메뉴 건너뛰기




Volumn 87, Issue 3, 2004, Pages 1697-1704

Proton conductance of influenza virus M2 protein in planar lipid bilayers

Author keywords

[No Author keywords available]

Indexed keywords

AMANTADINE; CHLORIDE ION; HYDROCHLORIC ACID; LIPOSOME; PROTEIN M2; PROTON; SODIUM ION; TETRYLAMMONIUM; VIRUS PROTEIN;

EID: 4444265755     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.104.043018     Document Type: Article
Times cited : (52)

References (53)
  • 2
    • 1842427673 scopus 로고    scopus 로고
    • A novel method of resistance for influenza against a channel-blocking antiviral drug
    • Astrahan, P., I. Kass, M. A. Cooper, and I. T. Arkin. 2004. A novel method of resistance for influenza against a channel-blocking antiviral drug. Proteins. 55:251-257.
    • (2004) Proteins , vol.55 , pp. 251-257
    • Astrahan, P.1    Kass, I.2    Cooper, M.A.3    Arkin, I.T.4
  • 3
    • 0033073762 scopus 로고    scopus 로고
    • The influenza virus M2 ion channel protein. Probing the structure of the transmembrane domain in intact cells by using engineered disulfide cross-linking
    • Bauer, C. M., L. H. Pinto, T. A. Cross, and R. A. Lamb. 1999. The influenza virus M2 ion channel protein. Probing the structure of the transmembrane domain in intact cells by using engineered disulfide cross-linking. Virology. 254:196-209.
    • (1999) Virology , vol.254 , pp. 196-209
    • Bauer, C.M.1    Pinto, L.H.2    Cross, T.A.3    Lamb, R.A.4
  • 5
    • 0037458056 scopus 로고    scopus 로고
    • Kinetic isotope effects of proton transfer in aqueous and methanol containing solutions, and in gramicidin A channels
    • Cherayshev, A., R. Pomès, and S. Cukierman. 2003. Kinetic isotope effects of proton transfer in aqueous and methanol containing solutions, and in gramicidin A channels. Biophys. Chem. 103:179-190.
    • (2003) Biophys. Chem. , vol.103 , pp. 179-190
    • Cherayshev, A.1    Pomès, R.2    Cukierman, S.3
  • 6
    • 0029816765 scopus 로고    scopus 로고
    • Selective proton permeability and pH regulation of the influenza virus M2 channel expressed in mouse erythroleukaemia cells
    • Chizhniakov, I. V., F. M. Geraghty, D. C. Ogden, A. Hayhurst, M. Antoniou, and A. J. Hay. 1996. Selective proton permeability and pH regulation of the influenza virus M2 channel expressed in mouse erythroleukaemia cells. J. Physiol. 494:329-336.
    • (1996) J. Physiol. , vol.494 , pp. 329-336
    • Chizhniakov, I.V.1    Geraghty, F.M.2    Ogden, D.C.3    Hayhurst, A.4    Antoniou, M.5    Hay, A.J.6
  • 8
    • 0345598917 scopus 로고    scopus 로고
    • Use of thiol-disulfide equilibria to measure the energetics of assembly of transmembrane helices in phospholipid bilayers
    • Cristian, L., J. D. Lear, and W. F. DeGrado. 2003. Use of thiol-disulfide equilibria to measure the energetics of assembly of transmembrane helices in phospholipid bilayers. Proc. Natl. Acad. Sci. USA. 100: 14772-14777.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 14772-14777
    • Cristian, L.1    Lear, J.D.2    DeGrado, W.F.3
  • 9
    • 0030786782 scopus 로고    scopus 로고
    • Proton conductance in gramicidin A and its dioxolane-linked dimer in different bilayers
    • Cukierman, S., E. P. Quigley, and D. S. Crumrine. 1997. Proton conductance in gramicidin A and its dioxolane-linked dimer in different bilayers. Biophys. J. 73:2489-2502.
    • (1997) Biophys. J. , vol.73 , pp. 2489-2502
    • Cukierman, S.1    Quigley, E.P.2    Crumrine, D.S.3
  • 10
    • 0037379781 scopus 로고    scopus 로고
    • Voltage-gated proton channels and other proton transfer pathways
    • DeCoursey, T. E. 2003. Voltage-gated proton channels and other proton transfer pathways. Physiol. Rev. 83:475-579.
    • (2003) Physiol. Rev. , vol.83 , pp. 475-579
    • DeCoursey, T.E.1
  • 11
    • 0026785994 scopus 로고
    • The transmembrane domain of influenza A M2 protein forms amantadine-sensitive proton channels in planar lipid bilayers
    • Duff, K. C., and R. H. Ashley. 1992. The transmembrane domain of influenza A M2 protein forms amantadine-sensitive proton channels in planar lipid bilayers. Virology. 190:485-89.
    • (1992) Virology , vol.190 , pp. 485-489
    • Duff, K.C.1    Ashley, R.H.2
  • 12
    • 0027963402 scopus 로고
    • Neutron diffraction reveals the site of amantadine blockage in the influenza A M2 ion channel
    • Duff, K. C., P. J. Gilchrist, A. M. Saxena, and J. P. Bradshaw. 1994. Neutron diffraction reveals the site of amantadine blockage in the influenza A M2 ion channel. Virology. 202:287-293.
    • (1994) Virology , vol.202 , pp. 287-293
    • Duff, K.C.1    Gilchrist, P.J.2    Saxena, A.M.3    Bradshaw, J.P.4
  • 13
    • 0034030929 scopus 로고    scopus 로고
    • Exploring models of the influenza A M2 channel: MD simulations in a phospholipid bilayer
    • Forrest, L. R., A. Kukol, I. T. Arkin, D. P. Tieleman, and M. S. P. Sansom. 2000. Exploring models of the influenza A M2 channel: MD simulations in a phospholipid bilayer. Biophys. J. 78:55-69.
    • (2000) Biophys. J. , vol.78 , pp. 55-69
    • Forrest, L.R.1    Kukol, A.2    Arkin, I.T.3    Tieleman, D.P.4    Sansom, M.S.P.5
  • 15
    • 0026787707 scopus 로고
    • Maturation of influenza A virus hemagglutinin-estimates of the pH encountered during transport and its regulation by the M2 protein
    • Grambas, S., and A. J. Hay. 1992. Maturation of influenza A virus hemagglutinin-estimates of the pH encountered during transport and its regulation by the M2 protein. Virology. 190:11-18.
    • (1992) Virology , vol.190 , pp. 11-18
    • Grambas, S.1    Hay, A.J.2
  • 16
    • 0002988267 scopus 로고
    • The action of adamantanamines against influenza A viruses: Inhibition of the M2 ion channel protein
    • Hay, A. J. 1992. The action of adamantanamines 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
  • 17
    • 0030777711 scopus 로고    scopus 로고
    • Transmembrane 4-helix bundle of influenza A M2 protein channel: Structural implications from helix tilt and orientation
    • Kovacs, F., and T. A. Cross. 1997. Transmembrane 4-helix bundle of influenza A M2 protein channel: structural implications from helix tilt and orientation. Biophys. J. 74:2511-2517.
    • (1997) Biophys. J. , vol.74 , pp. 2511-2517
    • Kovacs, F.1    Cross, T.A.2
  • 19
    • 0042836535 scopus 로고    scopus 로고
    • Proton conduction through the M2 protein of the influenza A virus; a quantitative, mechanistic analysis of experimental data
    • Lear, J. D. 2003. Proton conduction through the M2 protein of the influenza A virus; a quantitative, mechanistic analysis of experimental data. FEBS Lett. 552:17-22.
    • (2003) FEBS Lett. , vol.552 , pp. 17-22
    • Lear, J.D.1
  • 20
    • 0018072320 scopus 로고
    • Number of water molecules coupled to the transport of sodium, potassium, and hydrogen ions via gramicidin, nonactin or valinomycirt
    • Levitt, D. G., S. R. Elias, and J. M. Hautman. 1978. Number of water molecules coupled to the transport of sodium, potassium, and hydrogen ions via gramicidin, nonactin or valinomycirt. Biochim. Biophys. Acta. 512:436-451.
    • (1978) Biochim. Biophys. Acta , vol.512 , pp. 436-451
    • Levitt, D.G.1    Elias, S.R.2    Hautman, J.M.3
  • 21
    • 0035085645 scopus 로고    scopus 로고
    • Definitive assignment of proton selectivity and attoampere unitary current to the M2 ion channel protein of influenza A virus
    • Lin, T., and C. Schroeder. 2001. Definitive assignment of proton selectivity and attoampere unitary current to the M2 ion channel protein of influenza A virus. J. Virol. 75:3647-3656.
    • (2001) J. Virol. , vol.75 , pp. 3647-3656
    • Lin, T.1    Schroeder, C.2
  • 25
    • 0037027306 scopus 로고    scopus 로고
    • + channel helical bundle combining precise orientational and distance restraints from solid state NMR
    • + channel helical bundle combining precise orientational and distance restraints from solid state NMR. Biochemistry. 41:13170-13177.
    • (2002) Biochemistry , vol.41 , pp. 13170-13177
    • Nishimura, K.1    Kim, S.2    Zhang, L.3    Cross, T.A.4
  • 26
    • 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., T. Miura, and H. Takeuchi. 2001. Protonation of histidine and histidine-tryptophan interaction in the activation of the M2 ion channel from influenza A virus. Biochemistry. 40:6053-6060.
    • (2001) Biochemistry , vol.40 , pp. 6053-6060
    • Okada, A.1    Miura, T.2    Takeuchi, H.3
  • 27
    • 0032755470 scopus 로고    scopus 로고
    • Noncontact dipole effects on channel permeation. III. Anomalous proton conductance effects in gramicidin
    • Phillips, L. R., C. D. Cole, R. J. Hendershot, M. Cotton, T. A. Cross, and D. D. Busath. 1999. Noncontact dipole effects on channel permeation. III. Anomalous proton conductance effects in gramicidin. Biophys. J. 77:2492-2501.
    • (1999) Biophys. J. , vol.77 , pp. 2492-2501
    • Phillips, L.R.1    Cole, C.D.2    Hendershot, R.J.3    Cotton, M.4    Cross, T.A.5    Busath, D.D.6
  • 29
    • 0029038155 scopus 로고
    • Understanding the mechanism of action of the anti-influenza virus drug amantadine
    • Pinto, L. H., and R. A. Lamb. 1995. Understanding the mechanism of action of the anti-influenza virus drug amantadine. Trends Microbiol. 3:271.
    • (1995) Trends Microbiol. , vol.3 , pp. 271
    • Pinto, L.H.1    Lamb, R.A.2
  • 30
    • 0030011088 scopus 로고    scopus 로고
    • + translocation along the single-file water chain in the gramicidin A channel
    • + translocation along the single-file water chain in the gramicidin A channel. Biophys. J. 71:19-39.
    • (1996) Biophys. J. , vol.71 , pp. 19-39
    • Pomès, R.1    Roux, B.2
  • 31
    • 0036225143 scopus 로고    scopus 로고
    • Molecular mechanism of H conduction in the single-file water chain of the gramicidin channel
    • Pomès, R., and B. Roux. 2002. Molecular mechanism of H conduction in the single-file water chain of the gramicidin channel. Biophys. J. 82: 2304-2316.
    • (2002) Biophys. J. , vol.82 , pp. 2304-2316
    • Pomès, R.1    Roux, B.2
  • 32
    • 0029757992 scopus 로고    scopus 로고
    • Thermodynamic stability of water molecules in the bacteriorhodopsin proton channel: A molecular dynamics free energy perturbation study
    • Roux, B., M. Nina, R. Pomes, and J. C. Smith. 1996. Thermodynamic stability of water molecules in the bacteriorhodopsin proton channel: a molecular dynamics free energy perturbation study. Biophys. J. 71: 670-681.
    • (1996) Biophys. J. , vol.71 , pp. 670-681
    • Roux, B.1    Nina, M.2    Pomes, R.3    Smith, J.C.4
  • 33
    • 0029878757 scopus 로고    scopus 로고
    • Structure and dynamics of hydronium in the ion channel gramicidin A
    • Sagnella, D. E., and G. A. Voth. 1996. Structure and dynamics of hydronium in the ion channel gramicidin A. Biophys. J. 70:2043-2051.
    • (1996) Biophys. J. , vol.70 , pp. 2043-2051
    • Sagnella, D.E.1    Voth, G.A.2
  • 34
    • 0030973121 scopus 로고    scopus 로고
    • The active oligomeric state of the minimalistic influenza virus M2 ion channel is a tetramer
    • Sakaguchi, T., Q. A. Tu, L. H. Pinto, and R. A. Lamb. 1997. The active oligomeric state of the minimalistic influenza virus M2 ion channel is a tetramer. Proc. Natl. Acad. Sci. USA. 94:5000-5005.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 5000-5005
    • Sakaguchi, T.1    Tu, Q.A.2    Pinto, L.H.3    Lamb, R.A.4
  • 35
    • 0034700255 scopus 로고    scopus 로고
    • pH-dependem tetramerization and amantadine binding of the transmembrane helix of M2 from the influenza A virus
    • Salom, D., B. R. Hill, J. D. Lear, and W. F. DeGrado. 2000. pH-dependem tetramerization and amantadine binding of the transmembrane helix of M2 from the influenza A virus. Biochemistry. 39:14160-14170.
    • (2000) Biochemistry , vol.39 , pp. 14160-14170
    • Salom, D.1    Hill, B.R.2    Lear, J.D.3    DeGrado, W.F.4
  • 36
    • 0034039757 scopus 로고    scopus 로고
    • Computer simulation of ion channel gating: The M2 channel on influenza A virus in a lipid bilayer
    • Schweighofer, K. J., and A. Pohorille. 2000. Computer simulation of ion channel gating: The M2 channel on influenza A virus in a lipid bilayer. Biophys. J. 78:150-163.
    • (2000) Biophys. J. , vol.78 , pp. 150-163
    • Schweighofer, K.J.1    Pohorille, A.2
  • 37
    • 0030061323 scopus 로고    scopus 로고
    • Ion selectivity and activation of the M2 ion channel of influenza virus
    • Shimbo, K., D. L. Baddard, R. A. Lamb, and L. H. Pinto. 1996. Ion selectivity and activation of the M2 ion channel of influenza virus. Biophys. J. 70:1335-1346.
    • (1996) Biophys. J. , vol.70 , pp. 1335-1346
    • Shimbo, K.1    Baddard, D.L.2    Lamb, R.A.3    Pinto, L.H.4
  • 38
    • 0036789499 scopus 로고    scopus 로고
    • Molecular dynamics simulation of proton transport through the influenza A virus M2 channel
    • Smondyrev, A. M., and G. A. Voth. 2002. Molecular dynamics simulation of proton transport through the influenza A virus M2 channel. Biophys. J. 83:1987-1996.
    • (2002) Biophys. J. , vol.83 , pp. 1987-1996
    • Smondyrev, A.M.1    Voth, G.A.2
  • 40
    • 0026008031 scopus 로고
    • Structural characteristics of the M2 protein of influenza A viruses: Evidence that it forms a tetrameric channel
    • Sugrue, R. J., and A. J. Hay. 1991. Structural characteristics of the M2 protein of influenza A viruses: Evidence that it forms a tetrameric channel. Virology. 180:617-624.
    • (1991) Virology , vol.180 , pp. 617-624
    • Sugrue, R.J.1    Hay, A.J.2
  • 41
    • 0037131381 scopus 로고    scopus 로고
    • The gate of the influenza virus M2 proton channel is formed by a single tryptophan residue
    • Tang, Y., F. Saitseva, R. A. Lamb, and L. H. Pinto. 2002. The gate of the influenza virus M2 proton channel is formed by a single tryptophan residue. J. Biol. Chem. 277:39880-39886.
    • (2002) J. Biol. Chem. , vol.277 , pp. 39880-39886
    • Tang, Y.1    Saitseva, F.2    Lamb, R.A.3    Pinto, L.H.4
  • 42
    • 0142210121 scopus 로고    scopus 로고
    • Initial structural and dynamic characterization of the M2 protein transmembrane and amphipathic helices in lipid bilayers
    • Tian, C., P. F. Gao, L. H. Pinto, R. A. Lamb, and T. A. Cross. 2003. Initial structural and dynamic characterization of the M2 protein transmembrane and amphipathic helices in lipid bilayers. Protein Sci. 12:2597-2605.
    • (2003) Protein Sci. , vol.12 , pp. 2597-2605
    • Tian, C.1    Gao, P.F.2    Pinto, L.H.3    Lamb, R.A.4    Cross, T.A.5
  • 43
    • 0037125949 scopus 로고    scopus 로고
    • Expression and initial structural insights from solid-state NMR of the M2 proton channel from influenza A virus
    • Tian, C., K. Tobler, R. A. Lamb, L. H. Pinto, and T. A. Cross. 2002. Expression and initial structural insights from solid-state NMR of the M2 proton channel from influenza A virus. Biochemistry. 41:11294-11300.
    • (2002) Biochemistry , vol.41 , pp. 11294-11300
    • Tian, C.1    Tobler, K.2    Lamb, R.A.3    Pinto, L.H.4    Cross, T.A.5
  • 44
    • 0025073251 scopus 로고
    • Ionization of phospholipids and phospholipid-supported interfacial lateral diffusion of protons in membrane model systems
    • Tocanne, J.-F., and J. Teissié. 1990. Ionization of phospholipids and phospholipid-supported interfacial lateral diffusion of protons in membrane model systems. Biochim. Biophys. Acta. 1031:111-142.
    • (1990) Biochim. Biophys. Acta , vol.1031 , pp. 111-142
    • Tocanne, J.-F.1    Teissié, J.2
  • 45
  • 46
    • 85030829789 scopus 로고    scopus 로고
    • Ion channel studies of influenza virus M2 in planar lipid bilayers
    • Abstr.
    • Vijayvergiya, V., T. A. Cross, and D. D. Busath. 2003. Ion channel studies of influenza virus M2 in planar lipid bilayers. Biophys. J. 84:488a (Abstr.)
    • (2003) Biophys. J. , vol.84
    • Vijayvergiya, V.1    Cross, T.A.2    Busath, D.D.3
  • 47
    • 85030825777 scopus 로고    scopus 로고
    • Single channel conductance of influenza virus M2 protein in planar lipid bilayers
    • Abstr.
    • Vijayvergiya, V., R. R. Wilson, A. Chorak, F. Gao, T. A. Cross, and D. D. Busath. 2004. Single channel conductance of influenza virus M2 protein in planar lipid bilayers. Biophys. J. 86:550a. (Abstr.)
    • (2004) Biophys. J. , vol.86
    • Vijayvergiya, V.1    Wilson, R.R.2    Chorak, A.3    Gao, F.4    Cross, T.A.5    Busath, D.D.6
  • 50
    • 0028980598 scopus 로고
    • Activation of the M2 ion channel of influenza virus: A role for the transmembrane domain histidine residue
    • Wang, C., R. A. Lamb, and L. H. Pinto. 1995. Activation of the M2 ion channel of influenza virus: a role for the transmembrane domain histidine residue. Biophys. J. 69:1363-1371.
    • (1995) Biophys. J. , vol.69 , pp. 1363-1371
    • Wang, C.1    Lamb, R.A.2    Pinto, L.H.3
  • 51
    • 0027185716 scopus 로고
    • Ion channel activity of influenza A virus M2 protein: Characterization of the amantadine block
    • Wang, C., K. Takeuchi, L. H. Pinto, and R. A. Lamb. 1993. Ion channel activity of influenza A virus M2 protein: characterization of the amantadine block. J. Virol. 67:5585-5594.
    • (1993) J. Virol. , vol.67 , pp. 5585-5594
    • Wang, C.1    Takeuchi, K.2    Pinto, L.H.3    Lamb, R.A.4
  • 53
    • 0037861907 scopus 로고    scopus 로고
    • Water and proton conduction through carbon nanotubes as models for biological channels
    • Zhu, F., and K. Schulten. 2003. Water and proton conduction through carbon nanotubes as models for biological channels. Biophys. J. 85: 236-244.
    • (2003) Biophys. J. , vol.85 , pp. 236-244
    • Zhu, F.1    Schulten, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.