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Volumn 254, Issue 1, 1999, Pages 196-209

The influenza virus M2 ion channel protein: Probing the structure of the transmembrane domain in intact cells by using engineered disulfide cross- linking

Author keywords

[No Author keywords available]

Indexed keywords

AMANTADINE; IODINE; ION CHANNEL; SIALIDASE; BIS(1,10 PHENANTHROLINE)COPPER(2+) ION; BIS(1,10-PHENANTHROLINE)COPPER(2+) ION; CROSS LINKING REAGENT; CYSTEINE; DISULFIDE; IODOACETAMIDE; M PROTEIN, INFLUENZA VIRUS; M-PROTEIN, INFLUENZA VIRUS; M2 PROTEIN, INFLUENZA A VIRUS; MATRIX PROTEIN; PHENANTHROLINE DERIVATIVE; THIOL REAGENT;

EID: 0033073762     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1998.9552     Document Type: Article
Times cited : (61)

References (49)
  • 1
    • 0026489631 scopus 로고
    • Thermal motions of surface α-helices in the D-galactose chemosensory receptor
    • Careaga, C. L., and Falke, J. J. (1992). Thermal motions of surface α-helices in the D-galactose chemosensory receptor. J. Mol. Biol. 226, 1219-1235.
    • (1992) J. Mol. Biol. , vol.226 , pp. 1219-1235
    • Careaga, C.L.1    Falke, J.J.2
  • 2
    • 0031564063 scopus 로고    scopus 로고
    • The cysteine residues of the M2 protein are not required for influenza A virus replication
    • Castrucci, M. R., Hughes, M., Calzoletti, L., Donatelli, I., Wells, K., Takada, A., and Kawaoka, Y. (1997). The cysteine residues of the M2 protein are not required for influenza A virus replication. Virology 238, 128-134.
    • (1997) Virology , vol.238 , pp. 128-134
    • Castrucci, M.R.1    Hughes, M.2    Calzoletti, L.3    Donatelli, I.4    Wells, K.5    Takada, A.6    Kawaoka, Y.7
  • 3
    • 0029130732 scopus 로고
    • Transmembrane signaling by the aspartate receptor: Engineered disulfides reveal static regions of the subunit interface
    • Chervitz, S. A., Lin, C. M., and Falke, J. J. (1995). Transmembrane signaling by the aspartate receptor: Engineered disulfides reveal static regions of the subunit interface. Biochemistry 34, 9722-9733.
    • (1995) Biochemistry , vol.34 , pp. 9722-9733
    • Chervitz, S.A.1    Lin, C.M.2    Falke, J.J.3
  • 5
  • 6
    • 0026772384 scopus 로고
    • Evidence that the amantadine-induced, M2-mediated conversion of influenza A virus hemagglutinin to the low pH conformation occurs in an acidic trans Golgi compartment
    • Ciampor, F., Bayley, P. M., Nermut, M. V., Hirst, E. M., Sugrue, R. J., and Hay, A. J. (1992). Evidence that the amantadine-induced, M2-mediated conversion of influenza A virus hemagglutinin to the low pH conformation occurs in an acidic trans Golgi compartment. Virology 188, 14-24.
    • (1992) Virology , vol.188 , pp. 14-24
    • Ciampor, F.1    Bayley, P.M.2    Nermut, M.V.3    Hirst, E.M.4    Sugrue, R.J.5    Hay, A.J.6
  • 7
    • 0026785994 scopus 로고
    • The transmembrane domain of influenza A M2 protein forms amantadine-sensitive proton channels in planar lipid bilayers
    • Duff, K. C., and Ashley, R. H. (1992). The transmembrane domain of influenza A M2 protein forms amantadine-sensitive proton channels in planar lipid bilayers. Virology 190, 485-489.
    • (1992) Virology , vol.190 , pp. 485-489
    • Duff, K.C.1    Ashley, R.H.2
  • 8
    • 0026745087 scopus 로고
    • The secondary structure of influenza A M2 transmembrane domain
    • Duff, K. C., Kelly, S. M., Price, N. C., and Bradshaw, J. P. (1992). The secondary structure of influenza A M2 transmembrane domain. FEBS Lett. 311, 256-258.
    • (1992) FEBS Lett. , vol.311 , pp. 256-258
    • Duff, K.C.1    Kelly, S.M.2    Price, N.C.3    Bradshaw, J.P.4
  • 9
    • 0023224051 scopus 로고
    • Global flexibility in a sensory receptor: A site-directed cross-linking approach
    • Falke, J. J., and Koshland, D. E., Jr. (1987). Global flexibility in a sensory receptor: A site-directed cross-linking approach. Science 237, 1596-1600.
    • (1987) Science , vol.237 , pp. 1596-1600
    • Falke, J.J.1    Koshland D.E., Jr.2
  • 10
    • 0031029785 scopus 로고    scopus 로고
    • Cysteine-scanning mutagenesis of helix II and flanking hydrophilic domains in the lactose permease of Escherichia coli
    • Frillingos, S., Sun, J., Gonzalez, A., and Kaback, H. R. (1997). Cysteine-scanning mutagenesis of helix II and flanking hydrophilic domains in the lactose permease of Escherichia coli. Biochemistry 36, 269-273.
    • (1997) Biochemistry , vol.36 , pp. 269-273
    • Frillingos, S.1    Sun, J.2    Gonzalez, A.3    Kaback, H.R.4
  • 12
    • 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 Hay, A. J. (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
  • 13
    • 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
  • 14
    • 0022157043 scopus 로고
    • The molecular basis of the specific anti-influenza action of amantadine
    • Hay, A. J., Wolstenholme, A. J., Skehel, J. J., and Smith, M. H. (1985). The molecular basis of the specific anti-influenza action of amantadine. EMBO J. 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
  • 15
    • 0025923280 scopus 로고
    • 2 integral membrane protein is a homotetramer stabilized by formation of disulfide bonds
    • 2 integral membrane protein is a homotetramer stabilized by formation of disulfide bonds. Virology 183, 32-43.
    • (1991) Virology , vol.183 , pp. 32-43
    • Holsinger, L.J.1    Lamb, R.A.2
  • 18
    • 0029910912 scopus 로고    scopus 로고
    • Detecting the conformational change of transmembrane signaling in a bacterial chemoreceptor by measuring effects on disulfide cross-linking in vivo
    • Hughson, A. G., and Hazelbauer, G. L. (1996). Detecting the conformational change of transmembrane signaling in a bacterial chemoreceptor by measuring effects on disulfide cross-linking in vivo. Proc. Natl. Acad. Sci. USA 93, 11546-11551.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 11546-11551
    • Hughson, A.G.1    Hazelbauer, G.L.2
  • 19
    • 0031056669 scopus 로고    scopus 로고
    • Analysis of protein structure in intact cells: Crosslinking in vivo between introduced cysteines in the transmembrane domain of a bacterial chemoreceptor
    • Hughson, A. G., Lee, G. F., and Hazelbauer, G. L. (1997). Analysis of protein structure in intact cells: Crosslinking in vivo between introduced cysteines in the transmembrane domain of a bacterial chemoreceptor. Protein Sci. 6, 315-322.
    • (1997) Protein Sci. , vol.6 , pp. 315-322
    • Hughson, A.G.1    Lee, G.F.2    Hazelbauer, G.L.3
  • 20
    • 0032499690 scopus 로고    scopus 로고
    • 0 ATP synthase of Escherichia coli defined by disulfide cross-linking
    • 0 ATP synthase of Escherichia coli defined by disulfide cross-linking. Proc. Natl. Acad. Sci. USA 95, 6607-6612.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6607-6612
    • Jiang, W.1    Fillingame, R.H.2
  • 21
    • 0023034995 scopus 로고
    • The crystallographically determined structures of atypical strained disulfides engineered into subtilisin
    • Katz, B. A., and Kossiakoff, A. (1986). The crystallographically determined structures of atypical strained disulfides engineered into subtilisin. J. Biol. Chem. 261, 15480-15485.
    • (1986) J. Biol. Chem. , vol.261 , pp. 15480-15485
    • Katz, B.A.1    Kossiakoff, A.2
  • 22
    • 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 Cross, T. A. (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
  • 23
    • 0017090158 scopus 로고
    • Synthesis of influenza virus proteins in infected cells: Translation of viral polypeptides, including three P polypeptides, from RNA produced by primary transcription
    • Lamb, R. A., and Choppin, P. W. (1976). Synthesis of influenza virus proteins in infected cells: Translation of viral polypeptides, including three P polypeptides, from RNA produced by primary transcription. Virology 74, 504-519.
    • (1976) Virology , vol.74 , pp. 504-519
    • Lamb, R.A.1    Choppin, P.W.2
  • 24
    • 0003156040 scopus 로고
    • 2 ion channel protein and its role in the influenza virus life cycle
    • (E. Wimmer, Ed.), Cold Spring Harbor Press, Cold Spring Harbor, New York
    • 2 ion channel protein and its role in the influenza virus life cycle. In "Receptor-Mediated Virus Entry into Cells" (E. Wimmer, Ed.), pp. 303-321, Cold Spring Harbor Press, Cold Spring Harbor, New York.
    • (1994) Receptor-Mediated Virus Entry into Cells , pp. 303-321
    • Lamb, R.A.1    Holsinger, L.J.2    Pinto, L.H.3
  • 25
    • 0021893484 scopus 로고
    • 2 protein is an integral membrane protein expressed on the infected-cell surface
    • 2 protein is an integral membrane protein expressed on the infected-cell surface. Cell 40, 627-633.
    • (1985) Cell , vol.40 , pp. 627-633
    • Lamb, R.A.1    Zebedee, S.L.2    Richardson, C.D.3
  • 26
    • 0028090254 scopus 로고
    • Deducing the organization of a transmembrane domain by disulfide cross-linking
    • Lee, G. F., Burrows, G. G., Lebert, M. R., Dutton, D. P., and Hazelbauer, G. L. (1994). Deducing the organization of a transmembrane domain by disulfide cross-linking. J. Biol. Chem. 269, 29920-29927.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29920-29927
    • Lee, G.F.1    Burrows, G.G.2    Lebert, M.R.3    Dutton, D.P.4    Hazelbauer, G.L.5
  • 27
    • 0029047850 scopus 로고
    • Identification of functionally important helical faces in transmembrane segments by scanning mutagenesis
    • Lee, G. F., Dutton, D. P., and Hazelbauer, G. L. (1995a). Identification of functionally important helical faces in transmembrane segments by scanning mutagenesis. Proc. Natl. Acad. Sci. USA 92, 5416-5420.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5416-5420
    • Lee, G.F.1    Dutton, D.P.2    Hazelbauer, G.L.3
  • 28
    • 0028924963 scopus 로고
    • Transmembrane signalling characterized in bacterials chemoreceptors by using sulfhydryl cross-linking in vivo
    • Lee, G. F., Lebert, M. R., Lilly, A. A., and Hazelbauer, G. L. (1995b). Transmembrane signalling characterized in bacterials chemoreceptors by using sulfhydryl cross-linking in vivo. Proc. Natl. Acad. Sci. USA 92, 3391-3395.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3391-3395
    • Lee, G.F.1    Lebert, M.R.2    Lilly, A.A.3    Hazelbauer, G.L.4
  • 29
    • 0025872118 scopus 로고
    • Disulfide cross-linking studies of the transmembrane regions of the aspartate sensory receptor of Escherichia coli
    • Lynch, B. A., and Koshland, D. E., Jr. (1991). Disulfide cross-linking studies of the transmembrane regions of the aspartate sensory receptor of Escherichia coli. Proc. Natl. Acad. Sci. USA 88, 10402-10406.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10402-10406
    • Lynch, B.A.1    Koshland D.E., Jr.2
  • 30
    • 0026605299 scopus 로고
    • Determination of transmembrane protein structure by disulfide cross-linking: The Escherichia coli Tar receptor
    • Pakula, A. A., and Simon, M. J. (1992). Determination of transmembrane protein structure by disulfide cross-linking: The Escherichia coli Tar receptor. Proc. Natl. Acad. Sci. USA 89, 4144-4148.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4144-4148
    • Pakula, A.A.1    Simon, M.J.2
  • 31
    • 0026502806 scopus 로고
    • Oligomeric organization and strain- specific proteolytic modification of the virion M2 protein of influenza A H1N1 viruses
    • Panayotov, P. P., and Schlesinger, R. W. (1992). Oligomeric organization and strain- specific proteolytic modification of the virion M2 protein of influenza A H1N1 viruses. Virology 186, 352-355.
    • (1992) Virology , vol.186 , pp. 352-355
    • Panayotov, P.P.1    Schlesinger, R.W.2
  • 32
    • 0002285832 scopus 로고
    • The molecular biology of influenza viruses and paramyxoviruses
    • (A. Davidson and R. M. Elliott, Eds.), IRL Oxford University Press, Oxford, UK
    • Paterson, R. G., and Lamb, R. A. (1993). The molecular biology of influenza viruses and paramyxoviruses. In "Molecular Virology: A Practical Approach" (A. Davidson and R. M. Elliott, Eds.), pp. 35-73, IRL Oxford University Press, Oxford, UK.
    • (1993) Molecular Virology: A Practical Approach , pp. 35-73
    • Paterson, R.G.1    Lamb, R.A.2
  • 35
    • 0025868356 scopus 로고
    • A new cationic liposome reagent mediating nearly quantitative transfection of animal cells
    • Rose, J. K., Bonagurio, B., and Whitt, M. A. (1991). A new cationic liposome reagent mediating nearly quantitative transfection of animal cells. Biotechniques 10, 520-525.
    • (1991) Biotechniques , vol.10 , pp. 520-525
    • Rose, J.K.1    Bonagurio, B.2    Whitt, M.A.3
  • 38
    • 0030803839 scopus 로고    scopus 로고
    • The influenza A virus M2 channel: A molecular modeling and simulation study
    • Sansom, M. S. P., Kerr, I. D., Smith, G. R., and Son, H. S. (1997). The influenza A virus M2 channel: A molecular modeling and simulation study. Virology 233, 162-173.
    • (1997) Virology , vol.233 , pp. 162-173
    • Sansom, M.S.P.1    Kerr, I.D.2    Smith, G.R.3    Son, H.S.4
  • 39
    • 0028631914 scopus 로고
    • Functional reconstitution in lipid vesicles of influenza virus M2 protein expressed by baculovirus: Evidence for proton transfer activity
    • Schroeder, C., Ford, C. M., Wharton, S. A., and Hay, A. J. (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
  • 41
    • 0026743377 scopus 로고
    • Structure and dynamics of transmembrane signaling by the Escherichia coli aspartate receptor
    • Stoddard, B. L., Bui, J. D., and Koshland, D. E., Jr. (1992). Structure and dynamics of transmembrane signaling by the Escherichia coli aspartate receptor. Biochemistry 31, 11978-11983.
    • (1992) Biochemistry , vol.31 , pp. 11978-11983
    • Stoddard, B.L.1    Bui, J.D.2    Koshland D.E., Jr.3
  • 42
    • 0026008031 scopus 로고
    • Structural characteristics of the M2 protein of the influenza A viruses: Evidence that it forms a tetrameric channel
    • Sugrue, R. J., and Hay, A. J. (1991). Structural characteristics of the M2 protein of the 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
  • 44
    • 0028100022 scopus 로고
    • 2 protein ion channel activity in mammalian cells
    • 2 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
  • 45
    • 0028980598 scopus 로고
    • 2 ion channel of influenza virus: A role for the transmembrane domain histidine residue
    • 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
  • 47
    • 0029085803 scopus 로고
    • Cysteine scanning mutagenesis of helix V in the lactose permease of Escherichia coli
    • Weitzman, C., and Kaback, H. R. (1995). Cysteine scanning mutagenesis of helix V in the lactose permease of Escherichia coli. Biochemistry 34, 9374-9379.
    • (1995) Biochemistry , vol.34 , pp. 9374-9379
    • Weitzman, C.1    Kaback, H.R.2
  • 49
    • 0022345295 scopus 로고
    • 2 integral membrane protein and expression at the infected-cell surface from cloned cDNA
    • 2 integral membrane protein and expression at the infected-cell surface from cloned cDNA. J. Virol. 56, 502-511.
    • (1985) J. Virol. , vol.56 , pp. 502-511
    • Zebedee, S.L.1    Richardson, C.D.2    Lamb, R.A.3


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