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Volumn 94, Issue 2, 2008, Pages 434-445

Proton transport through influenza A virus M2 protein reconstituted in vesicles

Author keywords

[No Author keywords available]

Indexed keywords

AMANTADINE; HYDROGEN; IONOPHORE; POTASSIUM; PROTEIN M2; VALINOMYCIN; GRAMICIDIN; LIPOSOME; M2 PROTEIN, INFLUENZA A VIRUS; MATRIX PROTEIN; PROTON; UNCLASSIFIED DRUG;

EID: 38349070736     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.107.109082     Document Type: Article
Times cited : (48)

References (47)
  • 1
    • 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
  • 2
    • 0026612385 scopus 로고
    • Influenza-virus M2 protein has ion channel activity
    • Pinto, L. H., L. J. Holsinger, and R. A. Lamb. 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
  • 3
    • 0029816765 scopus 로고    scopus 로고
    • Selective proton permeability and pH regulation of the influenza virus M2 channel expressed in mouse erythroleukaemia cells
    • Chizhmakov, 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
    • Chizhmakov, I.V.1    Geraghty, F.M.2    Ogden, D.C.3    Hayhurst, A.4    Antoniou, M.5    Hay, A.J.6
  • 7
    • 20444385829 scopus 로고    scopus 로고
    • Chemical rescue of histidine selectivity filter mutants of the M2 ion channel of influenza A virus
    • Venkataraman, P., R. A. Lamb, and L. H. Pinto. 2005. Chemical rescue of histidine selectivity filter mutants of the M2 ion channel of influenza A virus. J. Biol. Chem. 280:21463-21472.
    • (2005) J. Biol. Chem , vol.280 , pp. 21463-21472
    • Venkataraman, P.1    Lamb, R.A.2    Pinto, L.H.3
  • 8
  • 9
    • 0037172965 scopus 로고    scopus 로고
    • Sequence determinants of the energetics of folding of a transmembrane four-helix-bundle protein
    • Howard, K. P., J. D. Lear, and W. F. DeGrado. 2002. Sequence determinants of the energetics of folding of a transmembrane four-helix-bundle protein. Proc. Natl. Acad. Sci. USA. 99:8568-8572.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 8568-8572
    • Howard, K.P.1    Lear, J.D.2    DeGrado, W.F.3
  • 10
    • 0034700255 scopus 로고    scopus 로고
    • pH-dependent 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-dependent 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
  • 11
    • 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
  • 13
    • 0030777711 scopus 로고    scopus 로고
    • Transmembrane four-helix bundle of influenza A M2 protein channel: Structural implications from helix tilt and orientation
    • Kovacs, F. A., and T. A. Cross. 1997. Transmembrane four-helix bundle of influenza A M2 protein channel: structural implications from helix tilt and orientation. Biophys. J. 73:2511-2517.
    • (1997) Biophys. J , vol.73 , pp. 2511-2517
    • Kovacs, F.A.1    Cross, T.A.2
  • 15
    • 0037027306 scopus 로고    scopus 로고
    • + channel helical bundle combining precise orientational and distance restraints from solid state NMR-1
    • + channel helical bundle combining precise orientational and distance restraints from solid state NMR-1. Biochemistry. 41:13170-13177.
    • (2002) Biochemistry , vol.41 , pp. 13170-13177
    • Nishimura, K.1    Kim, S.G.2    Zhang, L.3    Cross, T.A.4
  • 16
    • 15244348542 scopus 로고    scopus 로고
    • The conformation of the pore region of the M2 proton channel depends on lipid bilayer environment
    • Duong-Ly, K. C., V. Nanda, W. F. Degrado, and K. P. Howard. 2005. The conformation of the pore region of the M2 proton channel depends on lipid bilayer environment. Protein Sci. 14:856-861.
    • (2005) Protein Sci , vol.14 , pp. 856-861
    • Duong-Ly, K.C.1    Nanda, V.2    Degrado, W.F.3    Howard, K.P.4
  • 17
    • 0034614541 scopus 로고    scopus 로고
    • Helix tilt of the M2 transmembrane peptide from influenza A virus: An intrinsic property
    • Kovacs, F. A., J. K. Denny, Z. Song, J. R. Quine, and T. A. Cross. 2000. Helix tilt of the M2 transmembrane peptide from influenza A virus: an intrinsic property. J. Mol. Biol. 295:117-125.
    • (2000) J. Mol. Biol , vol.295 , pp. 117-125
    • Kovacs, F.A.1    Denny, J.K.2    Song, Z.3    Quine, J.R.4    Cross, T.A.5
  • 19
    • 0036157061 scopus 로고    scopus 로고
    • C-deuterated alanine: A new label to study membrane protein structure using site-specific infrared dichroism
    • Torres, J., and I. T. Arkin. 2002. C-deuterated alanine: a new label to study membrane protein structure using site-specific infrared dichroism. Biophys. J. 82:1068-1075.
    • (2002) Biophys. J , vol.82 , pp. 1068-1075
    • Torres, J.1    Arkin, I.T.2
  • 20
    • 0142210121 scopus 로고    scopus 로고
    • Initial structural and dynamic characterization of the M2 protein transmembrane and amphipathic helices in lipid bilayers
    • Tian, C. L., 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.L.1    Gao, P.F.2    Pinto, L.H.3    Lamb, R.A.4    Cross, T.A.5
  • 21
    • 0042836529 scopus 로고    scopus 로고
    • Computational studies of proton transport through the M2 channel
    • Wu, Y. J., and G. A. Voth. 2003. Computational studies of proton transport through the M2 channel. FEBS Lett. 552:23-27.
    • (2003) FEBS Lett , vol.552 , pp. 23-27
    • Wu, Y.J.1    Voth, G.A.2
  • 22
    • 28844493428 scopus 로고    scopus 로고
    • How pH opens a H1 channel: The gating mechanism of influenza A M2
    • Kass, I., and I. T. Arkin. 2005. How pH opens a H1 channel: The gating mechanism of influenza A M2. Structure. 13:1789-1798.
    • (2005) Structure , vol.13 , pp. 1789-1798
    • Kass, I.1    Arkin, I.T.2
  • 23
    • 0030803839 scopus 로고    scopus 로고
    • The influenza A virus M2 channel: A molecular modeling and simulation study
    • Sansom, M. S. P., I. D. Kerr, G. R. Smith, and H. S. Son. 1997. The influenza A virus M2 channel: A molecular modeling and simulation study. Virology. 233:163-173.
    • (1997) Virology , vol.233 , pp. 163-173
    • Sansom, M.S.P.1    Kerr, I.D.2    Smith, G.R.3    Son, H.S.4
  • 24
    • 25844476272 scopus 로고    scopus 로고
    • A computational study of the closed and open states of the influenza a M2 proton channel
    • Wu, Y., and G. A. Voth. 2005. A computational study of the closed and open states of the influenza a M2 proton channel. Biophys. J. 89:2402-2411.
    • (2005) Biophys. J , vol.89 , pp. 2402-2411
    • Wu, Y.1    Voth, G.A.2
  • 25
    • 0030973121 scopus 로고    scopus 로고
    • The active oligomeric state of the minimalistic influenza virus M-2 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 M-2 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
  • 26
    • 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
  • 27
    • 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
  • 28
    • 0028980598 scopus 로고
    • Activation of the M(2) 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 M(2) 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
  • 29
    • 0030061323 scopus 로고    scopus 로고
    • Ion selectivity and activation of the M(2) ion channel of influenza virus
    • Shimbo, K., D. L. Brassard, R. A. Lamb, and L. H. Pinto. 1996. Ion selectivity and activation of the M(2) ion channel of influenza virus. Biophys. J. 70:1335-1346.
    • (1996) Biophys. J , vol.70 , pp. 1335-1346
    • Shimbo, K.1    Brassard, D.L.2    Lamb, R.A.3    Pinto, L.H.4
  • 30
    • 0028100022 scopus 로고
    • Direct measurement of the influenza A virus M2 protein ion-channel activity in mammalian cells
    • Wang, C., R. A. Lamb, and L. H. Pinto. 1994. Direct measurement of the influenza A virus M2 protein ion-channel activity in mammalian cells. Virology. 205:133-140.
    • (1994) Virology , vol.205 , pp. 133-140
    • Wang, C.1    Lamb, R.A.2    Pinto, L.H.3
  • 31
    • 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
  • 32
    • 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. I., and C. Schroeder. 2001. Definitive assignment of proton selectivity and attoampere unitary current to the M2 ion channel protein of influenza A virus. Semin. Virol. 75:3647-3656.
    • (2001) Semin. Virol , vol.75 , pp. 3647-3656
    • Lin, T.I.1    Schroeder, C.2
  • 33
    • 0028631914 scopus 로고
    • Functional reconstitution in lipid vesicles of influenza virus M2 protein expressed by baculovirus: Evidence for proton-transfer activity
    • Schroeder, C., C. M. Ford, S. A. Wharton, and A. J. Hay. 1994. Functional reconstitution in lipid vesicles of influenza virus M2 protein expressed by baculovirus: evidence for proton-transfer activity. J. Gen. Virol. 75:3477-3484.
    • (1994) J. Gen. Virol , vol.75 , pp. 3477-3484
    • Schroeder, C.1    Ford, C.M.2    Wharton, S.A.3    Hay, A.J.4
  • 34
    • 0035750381 scopus 로고    scopus 로고
    • Characterization of reconstituted Fo from wild-type Escherichia coli and identification of two other fluxes co-purifying with Fo
    • Cao, N. J. Y., W. S. A. Brusilow, J. J. Tomashek, and D. J. Woodbury. 2001. Characterization of reconstituted Fo from wild-type Escherichia coli and identification of two other fluxes co-purifying with Fo. Cell Biochem. Biophys. 34:305-320.
    • (2001) Cell Biochem. Biophys , vol.34 , pp. 305-320
    • Cao, N.J.Y.1    Brusilow, W.S.A.2    Tomashek, J.J.3    Woodbury, D.J.4
  • 35
    • 16344382800 scopus 로고    scopus 로고
    • Determination of proton flux and conductance at pH 6.8 through single Fo sectors from Escherichia coli
    • Franklin, M. J., W. S. A. Brusilow, and D. J. Woodbury. 2004. Determination of proton flux and conductance at pH 6.8 through single Fo sectors from Escherichia coli. Biophys. J. 87:3594-3599.
    • (2004) Biophys. J , vol.87 , pp. 3594-3599
    • Franklin, M.J.1    Brusilow, W.S.A.2    Woodbury, D.J.3
  • 39
    • 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. L., 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.L.1    Tobler, K.2    Lamb, R.A.3    Pinto, L.H.4    Cross, T.A.5
  • 40
    • 33646494326 scopus 로고    scopus 로고
    • Histidines, heart of the hydrogen ion channel from influenza A virus: Toward an understanding of conductance and proton selectivity
    • Hu, J., R. Fu, K. Nishimura, L. Zhang, H. X. Zhou, D. D. Busath, V. Vijayvergiya, and T. A. Cross. 2006. Histidines, heart of the hydrogen ion channel from influenza A virus: toward an understanding of conductance and proton selectivity. Proc. Natl. Acad. Sci. USA. 103:6865-6870.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 6865-6870
    • Hu, J.1    Fu, R.2    Nishimura, K.3    Zhang, L.4    Zhou, H.X.5    Busath, D.D.6    Vijayvergiya, V.7    Cross, T.A.8
  • 41
    • 11444260782 scopus 로고    scopus 로고
    • Influence of residue 44 on the activity of the M2 proton channel of influenza A virus
    • Betakova, T., F. Ciampor, and A. J. Hay. 2005. Influence of residue 44 on the activity of the M2 proton channel of influenza A virus. J. Gen. Virol. 86:181-184.
    • (2005) J. Gen. Virol , vol.86 , pp. 181-184
    • Betakova, T.1    Ciampor, F.2    Hay, A.J.3
  • 42
    • 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. 88:475-579.
    • (2003) Physiol. Rev , vol.88 , pp. 475-579
    • Decoursey, T.E.1
  • 43
    • 2942675081 scopus 로고    scopus 로고
    • The proton-driven rotor of ATP synthase: Ohmic conductance (10 fS), and absence of voltage gating
    • Feniouk, B. A., M. A. Kozlova, D. A. Knorre, D. A. Cherepanov, A. Y. Mulkidjanian, and W. Junge. 2004. The proton-driven rotor of ATP synthase: Ohmic conductance (10 fS), and absence of voltage gating. Biophys. J. 86:4094-4109.
    • (2004) Biophys. J , vol.86 , pp. 4094-4109
    • Feniouk, B.A.1    Kozlova, M.A.2    Knorre, D.A.3    Cherepanov, D.A.4    Mulkidjanian, A.Y.5    Junge, W.6
  • 44
    • 0023701797 scopus 로고
    • + ion conductance through the gramicidin channel
    • + ion conductance through the gramicidin channel. Biophys. J. 53:25-32.
    • (1988) Biophys. J , vol.53 , pp. 25-32
    • Decker, E.R.1    Levitt, D.G.2
  • 45
    • 0015499163 scopus 로고
    • Ion transfer across lipid membranes in the presence of gramicidin A
    • Myers, V. B., and D. A. Haydon. 1972. Ion transfer across lipid membranes in the presence of gramicidin A. Biophys. J. 274:313-322.
    • (1972) Biophys. J , vol.274 , pp. 313-322
    • Myers, V.B.1    Haydon, D.A.2
  • 46
    • 0016290374 scopus 로고
    • The conformation of gramicidin A
    • Veatch, W. R., E. T. Fossel, and E. R. Blout. 1974. The conformation of gramicidin A. Biochemistry. 13:5249-5256.
    • (1974) Biochemistry , vol.13 , pp. 5249-5256
    • Veatch, W.R.1    Fossel, E.T.2    Blout, E.R.3
  • 47
    • 0033554426 scopus 로고    scopus 로고
    • Total chemical synthesis of the integral membrane protein influenza A virus M2: Role of its C-terminal domain in tetramer assembly
    • Kochendoerfer, G. G., D. Salom, J. D. Lear, R. Wilk-Orescan, S. B. H. Kent, and W. F. DeGrado. 1999. Total chemical synthesis of the integral membrane protein influenza A virus M2: role of its C-terminal domain in tetramer assembly. Biochemistry. 38:11905-11913.
    • (1999) Biochemistry , vol.38 , pp. 11905-11913
    • Kochendoerfer, G.G.1    Salom, D.2    Lear, J.D.3    Wilk-Orescan, R.4    Kent, S.B.H.5    DeGrado, W.F.6


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