View More View Less
  • 1 Institute of Virology, Slovak Academy of Sciences Dúbravská cesta 9, 842 45 Bratislava, Slovak Republic
Restricted access

Purchase article

USD  $25.00

1 year subscription (Individual Only)

USD  $784.00

Pathogenicity and virulence are multifactorial traits, depending on interaction of viruses with susceptible cells and organisms. The ion channels coded by viruses, viroporins, represent only one factor taking part in the cascade of interactions between virus and cell, leading to the entry of virus, replication and to profound changes in membrane permeability. The M2 protein from influenza A virus forms proton-selective, pH-regulated channel involved in regulating vesicular pH, a function important for the correct maturation of HA glycoprotein. The NB glycoprotein of influenza B viruses is an integral membrane protein with an ion channel activity. The CM2 protein of influenza C virus is an integral membrane glycoprotein structurally analogous to influenza A virus M2 and influenza B virus NB proteins. The picornavirus 3A protein is involved in cell lysis and shows homology with other lytic proteins. Vpu is an oligomeric integral membrane protein encoded by HIV-1, which forms ion channels. The togavirus 6K protein shows structural similarities with other viroporins.

  • Wharton, S. A., Belshe, R. B., Skehel, J. J., Hay, A. J.: Role of virion M2 protein in influenza virus uncoating: specific reduction in the rate of membrane fusion between virus and liposomes by amantadine. J Gen Virol 75, 945-955 (1994).

    'Role of virion M2 protein in influenza virus uncoating: specific reduction in the rate of membrane fusion between virus and liposomes by amantadine. ' () 75 J Gen Virol : 945 -955.

    • Search Google Scholar
  • Sakaguchi, T., Lesser, G. P., Lamb, R. A.: The ion channel activity of the influenza virus M2 protein affects transport through the Golgi apparatus. J Cell Biol 133, 733-747 (1996).

    'The ion channel activity of the influenza virus M2 protein affects transport through the Golgi apparatus. ' () 133 J Cell Biol : 733 -747.

    • Search Google Scholar
  • Chen, J., Lee, K. H., Steinhauer, D. A., Stevens, D. J., Skehel, J. J., Wiley, D. C.: Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation. Cell 95, 409-417 (1998).

    'Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation. ' () 95 Cell : 409 -417.

    • Search Google Scholar
  • Čon;iampor, F., Thompson, C. A., Grambas, S., Hay, A. J.: Regulation of pH by the M2 protein of influenza A viruses. Virus Res 22, 247-258 (1992b).

    'Regulation of pH by the M2 protein of influenza A viruses. ' () 22 Virus Res : 247 -258.

  • Lin, Tse-I., Heider, H., Schroeder, C.: Different modes of inhibition by amantadine amine derivates and natural polyamines of the functionally reconstituted influenza virus M2 proton channel. J Gen Virol 78, 767-774 (1997).

    'Different modes of inhibition by amantadine amine derivates and natural polyamines of the functionally reconstituted influenza virus M2 proton channel. ' () 78 J Gen Virol : 767 -774.

    • Search Google Scholar
  • Helenius, A.: Unpacking the incoming influenza virus. Cell 69, 577-578 (1992).

    'Unpacking the incoming influenza virus. ' () 69 Cell : 577 -578.

  • Čon;iampor, F.: Electron microscopy and confocal scanning imaging system in the process of intracellular transport and conformational changes of virus structural proteins. Microscopia Elletronica 2, 445-449 (1993).

    'Electron microscopy and confocal scanning imaging system in the process of intracellular transport and conformational changes of virus structural proteins. ' () 2 Microscopia Elletronica : 445 -449.

    • Search Google Scholar
  • Čon;iampor, F., Varečon;ková, E., Mucha, V., Betáková, T., Cmarko, D., Hanincová, J., Závodská, E.: Immuno-electron microscopy of influenza haemagglutinin (HA1 and HA2) and M2 protein molecules and their intracellular transport. Am J Trop Med Hyg 3, S645 (1993).

    'Immuno-electron microscopy of influenza haemagglutinin (HA1 and HA2) and M2 protein molecules and their intracellular transport. ' () 3 Am J Trop Med Hyg : S645.

    • Search Google Scholar
  • Čon;iampor, F., Závodská, E., Cmarko, D., Cmarková, J., Varečon;ková, E.: Effects of brefeldin A on the expression and transport of influenza A virus haemagglutinin, M1 and M2 proteins within the cell. Acta Virol 41, 83-91 (1997).

    'Effects of brefeldin A on the expression and transport of influenza A virus haemagglutinin, M1 and M2 proteins within the cell. ' () 41 Acta Virol : 83 -91.

    • Search Google Scholar
  • Appleyard, G.: Amantadine-resistance as a genetic marker for influenza viruses. J Gen Virol 36, 249-255 (1977).

    'Amantadine-resistance as a genetic marker for influenza viruses. ' () 36 J Gen Virol : 249 -255.

    • Search Google Scholar
  • Betaková, T., Nermut, M. V., Hay, A. J.: The NB protein is an integral component of the membrane of influenza B virus. J Gen Virol 77, 2689-2694 (1966).

    'The NB protein is an integral component of the membrane of influenza B virus. ' () 77 J Gen Virol : 2689 -2694.

    • Search Google Scholar
  • Sunstrom, N, A., Premkumar, L. S., Premkumar, A., Ewart, G., Cox, G. B., Gage, P. W.: Ion channels formed by NB, an influenza B virus protein. J Membr Biol 150, 127-132 (1996).

    'Ion channels formed by NB, an influenza B virus protein. ' () 150 J Membr Biol : 127 -132.

    • Search Google Scholar
  • Pekosz, A., Lamb, R. A.: The CM2 protein of influenza C virus is an oligomeric integral membrane glycoprotein structurally analogous to influenza A virus M2 and influenza B virus NB proteins. Virology 237, 439-451 (1997).

    'The CM2 protein of influenza C virus is an oligomeric integral membrane glycoprotein structurally analogous to influenza A virus M2 and influenza B virus NB proteins. ' () 237 Virology : 439 -451.

    • Search Google Scholar
  • Van Kuppeveld, F. J. M., Hornderop, J. G. J., Smeets, R. L. L., Willems, P. H. G. M., Dijkman, H. B. P. M., Galama, J. M. D., Melchers, W. J. G.: Coxackievirus protein 2B modifies endoplasmic reticulum membrane and plasma membrane permeability and facilitates virus release. EMBO J 16, 3519-3532 (1997).

    'Coxackievirus protein 2B modifies endoplasmic reticulum membrane and plasma membrane permeability and facilitates virus release. ' () 16 EMBO J : 3519 -3532.

    • Search Google Scholar
  • Carrasco, L., Pérez, L., Irurzun, A., Lama, J., Martinéz-Abarca, F., Rodriguez, P., Guinea, R., Castrillo, J. L., Sanz, M. A., Ayala, J.: Modification of membrane permeability by animal viruses. In: Carrasco, L. et al. (eds): Regulation of gene expression in animal viruses. Plenum Press, New York, 1993, 283-303.

    Regulation of gene expression in animal viruses. , () 283 -303.

  • Carrasco, L.: Modification of membrane permeability by animal viruses. Adv Virus Res 45, 61-112 (1995).

    'Modification of membrane permeability by animal viruses. ' () 45 Adv Virus Res : 61 -112.

    • Search Google Scholar
  • Sugrue, R. J., Hay, A. J.: Structural characteristics of the M2 protein of influenza A viruses: evidence that it forms a tetrameric channel. Virology 180, 617-624 (1991).

    'Structural characteristics of the M2 protein of influenza A viruses: evidence that it forms a tetrameric channel. ' () 180 Virology : 617 -624.

    • Search Google Scholar
  • Čon;iampor, F., Cmarko, D., Cmarková, J., Závodská, E.: Influenza virus M2 protein and haemagglutinin conformation changes during intracellular transport. Acta Virol 39, 171-181 (1995).

    'Influenza virus M2 protein and haemagglutinin conformation changes during intracellular transport. ' () 39 Acta Virol : 171 -181.

    • Search Google Scholar
  • Pinto, L. H., Dieckmann, G. R., Gandhi, C. S., Papworth, C. G., Braman, J., Shaughnessy, M. A., Lear, J. D., Lamb, R. A., DeGrado, W. F.: A functionally defined model for the M2 proton channel of influenza A virus suggests a mechanism for its ion selectivity. Proc Natl Acad Sci USA 94, 11301-11306 (1997).

    'A functionally defined model for the M2 proton channel of influenza A virus suggests a mechanism for its ion selectivity. ' () 94 Proc Natl Acad Sci USA : 11301 -11306.

    • Search Google Scholar
  • Čon;iampor, F., Bayley, P. M., Nermut, M. V., Hirst, E. M. A., Sugrue, R. J., Hay, A. J.: 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 88, 14-24 (1992a).

    '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. ' () 88 Virology : 14 -24.

    • Search Google Scholar
  • Sansom, M. S. P., Kerr, I. D., Smith, G. R., Son, H. S.: The influenza A virus M2 channel: a molecular modeling and simulation study. Virology 233, 163-173 (1997).

    'The influenza A virus M2 channel: a molecular modeling and simulation study. ' () 233 Virology : 163 -173.

    • Search Google Scholar
  • Grice, A. L., Kerr, I. D., Sansom, M. S. P.: Ion channels formed by HIV-1 Vpu: a modeling and simulation study. FEBS Letters 405, 299-304 (1997).

    'Ion channels formed by HIV-1 Vpu: a modeling and simulation study. ' () 405 FEBS Letters : 299 -304.

    • Search Google Scholar
  • Ewart, G. D., Sutherland, T., Gage, P. W., Cox, G. B.: The Vpu protein of human immuno-deficiency virus type 1 forms cation-selective ion channels. J Virol 70, 7108-7115 (1996).

    'The Vpu protein of human immuno-deficiency virus type 1 forms cation-selective ion channels. ' () 70 J Virol : 7108 -7115.

    • Search Google Scholar
  • Tian, P., Yanfang, H., Schilling, W. P., Lindsay, D. A., Estes, M. K.: Rotavirus NSP4 affects intracellular calcium levels. J Virol 68, 251-257 (1994).

    'Rotavirus NSP4 affects intracellular calcium levels. ' () 68 J Virol : 251 -257.

  • Newton, K., Meyer, J. C., Bellamy, R., Taylor, J. A.: Rotavirus nonstructural glycoprotein NSP4 alters plasma membrane permeability in mammalian cells. J Virol 71, 9458-9465 (1997).

    'Rotavirus nonstructural glycoprotein NSP4 alters plasma membrane permeability in mammalian cells. ' () 71 J Virol : 9458 -9465.

    • Search Google Scholar
  • Hille, B.: Ion channels, all in one place. Cell 69, 579-580 (1992).

    'Ion channels, all in one place. ' () 69 Cell : 579 -580.

Monthly Content Usage

Abstract Views Full Text Views PDF Downloads
Sep 2020 3 0 0
Oct 2020 1 0 0
Nov 2020 9 0 0
Dec 2020 3 0 0
Jan 2021 0 0 0
Feb 2021 2 0 0
Mar 2021 0 0 0