypes of human influenza virus are closely related
    • Hiti, A. L., Davis, A. R., and Nayak, D. R. (1981). Complete sequence analysis shows that the hemagglutinins of the H1 and H2 subtypes of human influenza virus are closely related. Virology 111, 113-124.
    • (1981) Virology , vol.111 , pp. 113-124
    • Hiti, A.L.1    Davis, A.R.2    Nayak, D.R.3
  • 20
    • 0024990401 scopus 로고
    • Determination of influenza virus proteins required for genome replication
    • Huang, T.-S.,. Palese, P., and Krystal, M. (1990). Determination of influenza virus proteins required for genome replication. J. Virol. 64, 5669-5673.
    • (1990) J. Virol. , vol.64 , pp. 5669-5673
    • Huang, T.-S.1    Palese, P.2    Krystal, M.3
  • 21
    • 0028179011 scopus 로고
    • Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion
    • Kemble, G. W., Danieli, T., and White, J. M. (1994). Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion. Cell 76, 382-391.
    • (1994) Cell , vol.76 , pp. 382-391
    • Kemble, G.W.1    Danieli, T.2    White, J.M.3
  • 22
    • 0023803844 scopus 로고
    • The molecular biology of influenza virus pathogenicity
    • Klenk, H. D., and Rott, R. (1988). The molecular biology of influenza virus pathogenicity. Adv. Virus Res. 34, 247-281.
    • (1988) Adv. Virus Res. , vol.34 , pp. 247-281
    • Klenk, H.D.1    Rott, R.2
  • 23
    • 0002210298 scopus 로고
    • Expression and replication of the influenza virus genome
    • R. M. Krug, Ed., Plenum Press, NY
    • Krug, R. M., Alonso-Caplen, F. V., Julkunen, I., and Katze, M. G. (1989). Expression and replication of the influenza virus genome. In "The Influenza Viruses" (R. M. Krug, Ed.), pp. 89-152. Plenum Press, NY.
    • (1989) The Influenza Viruses , pp. 89-152
    • Krug, R.M.1    Alonso-Caplen, F.V.2    Julkunen, I.3    Katze, M.G.4
  • 25
    • 0026598861 scopus 로고
    • Influenza A virus transfectants with chimeric hemagglutinins containing epitopes from different subtypes
    • Li, S.-Q., Schulman, J. L., Moran, T., Bona, C., and Palese, P. (1992). Influenza A virus transfectants with chimeric hemagglutinins containing epitopes from different subtypes. J. Virol. 66, 399-404.
    • (1992) J. Virol. , vol.66 , pp. 399-404
    • Li, S.-Q.1    Schulman, J.L.2    Moran, T.3    Bona, C.4    Palese, P.5
  • 26
    • 0023273975 scopus 로고
    • Impact of Influenza epidemics on mortality in the United States from October 1972 to May 1985
    • Lui, K.-J., and Kendal, A. P. (1987). Impact of Influenza epidemics on mortality in the United States from October 1972 to May 1985. Am. J. Public Health 77, 712-716.
    • (1987) Am. J. Public Health , vol.77 , pp. 712-716
    • Lui, K.-J.1    Kendal, A.P.2
  • 27
    • 0026747168 scopus 로고
    • Mechanism of attenuation of a chimeric influenza A/B transfectant virus
    • Luo, G.-X., Bergmann, M., Garcia-Sastre, A., and Palese, P. (1992). Mechanism of attenuation of a chimeric influenza A/B transfectant virus. J. Virol. 66, 4679-4685.
    • (1992) J. Virol. , vol.66 , pp. 4679-4685
    • Luo, G.-X.1    Bergmann, M.2    Garcia-Sastre, A.3    Palese, P.4
  • 28
  • 29
    • 0024846089 scopus 로고
    • Amplification, expression and packaging of a foreign gene by influenza virus
    • Luytjes, W., Krystal, M., Enami, M., Parvin, J. D., and Palese, P. (1989). Amplification, expression and packaging of a foreign gene by influenza virus. Cell 59, 1107-1113.
    • (1989) Cell , vol.59 , pp. 1107-1113
    • Luytjes, W.1    Krystal, M.2    Enami, M.3    Parvin, J.D.4    Palese, P.5
  • 30
    • 0001237715 scopus 로고
    • Orthomyxoviruses
    • B. N. Fields and D. M. Knipe, Eds., 2nd ed., Raven Press, New York
    • Murphy, B. R., and Webster, R. G. (1990). Orthomyxoviruses. In "Virology" (B. N. Fields and D. M. Knipe, Eds.), 2nd ed., pp. 1091-1152. Raven Press, New York.
    • (1990) Virology , pp. 1091-1152
    • Murphy, B.R.1    Webster, R.G.2
  • 31
    • 0026175939 scopus 로고
    • Comparison of complete amino acid sequences and receptor-binding properties among 13 serotypes of hemagglutinins of influenza A viruses
    • Nobusawa, E., Aoyama, T., Kato, H., Suzuki, Y., Tateno, Y., and Nakajima, K. (1991). Comparison of complete amino acid sequences and receptor-binding properties among 13 serotypes of hemagglutinins of influenza A viruses. Virology 182, 475-485.
    • (1991) Virology , vol.182 , pp. 475-485
    • Nobusawa, E.1    Aoyama, T.2    Kato, H.3    Suzuki, Y.4    Tateno, Y.5    Nakajima, K.6
  • 32
    • 0027952589 scopus 로고
    • Intermediates in influenza virus PR/8 haemagglutinin-induced membrane fusion
    • Pak, C. C., Krumbiegel, M., and Blumenthal, R. (1994). Intermediates in influenza virus PR/8 haemagglutinin-induced membrane fusion. J. Gen. Virol. 75, 395-399.
    • (1994) J. Gen. Virol. , vol.75 , pp. 395-399
    • Pak, C.C.1    Krumbiegel, M.2    Blumenthal, R.3
  • 33
    • 0017326035 scopus 로고
    • The genes of influenza virus
    • Palese, P. (1977). The genes of influenza virus. Cell 10, 1-10.
    • (1977) Cell , vol.10 , pp. 1-10
    • Palese, P.1
  • 34
    • 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
  • 35
    • 0026612385 scopus 로고
    • Influenza virus M2 protein has ion channel activity
    • Pinto, L. H., Holsinger, L. J., and Lamb, R. A. (1992). Influenza virus M2 protein has ion channel activity. Cell 69, 517-528.
    • (1992) Cell , vol.69 , pp. 517-528
    • Pinto, L.H.1    Holsinger, L.J.2    Lamb, R.A.3
  • 36
    • 0029038155 scopus 로고
    • Understanding the mechanism of action of the anti-influenza virus drug amantadine
    • Pinto, L. H., and Lamb, R. A. (1995). Understanding the mechanism of action of the anti-influenza virus drug amantadine. Trends Microbiol. 3(7), 271.
    • (1995) Trends Microbiol. , vol.3 , Issue.7 , pp. 271
    • Pinto, L.H.1    Lamb, R.A.2
  • 37
    • 0003077804 scopus 로고
    • Membrane insertion and intracellular transport of influenza virus glycoproteins
    • R. M. Krug, Ed. Plenum Press, NY
    • Roth, M. G., Gething, M.-J., and Sambrook, J. (1989). Membrane insertion and intracellular transport of influenza virus glycoproteins. In "The Influenza Viruses" (R. M. Krug, Ed.) pp. 219-267, Plenum Press, NY.
    • (1989) The Influenza Viruses , pp. 219-267
    • Roth, M.G.1    Gething, M.-J.2    Sambrook, J.3
  • 38
    • 0028827789 scopus 로고
    • GG-167 (4-Guanidino-2,4-dideoxy-2,3-dehydro-N-aceylneuraminic acid) is a potent inhibitor of influenza virus in ferrets
    • Ryan, D. M., Ticehurst, J., and Dempsey, M. H. (1995). GG-167 (4-Guanidino-2,4-dideoxy-2,3-dehydro-N-aceylneuraminic acid) is a potent inhibitor of influenza virus in ferrets. Antimicrob. Agents Chemother. 39, 2583-2584.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 2583-2584
    • Ryan, D.M.1    Ticehurst, J.2    Dempsey, M.H.3
  • 39
    • 0027981472 scopus 로고
    • Inhibition of influenza virus replication in mice by GG-167 (4-Guanidino-2,4-dideoxy-2,3-dehydro-N-aceylneuraminic acid) is consistent with extracellular activity of viral neuraminidase (sialidase)
    • Ryan, D. M., Ticehurst, J., Dempsey, M. H., and Penn, C. R. (1994). Inhibition of influenza virus replication in mice by GG-167 (4-Guanidino-2,4-dideoxy-2,3-dehydro-N-aceylneuraminic 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
  • 40
  • 41
    • 0017107505 scopus 로고
    • Selection and identification of influenza virus recombinants of defined genetic composition
    • Schulman, J. L., and Palese, P. (1976). Selection and identification of influenza virus recombinants of defined genetic composition. J. Virol. 20, 248-254.
    • (1976) J. Virol. , vol.20 , pp. 248-254
    • Schulman, J.L.1    Palese, P.2
  • 43
    • 0002506954 scopus 로고
    • Influenza virus fusion: From models toward a mechanism
    • J. Bentz, Ed., CRC Press, Boca Raton, FL
    • Stegmann, T., and Helenius, A. (1993). Influenza virus fusion: from models toward a mechanism. In "Viral Fusion Mechanisms" (J. Bentz, Ed.), pp. 89-111. CRC Press, Boca Raton, FL.
    • (1993) Viral Fusion Mechanisms , pp. 89-111
    • Stegmann, T.1    Helenius, A.2
  • 45
    • 0028820162 scopus 로고
    • Influenza hemagglutinin assumes a tilted conformation during membrane fusion as determined by attenuated total reflection FTIR spectroscopy
    • Tatulian, S. A., Hinterdorfer, P., Baber, G., and Tamm, L. K. (1995). Influenza hemagglutinin assumes a tilted conformation during membrane fusion as determined by attenuated total reflection FTIR spectroscopy. EMBO J. 14, 5514-5523.
    • (1995) EMBO J. , vol.14 , pp. 5514-5523
    • Tatulian, S.A.1    Hinterdorfer, P.2    Baber, G.3    Tamm, L.K.4
  • 48
    • 0029665753 scopus 로고    scopus 로고
    • Characterization of inhibition of M2 ion channel activity by BL-1743, a novel inhibitor of influenza A virus
    • Tu, Q., Pinto, L. H., Luo, G., Shaughnessy, M. A., Mullaney, D., Kurtz, S., Krystal, M., and Lamb, R. A. (1996). Characterization of inhibition of M2 ion channel activity by BL-1743, a novel inhibitor of influenza A virus. J. Virol. 70, 4246-4252.
    • (1996) J. Virol. , vol.70 , pp. 4246-4252
    • Tu, Q.1    Pinto, L.H.2    Luo, G.3    Shaughnessy, M.A.4    Mullaney, D.5    Kurtz, S.6    Krystal, M.7    Lamb, R.A.8
  • 51
    • 0023915219 scopus 로고
    • Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid
    • Weis, W., Brown, J. H., Cusack, S., Paulson, J. C., Skehel, J., and Wiley, D. C. (1988). Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid. Nature 332, 426-431.
    • (1988) Nature , vol.332 , pp. 426-431
    • Weis, W.1    Brown, J.H.2    Cusack, S.3    Paulson, J.C.4    Skehel, J.5    Wiley, D.C.6
  • 52
    • 0025276435 scopus 로고
    • Viral and Cellular membrane fusion proteins
    • White, J. M. (1990). Viral and Cellular membrane fusion proteins. Annu. Rev. Physiol. 52, 675-697.
    • (1990) Annu. Rev. Physiol. , vol.52 , pp. 675-697
    • White, J.M.1
  • 53
    • 0026492542 scopus 로고
    • Membrane fusion
    • White, J. M. (1992). Membrane fusion. Science 258, 917-924.
    • (1992) Science , vol.258 , pp. 917-924
    • White, J.M.1
  • 54
    • 0023082135 scopus 로고
    • The structure and function of the hemagglutinin membrane glycoprotein of influenza virus
    • Wiley, D. C., and Skehel, J. J. (1987). The structure and function of the hemagglutinin membrane glycoprotein of influenza virus. Annu. Rev. Biochem. 56, 365-394.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 365-394
    • Wiley, D.C.1    Skehel, J.J.2
  • 55
    • 0019890491 scopus 로고
    • Structure of the hemagglutinin membrane glycoprotein of influenza virus at 3Å resolution
    • Wilson, I. A., Skehel, J. J., and Wiley, D. C. (1981). Structure of the hemagglutinin membrane glycoprotein of influenza virus at 3Å resolution. Nature 289, 366-373.
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 56
    • 0027162942 scopus 로고
    • 4-Guanidino-2,4-Dideoxy-2,3-Dehydro-N-Acetyl-neuraminic Acid is a highly effective inhibitor both of sialidase (neuraminidase) and of growth of a wide range of influenza A and B viruses in vitro
    • Woods, J. M., Bethell, R. C., Coates, J. A. V., Healy, N., Hiscox, S. A., Pearson, B. A., Ryan, D. M., Ticehurst, J., Tilling, J., Walcott, S. M., and Penn, C. R. (1993). 4-Guanidino-2,4-Dideoxy-2,3-Dehydro-N-Acetyl-neuraminic Acid is a highly effective inhibitor both of 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


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