메뉴 건너뛰기




Volumn 13, Issue 3, 2012, Pages 205-210

Recent progress in computational approaches to studying the M2 proton channel and its implication to drug design against influenza viruses

Author keywords

Allosteric inhibition mechanism; Amantadine; Influenza a virus; M2 proton channel; PKa shift; Rational drug design; Rimantadine

Indexed keywords

AMANTADINE; ANTIINFLUENZA VIRUS AGENT; ANTIVIRUS AGENT; PROTEIN M2; RIMANTADINE; UNCLASSIFIED DRUG;

EID: 84862585703     PISSN: 13892037     EISSN: 18755550     Source Type: Journal    
DOI: 10.2174/138920312800785030     Document Type: Review
Times cited : (9)

References (48)
  • 1
    • 78650263902 scopus 로고    scopus 로고
    • Influenza M2 proton channels Biochim
    • Pielak, R.M.; Chou, J.J. Influenza M2 proton channels Biochim. Biophys. Acta, 2011, 1808, 522-529.
    • (2011) Biophys. Acta , vol.1808 , pp. 522-529
    • Pielak, R.M.1    Chou, J.J.2
  • 3
    • 0036651804 scopus 로고    scopus 로고
    • New millennium antivirals against pandemic and epidemic influenza: The neuraminidase inhibitors
    • Oxford, J.S.; Novelli, P.; Sefton, A.; Lambkin, R. New millennium antivirals against pandemic and epidemic influenza: the neuraminidase inhibitors. Antivir. Chem. Chemother., 2002, 13, 205-217.
    • (2002) Antivir. Chem. Chemother , vol.13 , pp. 205-217
    • Oxford, J.S.1    Novelli, P.2    Sefton, A.3    Lambkin, R.4
  • 5
    • 0033897803 scopus 로고    scopus 로고
    • Resistance of influenza viruses to neuraminidase inhibitors--a review
    • McKimm-Breschkin, J.L. Resistance of influenza viruses to neuraminidase inhibitors--a review. Antiviral Res., 2000, 47, 1-17.
    • (2000) Antiviral Res , vol.47 , pp. 1-17
    • McKimm-Breschkin, J.L.1
  • 6
    • 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.; Air, G.M. Influenza type A virus neuraminidase does not play a role in viral entry, replication, assembly, or budding. J. Virol., 1995, 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
  • 7
    • 0034084227 scopus 로고    scopus 로고
    • Discovery and development of GS 4104 (oseltamivir): An orally active influenza neuraminidase inhibitor
    • Lew, W.; Chen, X.; Kim, C.U. Discovery and development of GS 4104 (oseltamivir): an orally active influenza neuraminidase inhibitor. Curr. Med. Chem., 2000, 7, 663-672.
    • (2000) Curr. Med. Chem , vol.7 , pp. 663-672
    • Lew, W.1    Chen, X.2    Kim, C.U.3
  • 8
    • 0032710055 scopus 로고    scopus 로고
    • Zanamivir: A review of its use in influenza
    • Dunn, C.J.; Goa, K.L. Zanamivir: a review of its use in influenza. Drugs, 1999, 58, 761-784.
    • (1999) Drugs , vol.58 , pp. 761-784
    • Dunn, C.J.1    Goa, K.L.2
  • 9
    • 33846617350 scopus 로고    scopus 로고
    • Study of drug resistance of chicken influenza A virus (H5N1) from homology-modeled 3D structures of neuraminidases
    • Wang, S.Q.; Du, Q.S. and Chou, K.C. Study of drug resistance of chicken influenza A virus (H5N1) from homology-modeled 3D structures of neuraminidases. Biochem. Biophys. Res. Comm., 2007, 354, 634-640.
    • (2007) Biochem. Biophys. Res. Comm , vol.354 , pp. 634-640
    • Wang, S.Q.1    Du, Q.S.2    Chou, K.C.3
  • 10
    • 77954982338 scopus 로고    scopus 로고
    • Flu channel drug resistance: A tale of two sites
    • Pielak, R.M.; Chou, J.J. Flu channel drug resistance: a tale of two sites. Protein & Cell, 2010, 1, 246-258.
    • (2010) Protein & Cell , vol.1 , pp. 246-258
    • Pielak, R.M.1    Chou, J.J.2
  • 12
    • 0035921095 scopus 로고    scopus 로고
    • Novel 3-(2-adamantyl)pyrrolidines with potent activity against influenza A virus-identification of aminoadamantane derivatives bearing two pharmacophoric amine groups
    • Stamatiou, G.; Kolocouris, A.; Kolocouris, N.; Fytas, G.; Foscolos, G.B.; Neyts, J.; De Clercq, E. Novel 3-(2-adamantyl)pyrrolidines with potent activity against influenza A virus-identification of aminoadamantane derivatives bearing two pharmacophoric amine groups. Bioorg. Med. Chem. Lett., 2001, 11, 2137-2142.
    • (2001) Bioorg. Med. Chem. Lett , vol.11 , pp. 2137-2142
    • Stamatiou, G.1    Kolocouris, A.2    Kolocouris, N.3    Fytas, G.4    Foscolos, G.B.5    Neyts, J.6    de Clercq, E.7
  • 13
    • 0025923280 scopus 로고
    • Influenza virus M2 integral membrane protein is a homotetramer stabilized by formation of disulfide bonds
    • Holsinger, L.J.; Lamb, R.A. Influenza virus M2 integral membrane protein is a homotetramer stabilized by formation of disulfide bonds. Virology, 1991, 183, 32-43.
    • (1991) Virology , vol.183 , pp. 32-43
    • Holsinger, L.J.1    Lamb, R.A.2
  • 14
    • 0026008031 scopus 로고
    • Structural characteristics of the M2 protein of influenza A viruses: Evidence that it forms a tetrameric channel
    • Sugrue, R.J.; Hay, A.J. Structural characteristics of the M2 protein of influenza A viruses: evidence that it forms a tetrameric channel. Virology, 1991, 180, 617-624.
    • (1991) Virology , vol.180 , pp. 617-624
    • Sugrue, R.J.1    Hay, A.J.2
  • 15
    • 0037293081 scopus 로고    scopus 로고
    • Influenza B virus BM2 protein is an oligomeric integral membrane protein expressed at the cell surface
    • Paterson, R.G.; Takeda, M.; Ohigashi, Y.; Pinto, L.H.; Lamb, R.A. Influenza B virus BM2 protein is an oligomeric integral membrane protein expressed at the cell surface. Virology, 2003, 306, 7-17.
    • (2003) Virology , vol.306 , pp. 7-17
    • Paterson, R.G.1    Takeda, M.2    Ohigashi, Y.3    Pinto, L.H.4    Lamb, R.A.5
  • 16
    • 0026612385 scopus 로고
    • Influenza virus M2 protein has ion channel activity
    • Pinto, L.H.; Holsinger, J.J.; Lamb, R. A. Influenza virus M2 protein has ion channel activity. Cell, 1992, 69, 517-528.
    • (1992) Cell , vol.69 , pp. 517-528
    • Pinto, L.H.1    Holsinger, J.J.2    Lamb, R.A.3
  • 18
    • 33646160618 scopus 로고    scopus 로고
    • Insights from modeling the 3D structure of H5N1 influenza virus neuraminidase and its binding interactions with ligands
    • Wei, D.Q.; Du, Q.S.; Sun, H.; Chou, K.C. Insights from modeling the 3D structure of H5N1 influenza virus neuraminidase and its binding interactions with ligands. Biochem. Biophys. Res. Comm., 2006, 344, 1048-1055.
    • (2006) Biochem. Biophys. Res. Comm , vol.344 , pp. 1048-1055
    • Wei, D.Q.1    Du, Q.S.2    Sun, H.3    Chou, K.C.4
  • 19
    • 34548261773 scopus 로고    scopus 로고
    • Analogue inhibitors by modifying oseltamivir based on the crystal neuraminidase structure for treating drug-resistant H5N1 virus
    • Du, Q.S.; Wang, S.Q.; Chou, K.C. Analogue inhibitors by modifying oseltamivir based on the crystal neuraminidase structure for treating drug-resistant H5N1 virus. Biochem. Biophys. Res. Comm., 2007, 362, 525-531.
    • (2007) Biochem. Biophys. Res. Comm , vol.362 , pp. 525-531
    • Du, Q.S.1    Wang, S.Q.2    Chou, K.C.3
  • 20
    • 38749106195 scopus 로고    scopus 로고
    • Structure and mechanism of the M2 proton channel of influenza A virus
    • Schnell, J.R.; Chou, J.J. Structure and mechanism of the M2 proton channel of influenza A virus. Nature, 2008, 451, 591-595.
    • (2008) Nature , vol.451 , pp. 591-595
    • Schnell, J.R.1    Chou, J.J.2
  • 21
    • 71449091133 scopus 로고    scopus 로고
    • Solution structure and functional analysis of the influenza B proton channel
    • Wang, J.; Pielak, R.M.; McClintock, M.A.; Chou, J. J. Solution structure and functional analysis of the influenza B proton channel. Nat. Struct. Mol. Biol., 2009, 16, 1267-1271.
    • (2009) Nat. Struct. Mol. Biol , vol.16 , pp. 1267-1271
    • Wang, J.1    Pielak, R.M.2    McClintock, M.A.3    Chou, J.J.4
  • 22
    • 39749108008 scopus 로고    scopus 로고
    • Flu virus proton channel analyzed: Structures of key surface protein suggest different drug mechanisms
    • Borman, S. Flu virus proton channel analyzed: Structures of key surface protein suggest different drug mechanisms. Chem. Eng. News, 2008, 86, 53-54.
    • (2008) Chem. Eng. News , vol.86 , pp. 53-54
    • Borman, S.1
  • 24
    • 0025150631 scopus 로고
    • Energetic approach to the folding of four a-helices connected sequentially
    • Carlacci, L.; Chou, K.C. Energetic approach to the folding of four a-helices connected sequentially. Protein Eng., 1990, 3, 509-514.
    • (1990) Protein Eng , vol.3 , pp. 509-514
    • Carlacci, L.1    Chou, K.C.2
  • 25
    • 0026667399 scopus 로고
    • The role of loophelix interactions in stabilizing four-helix bundle proteins
    • Chou, K.C.; Maggiora, G.M.; Scheraga, H.A. The role of loophelix interactions in stabilizing four-helix bundle proteins. Proc. Nat. Acad. Sci. USA, 1992, 89, 7315-7319.
    • (1992) Proc. Nat. Acad. Sci. USA , vol.89 , pp. 7315-7319
    • Chou, K.C.1    Maggiora, G.M.2    Scheraga, H.A.3
  • 26
    • 0026714974 scopus 로고
    • Strong electrostatic loop-helix interactions in bundle motif protein structures
    • Chou, K.C.; Zheng, C. Strong electrostatic loop-helix interactions in bundle motif protein structures. Biophys. J., 1992, 63, 682-688.
    • (1992) Biophys. J , vol.63 , pp. 682-688
    • Chou, K.C.1    Zheng, C.2
  • 27
    • 0028879305 scopus 로고
    • What is the origin of the strong electrostatic loop-helix interactions in bundle motif protein structures?
    • Thompson, T.B.; Chou, K.C.; Zheng, C. What is the origin of the strong electrostatic loop-helix interactions in bundle motif protein structures? J. Protein Chem., 1995, 14, 559-566.
    • (1995) J. Protein Chem , vol.14 , pp. 559-566
    • Thompson, T.B.1    Chou, K.C.2    Zheng, C.3
  • 28
    • 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. J. Am. Med. Assoc., 2006, 295, 891-894.
    • (2006) J. Am. Med. Assoc , vol.295 , pp. 891-894
    • Bright, R.A.1    Shay, D.K.2    Shu, B.3    Cox, N.J.4    Klimov, A.I.5
  • 31
    • 0042335655 scopus 로고    scopus 로고
    • Roles of the histidine and tryptophan side chains in the M2 proton channel from influenza A virus
    • Takeuchi, H.; Okada, A.; Miura, T. Roles of the histidine and tryptophan side chains in the M2 proton channel from influenza A virus. FEBS Lett., 2003, 552, 35-38.
    • (2003) FEBS Lett , vol.552 , pp. 35-38
    • Takeuchi, H.1    Okada, A.2    Miura, T.3
  • 32
    • 0035918599 scopus 로고    scopus 로고
    • Protonation of histidine and histidine-tryptophan interaction in the activation of the M2 ion channel from influenza a virus
    • Okada, A.; Miura, T.; Takeuchi, H. Protonation of histidine and histidine-tryptophan interaction in the activation of the M2 ion channel from influenza a virus. Biochemistry, 2001, 40, 6053-6060.
    • (2001) Biochemistry , vol.40 , pp. 6053-6060
    • Okada, A.1    Miura, T.2    Takeuchi, H.3
  • 33
    • 56349166106 scopus 로고    scopus 로고
    • An in-depth analysis of the biological functional studies based on the NMR M2 channel structure of influenza A virus
    • Huang, R.B.; Du, Q.S.; Wang, C.H.; Chou, K.C. An in-depth analysis of the biological functional studies based on the NMR M2 channel structure of influenza A virus. Biochem. Biophys. Res. Comm., 2008, 377, 1243-1247.
    • (2008) Biochem. Biophys. Res. Comm , vol.377 , pp. 1243-1247
    • Huang, R.B.1    Du, Q.S.2    Wang, C.H.3    Chou, K.C.4
  • 34
    • 67349139888 scopus 로고    scopus 로고
    • Energetic analysis of the two controversial drug binding sites of the M2 proton channel in influenza A virus
    • Du, Q.S.; Huang, R.B.; Wang, C.H.; Li, X.M.; Chou, K.C. Energetic analysis of the two controversial drug binding sites of the M2 proton channel in influenza A virus. J. Theor. Biol., 2009, 259, 159-164.
    • (2009) J. Theor. Biol , vol.259 , pp. 159-164
    • Du, Q.S.1    Huang, R.B.2    Wang, C.H.3    Li, X.M.4    Chou, K.C.5
  • 35
    • 2942677105 scopus 로고    scopus 로고
    • The determinants of carboxyl pKa values in turkey ovomucoid third domain
    • Li, H.; Robertson, A.D.; Jensen, J.H. The determinants of carboxyl pKa values in turkey ovomucoid third domain. Proteins, 2004, 55, 689-704.
    • (2004) Proteins , vol.55 , pp. 689-704
    • Li, H.1    Robertson, A.D.2    Jensen, J.H.3
  • 36
    • 28644432877 scopus 로고    scopus 로고
    • Very fast empirical prediction and rationalization of protein pKa values
    • Li, H.; Robertson, A.D.; Jensen, J.H. Very fast empirical prediction and rationalization of protein pKa values. Proteins, 2005, 61, 704-721.
    • (2005) Proteins , vol.61 , pp. 704-721
    • Li, H.1    Robertson, A.D.2    Jensen, J.H.3
  • 37
    • 73849104238 scopus 로고    scopus 로고
    • A fast and accurate method for predicting pKa of residues in proteins
    • Huang, R.B.; Du, Q.S.; Wang, C.H.; Liao, S.M.; Chou, K.C. A fast and accurate method for predicting pKa of residues in proteins. Protein Eng. Des. Sel., 2010, 23, 35-42.
    • (2010) Protein Eng. Des. Sel , vol.23 , pp. 35-42
    • Huang, R.B.1    Du, Q.S.2    Wang, C.H.3    Liao, S.M.4    Chou, K.C.5
  • 38
    • 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
  • 39
    • 0028181687 scopus 로고
    • Influenza A virus M2 ion channel protein: A structure-function analysis
    • Holsinger, L.J.; Nichani, D.; Pinto, L.H.; Lamb, R.A. Influenza A virus M2 ion channel protein: a structure-function analysis J. Virol., 1994, 68, 1551-1563.
    • (1994) J. Virol , vol.68 , pp. 1551-1563
    • Holsinger, L.J.1    Nichani, D.2    Pinto, L.H.3    Lamb, R.A.4
  • 40
    • 77954964960 scopus 로고    scopus 로고
    • Insights from studying the mutationinduced allostery in the M2 proton channel by molecular dynamics
    • Wang, J.F.; Chou, K.C. Insights from studying the mutationinduced allostery in the M2 proton channel by molecular dynamics. Protein Eng. Des. Sel., 2010, 23, 663-666.
    • (2010) Protein Eng. Des. Sel , vol.23 , pp. 663-666
    • Wang, J.F.1    Chou, K.C.2
  • 41
    • 67650073942 scopus 로고    scopus 로고
    • Investigation into adamantane-based M2 inhibitors with FB-QSAR
    • Wei, H.; Wang, C.H.; Du, Q.S.; Meng, J.; Chou, K.C. Investigation into adamantane-based M2 inhibitors with FB-QSAR. Med. Chem., 2009, 5, 305-317.
    • (2009) Med. Chem , vol.5 , pp. 305-317
    • Wei, H.1    Wang, C.H.2    Du, Q.S.3    Meng, J.4    Chou, K.C.5
  • 43
    • 77949597169 scopus 로고    scopus 로고
    • Designing inhibitors of M2 proton channel against H1N1 swine influenza virus
    • Du, Q.S.; Huang, R.B.; Wang, S.Q.; Chou, K.C. Designing inhibitors of M2 proton channel against H1N1 swine influenza virus PLoS ONE, 2010, 5, e9388.
    • (2010) PLoS ONE , vol.5
    • Du, Q.S.1    Huang, R.B.2    Wang, S.Q.3    Chou, K.C.4
  • 44
    • 0034680475 scopus 로고    scopus 로고
    • Preparation of (R)-(1-adamantyl)glycine and (R)-2-(1-adamantyl)-2- aminoethanol: A combination of cobalt-mediated b-ketoester alkylation and enzyme-based aminoalcohol resolution
    • Clariana, J.; Garcia-Granda, S.; Gotor, V.; Gutierrez-Fernandez, A.; Luna, A.; Moreno-Mañas, M.; Vallribera, A. Preparation of (R)-(1-adamantyl)glycine and (R)-2-(1-adamantyl)-2- aminoethanol: a combination of cobalt-mediated b-ketoester alkylation and enzyme-based aminoalcohol resolution. Tetrahedron: Asymmetry, 2000, 11, 4549-4557.
    • (2000) Tetrahedron: Asymmetry , vol.11 , pp. 4549-4557
    • Clariana, J.1    Garcia-Granda, S.2    Gotor, V.3    Gutierrez-Fernandez, A.4    Luna, A.5    Moreno-Mañas, M.6    Vallribera, A.7
  • 45
    • 69249222514 scopus 로고    scopus 로고
    • Insights from investigating the interactions of adamantane-based drugs with the M2 proton channel from the H1N1 swine virus
    • Wang, J.F.; Wei, D.Q.; Chou, K.C. Insights from investigating the interactions of adamantane-based drugs with the M2 proton channel from the H1N1 swine virus. Biochem. Biophys. Res. Commun., 2009, 388, 413-417.
    • (2009) Biochem. Biophys. Res. Commun , vol.388 , pp. 413-417
    • Wang, J.F.1    Wei, D.Q.2    Chou, K.C.3
  • 47
    • 0022416469 scopus 로고
    • Gene and protein sequence of an influenza neuraminidase with hemagglutinin activity
    • Air, G.M.; Ritchie, L.R.; Laver, W.G.; Colman, P.M. Gene and protein sequence of an influenza neuraminidase with hemagglutinin activity. Virology, 1985, 145, 117-122.
    • (1985) Virology , vol.145 , pp. 117-122
    • Air, G.M.1    Ritchie, L.R.2    Laver, W.G.3    Colman, P.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.