메뉴 건너뛰기




Volumn 99, Issue 3, 2013, Pages 281-291

Role of the viral hemagglutinin in the anti-influenza virus activity of newly synthesized polycyclic amine compounds

Author keywords

Amantadine; Hemagglutinin; Influenza A virus; M2 protein; Polycyclic amines

Indexed keywords

AMANTADINE; AMINE; POLYCYCLIC AMINE DERIVATIVE; POLYCYCLIC HYDROCARBON; PROTON; PYRROLIDINE DERIVATIVE; RIMANTADINE DERIVATIVE; UNCLASSIFIED DRUG; VIRUS HEMAGGLUTININ; ANTIVIRUS AGENT; HEMAGGLUTININ; INFLUENZA VIRUS HEMAGGLUTININ; N METHYL DEXTRO ASPARTIC ACID; PROTEIN M2; 4 ACETAMIDO 5 AMINO 3 (1 ETHYLPROPOXY) 1 CYCLOHEXENE 1 CARBOXYLIC ACID; ADAMANTANE DERIVATIVE; AMIDINE; DODECANE; GUANIDINE DERIVATIVE; MEMANTINE; NITROGEN; RIBAVIRIN; RIMANTADINE; ZANAMIVIR;

EID: 84884576955     PISSN: 01663542     EISSN: 18729096     Source Type: Journal    
DOI: 10.1016/j.antiviral.2013.06.006     Document Type: Article
Times cited : (24)

References (56)
  • 3
    • 72449187005 scopus 로고    scopus 로고
    • Design and pharmacological characterization of inhibitors of amantadine-resistant mutants of the M2 ion channel of influenza A virus
    • Balannik V., Wang J., Ohigashi Y., Jing X., Magavern E., Lamb R.A., DeGrado W.F., Pinto L.H. Design and pharmacological characterization of inhibitors of amantadine-resistant mutants of the M2 ion channel of influenza A virus. Biochemistry 2009, 48:11872-11882.
    • (2009) Biochemistry , vol.48 , pp. 11872-11882
    • Balannik, V.1    Wang, J.2    Ohigashi, Y.3    Jing, X.4    Magavern, E.5    Lamb, R.A.6    DeGrado, W.F.7    Pinto, L.H.8
  • 5
    • 25844438380 scopus 로고    scopus 로고
    • Incidence of adamantane resistance among influenza A (H3N2) viruses isolated worldwide from 1994 to 2005: a cause for concern
    • Bright R.A., Medina M.J., Xu X., Pérez-Oronoz G., Wallis T.R., Davis X.M., Povinelli L., Cox N.J., Klimov A.I. Incidence of adamantane resistance among influenza A (H3N2) viruses isolated worldwide from 1994 to 2005: a cause for concern. Lancet 2005, 366:1175-1181.
    • (2005) Lancet , vol.366 , pp. 1175-1181
    • Bright, R.A.1    Medina, M.J.2    Xu, X.3    Pérez-Oronoz, G.4    Wallis, T.R.5    Davis, X.M.6    Povinelli, L.7    Cox, N.J.8    Klimov, A.I.9
  • 6
    • 33644536465 scopus 로고    scopus 로고
    • Adamantane resistance among influenza A viruses isolated early during the 2005-2006 influenza season in the United States
    • Bright R.A., Shay D.K., Shu B., Cox N.J., Klimov A.I. Adamantane resistance among influenza A viruses isolated early during the 2005-2006 influenza season in the United States. Jama 2006, 295:891-894.
    • (2006) Jama , vol.295 , pp. 891-894
    • Bright, R.A.1    Shay, D.K.2    Shu, B.3    Cox, N.J.4    Klimov, A.I.5
  • 7
    • 68249121326 scopus 로고    scopus 로고
    • Structure and function of the influenza A M2 proton channel
    • Cady S.D., Luo W., Hu F., Hong M. Structure and function of the influenza A M2 proton channel. Biochemistry 2009, 48:7356-7364.
    • (2009) Biochemistry , vol.48 , pp. 7356-7364
    • Cady, S.D.1    Luo, W.2    Hu, F.3    Hong, M.4
  • 8
    • 76249125649 scopus 로고    scopus 로고
    • Structure of the amantadine binding site of influenza M2 proton channels in lipid bilayers
    • Cady S.D., Schmidt-Rohr K., Wang J., Soto C.S., DeGrado W.F., Hong M. Structure of the amantadine binding site of influenza M2 proton channels in lipid bilayers. Nature 2010, 463:689-692.
    • (2010) Nature , vol.463 , pp. 689-692
    • Cady, S.D.1    Schmidt-Rohr, K.2    Wang, J.3    Soto, C.S.4    DeGrado, W.F.5    Hong, M.6
  • 9
    • 79953041331 scopus 로고    scopus 로고
    • Specific binding of adamantane drugs and direction of their polar amines in the pore of the influenza M2 transmembrane domain in lipid bilayers and dodecylphosphocholine micelles determined by NMR spectroscopy
    • Cady S.D., Wang J., Wu Y., DeGrado W.F., Hong M. Specific binding of adamantane drugs and direction of their polar amines in the pore of the influenza M2 transmembrane domain in lipid bilayers and dodecylphosphocholine micelles determined by NMR spectroscopy. J. Am. Chem. Soc. 2011, 133:4274-4284.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 4274-4284
    • Cady, S.D.1    Wang, J.2    Wu, Y.3    DeGrado, W.F.4    Hong, M.5
  • 13
    • 0035881708 scopus 로고    scopus 로고
    • Studies on influenza haemagglutinin fusion peptide mutants generated by reverse genetics
    • Cross K.J., Wharton S.A., Skehel J.J., Wiley D.C., Steinhauer D.A. Studies on influenza haemagglutinin fusion peptide mutants generated by reverse genetics. EMBO J. 2001, 20:4432-4442.
    • (2001) EMBO J. , vol.20 , pp. 4432-4442
    • Cross, K.J.1    Wharton, S.A.2    Skehel, J.J.3    Wiley, D.C.4    Steinhauer, D.A.5
  • 16
    • 79952217106 scopus 로고    scopus 로고
    • Antiviral agents for the treatment and chemoprophylaxis of influenza - recommendations of the Advisory Committee on Immunization Practices (ACIP)
    • Fiore A.E., Fry A., Shay D., Gubareva L., Bresee J.S., Uyeki T.M. Antiviral agents for the treatment and chemoprophylaxis of influenza - recommendations of the Advisory Committee on Immunization Practices (ACIP). MMWR Recomm. Rep. 2011, 60:1-24.
    • (2011) MMWR Recomm. Rep. , vol.60 , pp. 1-24
    • Fiore, A.E.1    Fry, A.2    Shay, D.3    Gubareva, L.4    Bresee, J.S.5    Uyeki, T.M.6
  • 18
    • 0022157043 scopus 로고
    • The molecular basis of the specific anti-influenza action of amantadine
    • Hay A.J., Wolstenholme A.J., Skehel J.J., Smith M.H. The molecular basis of the specific anti-influenza action of amantadine. EMBO J. 1985, 4:3021-3024.
    • (1985) EMBO J. , vol.4 , pp. 3021-3024
    • Hay, A.J.1    Wolstenholme, A.J.2    Skehel, J.J.3    Smith, M.H.4
  • 19
    • 0021878483 scopus 로고
    • Comparative single-dose pharmacokinetics of amantadine hydrochloride and rimantadine hydrochloride in young and elderly adults
    • Hayden F.G., Minocha A., Spyker D.A., Hoffman H.E. Comparative single-dose pharmacokinetics of amantadine hydrochloride and rimantadine hydrochloride in young and elderly adults. Antimicrob. Agents Chemother. 1985, 28:216-221.
    • (1985) Antimicrob. Agents Chemother. , vol.28 , pp. 216-221
    • Hayden, F.G.1    Minocha, A.2    Spyker, D.A.3    Hoffman, H.E.4
  • 20
    • 0035559445 scopus 로고    scopus 로고
    • Universal primer set for the full-length amplification of all influenza A viruses
    • Hoffmann E., Stech J., Guan Y., Webster R.G., Pérez D.R. Universal primer set for the full-length amplification of all influenza A viruses. Arch Virol. 2001, 146:2275-2289.
    • (2001) Arch Virol. , vol.146 , pp. 2275-2289
    • Hoffmann, E.1    Stech, J.2    Guan, Y.3    Webster, R.G.4    Pérez, D.R.5
  • 21
    • 84867681380 scopus 로고    scopus 로고
    • Structural basis for proton conduction and inhibition by the influenza M2 protein
    • Hong M., DeGrado W.F. Structural basis for proton conduction and inhibition by the influenza M2 protein. Protein Sci. 2012, 21:1620-1633.
    • (2012) Protein Sci. , vol.21 , pp. 1620-1633
    • Hong, M.1    DeGrado, W.F.2
  • 22
    • 77958162674 scopus 로고    scopus 로고
    • Mechanisms of proton conduction and gating in influenza M2 proton channels from solid-state NMR
    • Hu F., Luo W., Hong M. Mechanisms of proton conduction and gating in influenza M2 proton channels from solid-state NMR. Science 2010, 330:505-508.
    • (2010) Science , vol.330 , pp. 505-508
    • Hu, F.1    Luo, W.2    Hong, M.3
  • 23
    • 84860746711 scopus 로고    scopus 로고
    • Amantadine: the journey from fighting flu to treating Parkinson disease
    • Hubsher G., Haider M., Okun M.S. Amantadine: the journey from fighting flu to treating Parkinson disease. Neurology 2012, 78:1096-1099.
    • (2012) Neurology , vol.78 , pp. 1096-1099
    • Hubsher, G.1    Haider, M.2    Okun, M.S.3
  • 25
    • 0033060915 scopus 로고    scopus 로고
    • Conformational intermediates and fusion activity of influenza virus hemagglutinin
    • Korte T., Ludwig K., Booy F.P., Blumenthal R., Herrmann A. Conformational intermediates and fusion activity of influenza virus hemagglutinin. J Virol. 1999, 73:4567-4574.
    • (1999) J Virol. , vol.73 , pp. 4567-4574
    • Korte, T.1    Ludwig, K.2    Booy, F.P.3    Blumenthal, R.4    Herrmann, A.5
  • 26
    • 77955615630 scopus 로고    scopus 로고
    • Use of the adamantane structure in medicinal chemistry
    • Lamoureux G., Artavia G. Use of the adamantane structure in medicinal chemistry. Curr. Med. Chem. 2010, 17:2967-2978.
    • (2010) Curr. Med. Chem. , vol.17 , pp. 2967-2978
    • Lamoureux, G.1    Artavia, G.2
  • 27
    • 0007600773 scopus 로고    scopus 로고
    • Adaptation of egg-grown and transfectant influenza viruses for growth in mammalian cells: selection of hemagglutinin mutants with elevated pH of membrane fusion
    • Lin Y.P., Wharton S.A., Martín J., Skehel J.J., Wiley D.C., Steinhauer D.A. Adaptation of egg-grown and transfectant influenza viruses for growth in mammalian cells: selection of hemagglutinin mutants with elevated pH of membrane fusion. Virology 1997, 233:402-410.
    • (1997) Virology , vol.233 , pp. 402-410
    • Lin, Y.P.1    Wharton, S.A.2    Martín, J.3    Skehel, J.J.4    Wiley, D.C.5    Steinhauer, D.A.6
  • 28
    • 33645095476 scopus 로고    scopus 로고
    • Paradigm shift in neuroprotection by NMDA receptor blockade: memantine and beyond
    • Lipton S.A. Paradigm shift in neuroprotection by NMDA receptor blockade: memantine and beyond. Nat. Rev. Drug Discov. 2006, 5:160-170.
    • (2006) Nat. Rev. Drug Discov. , vol.5 , pp. 160-170
    • Lipton, S.A.1
  • 29
    • 79955637311 scopus 로고    scopus 로고
    • The many faces of the adamantyl group in drug design
    • Liu J., Obando D., Liao V., Lifa T., Codd R. The many faces of the adamantyl group in drug design. Eur. J. Med. Chem. 2011, 46:1949-1963.
    • (2011) Eur. J. Med. Chem. , vol.46 , pp. 1949-1963
    • Liu, J.1    Obando, D.2    Liao, V.3    Lifa, T.4    Codd, R.5
  • 35
    • 33646932780 scopus 로고    scopus 로고
    • The M2 proton channels of influenza A and B viruses
    • Pinto L.H., Lamb R.A. The M2 proton channels of influenza A and B viruses. J. Biol. Chem. 2006, 281:8997-9000.
    • (2006) J. Biol. Chem. , vol.281 , pp. 8997-9000
    • Pinto, L.H.1    Lamb, R.A.2
  • 38
    • 33745158157 scopus 로고
    • A simple method of estimating fifty percent endpoints
    • Reed L.J., Muench H. A simple method of estimating fifty percent endpoints. Am. J. Epidemiol. 1938, 27:493-497.
    • (1938) Am. J. Epidemiol. , vol.27 , pp. 493-497
    • Reed, L.J.1    Muench, H.2
  • 39
    • 77956383657 scopus 로고    scopus 로고
    • Coexistence of two adamantane binding sites in the influenza A M2 ion channel
    • Rosenberg M.R., Casarotto M.G. Coexistence of two adamantane binding sites in the influenza A M2 ion channel. Proc. Natl. Acad. Sci. USA 2010, 107:13866-13871.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 13866-13871
    • Rosenberg, M.R.1    Casarotto, M.G.2
  • 40
    • 79952069060 scopus 로고    scopus 로고
    • Influenza virus assembly and budding
    • Rossman J.S., Lamb R.A. Influenza virus assembly and budding. Virology 2011, 411:229-236.
    • (2011) Virology , vol.411 , pp. 229-236
    • Rossman, J.S.1    Lamb, R.A.2
  • 41
    • 0032005664 scopus 로고    scopus 로고
    • How to overcome resistance of influenza A viruses against adamantane derivatives
    • Scholtissek C., Quack G., Klenk H.D., Webster R.G. How to overcome resistance of influenza A viruses against adamantane derivatives. Antiviral Res. 1998, 37:83-95.
    • (1998) Antiviral Res. , vol.37 , pp. 83-95
    • Scholtissek, C.1    Quack, G.2    Klenk, H.D.3    Webster, R.G.4
  • 42
    • 77958156306 scopus 로고    scopus 로고
    • Insight into the mechanisms of the influenza A proton channel from a structure in a lipid bilayer
    • Sharma M., Yi M., Dong H., Qin H., Peterson E., Busath D.D., Zhou H.-X., Cross T.A. Insight into the mechanisms of the influenza A proton channel from a structure in a lipid bilayer. Science 2010, 330:509-512.
    • (2010) Science , vol.330 , pp. 509-512
    • Sharma, M.1    Yi, M.2    Dong, H.3    Qin, H.4    Peterson, E.5    Busath, D.D.6    Zhou, H.-X.7    Cross, T.A.8
  • 43
    • 33746724834 scopus 로고    scopus 로고
    • Prevention and control of influenza - recommendations of the Advisory Committee on Immunization Practices (ACIP)
    • Smith N.M., Bresee J.S., Shay D., Uyeki T.M., Cox N.J., Strikas R.A. Prevention and control of influenza - recommendations of the Advisory Committee on Immunization Practices (ACIP). MMWR Recomm. Rep. 2006, 55:1-42.
    • (2006) MMWR Recomm. Rep. , vol.55 , pp. 1-42
    • Smith, N.M.1    Bresee, J.S.2    Shay, D.3    Uyeki, T.M.4    Cox, N.J.5    Strikas, R.A.6
  • 44
    • 1642352884 scopus 로고    scopus 로고
    • Structure of the uncleaved human H1 hemagglutinin from the extinct 1918 influenza virus
    • Stevens J., Corper A.L., Basler C.F., Taubenberger J.K., Palese P., Wilson I.A. Structure of the uncleaved human H1 hemagglutinin from the extinct 1918 influenza virus. Science 2004, 303:1866-1870.
    • (2004) Science , vol.303 , pp. 1866-1870
    • Stevens, J.1    Corper, A.L.2    Basler, C.F.3    Taubenberger, J.K.4    Palese, P.5    Wilson, I.A.6
  • 45
  • 47
    • 36749003222 scopus 로고    scopus 로고
    • Analysis of residues near the fusion peptide in the influenza hemagglutinin structure for roles in triggering membrane fusion
    • Thoennes S., Li Z.N., Lee B.J., Langley W.A., Skehel J.J., Russell R.J., Steinhauer D.A. Analysis of residues near the fusion peptide in the influenza hemagglutinin structure for roles in triggering membrane fusion. Virology 2008, 370:403-414.
    • (2008) Virology , vol.370 , pp. 403-414
    • Thoennes, S.1    Li, Z.N.2    Lee, B.J.3    Langley, W.A.4    Skehel, J.J.5    Russell, R.J.6    Steinhauer, D.A.7
  • 49
    • 77950840696 scopus 로고    scopus 로고
    • Novel inhibitors of influenza virus fusion: structure-activity relationship and interaction with the viral hemagglutinin
    • Vanderlinden E., Göktas F., Cesur Z., Froeyen M., Reed M.L., Russell C.J., Cesur N., Naesens L. Novel inhibitors of influenza virus fusion: structure-activity relationship and interaction with the viral hemagglutinin. J. Virol. 2010, 84:4277-4288.
    • (2010) J. Virol. , vol.84 , pp. 4277-4288
    • Vanderlinden, E.1    Göktas, F.2    Cesur, Z.3    Froeyen, M.4    Reed, M.L.5    Russell, C.J.6    Cesur, N.7    Naesens, L.8
  • 51
    • 0037777695 scopus 로고    scopus 로고
    • 1-[[(3-Hydroxy-1-adamantyl)amino]acetyl]-2-cyano-(S)-pyrrolidine: a potent, selective, and orally bioavailable dipeptidyl peptidase IV inhibitor with antihyperglycemic properties
    • Villhauer E.B., Brinkman J.A., Naderi G.B., Burkey B.F., Dunning B.E., Prasad K., Mangold B.L., Russell M.E., Hughes T.E. 1-[[(3-Hydroxy-1-adamantyl)amino]acetyl]-2-cyano-(S)-pyrrolidine: a potent, selective, and orally bioavailable dipeptidyl peptidase IV inhibitor with antihyperglycemic properties. J. Med. Chem. 2003, 46:2774-2789.
    • (2003) J. Med. Chem. , vol.46 , pp. 2774-2789
    • Villhauer, E.B.1    Brinkman, J.A.2    Naderi, G.B.3    Burkey, B.F.4    Dunning, B.E.5    Prasad, K.6    Mangold, B.L.7    Russell, M.E.8    Hughes, T.E.9
  • 53
    • 79551687044 scopus 로고    scopus 로고
    • Structural and dynamic mechanisms for the function and inhibition of the M2 proton channel from influenza A virus
    • Wang J., Qui J.X., Soto C., DeGrado W.F. Structural and dynamic mechanisms for the function and inhibition of the M2 proton channel from influenza A virus. Curr. Opin. Struct. Biol. 2011, 21:68-80.
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 68-80
    • Wang, J.1    Qui, J.X.2    Soto, C.3    DeGrado, W.F.4
  • 55
    • 77956574180 scopus 로고    scopus 로고
    • Heterodimers of histidine and amantadine as inhibitors for wild type and mutant M2 channels of influenza A
    • Zhang W., Xu J., Liu F., Li C., Jie Y., Chen S., Li Z., Liu J., Chen L., Zhou G. Heterodimers of histidine and amantadine as inhibitors for wild type and mutant M2 channels of influenza A. Chin. J. Chem. 2010, 28:1417-1423.
    • (2010) Chin. J. Chem. , vol.28 , pp. 1417-1423
    • Zhang, W.1    Xu, J.2    Liu, F.3    Li, C.4    Jie, Y.5    Chen, S.6    Li, Z.7    Liu, J.8    Chen, L.9    Zhou, G.10
  • 56
    • 77957816428 scopus 로고    scopus 로고
    • Crystal structure of the swine-origin A (H1N1)-2009 influenza A virus hemagglutinin (HA) reveals similar antigenicity to that of the 1918 pandemic virus
    • Zhang W., Qi J., Shi Y., Li Q., Gao F., Sun Y., Lu X., Lu Q., Vavricka C.J., Liu D., Yan J., Gao G.F. Crystal structure of the swine-origin A (H1N1)-2009 influenza A virus hemagglutinin (HA) reveals similar antigenicity to that of the 1918 pandemic virus. Protein Cell 2010, 1:459-467.
    • (2010) Protein Cell , vol.1 , pp. 459-467
    • Zhang, W.1    Qi, J.2    Shi, Y.3    Li, Q.4    Gao, F.5    Sun, Y.6    Lu, X.7    Lu, Q.8    Vavricka, C.J.9    Liu, D.10    Yan, J.11    Gao, G.F.12


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.