Antiviral Activity of Binase against the Pandemic Influenza A (H1N1) Virus

Cover Page

Cite item

Abstract

The lack of effective antiviral drugs restricts the control of the dangerous RNA-containing influenza A (H1N1) virus. Extracellular ribonuclease of Bacilli (binase) was shown to manifest antiviral activity during single- and multi-cycle viral replication in the range of concentrations non-toxic to epithelial cells and 0.01-0.1 multiplicity of infection. During antiviral treatment for 15-30 min, the concentration of 1 μg/ml binase reduced the amount of focus-forming units of viruses by a factor of 3-10 and suppressed the virus-induced cytopathic effect in A549 human lung cells. The possible mechanisms of interaction between the virus and enzyme are discussed. Positive charges in both binase and viral hemagglutinin cause electrostatic interaction with negatively charged sialic acid on the host cell’s surface followed by its penetration into the cell. Capsid elimination and release of viral RNA from endosome to the cytoplasm allows catalytic RNA cleavage by internalized binase. The data obtained confirm that binase is an effective antiviral agent against the pandemic influenza A (H1N1) virus. Certain progress in this field is associated with clarifying the detailed mechanism underlying the antiviral action of binase and development of the most effective way for its practical use.

Full Text

Antiviral Activity of Binase against the Pandemic Influenza A (H1N1) Virus

×

About the authors

R. Shah Mahmud

Institute of Fundamental Medicine and Biology, Kazan (Volga Region) Federal University

Author for correspondence.
Email: raihan.shah@gmail.com
Russian Federation

O. N. Ilinskaya

Institute of Fundamental Medicine and Biology, Kazan (Volga Region) Federal University

Email: raihan.shah@gmail.com
Russian Federation

References

  1. Makarov A.A., Ilinskaya O.N. // FEBS Lett. 2003, V.540, №1-3, P.15-20
  2. Makarov A.A., Kolchinsky A., Ilinskaya O.N. // Bioessays. 2008, V.30, №8, P.781-790
  3. Ardelt W., Ardelt B., Darzynkiewicz Z. // Eur. J. Pharmacol. 2009, V.625, №1-3, P.181-189
  4. Youle R.J., Wu Y.N., Mikulski S.M., Shogen K., Hamilton R.S., Newton D., D’Alessio G., Gravell M. // Proc. Natl. Acad. Sci. 1994, V.91, №13, P.6012-6016
  5. Gribencha S.V., Potselueva L.A., Barinskij I.F., Balandin T.G., Deev S.M., Leshchinskaia I.B. // Vopr. Virusol. 2004, V.49, №6, P.38-41
  6. Sharipova M.R., Toimentseva A.A., Sabirova A.R., Mukhametzianova A.D., Akhmetova A.I., Mardanova A.M., Balaban N.P. // Mikrobiologiia. 2011, V.80, №3, P.424-426
  7. Leland P.A., Raines R.T. // Chem. Biol. 2001, V.8, №5, P.405-413
  8. Gribencha S.V., Potselueva L.A., Barinskii I.F., Deev S.M., Balandin T.G., Leshchinskaia I.B. // Vopr. Virusol. 2006, V.51, №5, P.41-43
  9. Ilinskaya O.N., Zelenikhin P.V., Petrushanko I.Y., Mitkevich V.A., Prassolov V.S., Makarov A.A. // Biochem. Biophys. Res. Commun. 2007, V.361, №4, P.1000-1005
  10. Schneider M.A., Shtil’bans E.B., Kuprianov-Ashin E.G., Potselueva L.A., Zaikonnikova I.V., Kurinenko B.M. // Antibiot. Khimioter. 1990, V.35, №3, P.27-31
  11. Schulga A., Kurbanov F., Kirpichnikov M., Protasevich I., Lobachev V., Ranjbar B., Chekhov V., Polyakov K., Engelborghs Y., Makarov A. // Protein Eng. 1998, V.11, №9, P.775-782
  12. Yakovlev G.I., Moiseyev G.P., Struminskaya N.K., Borzykh O.A., Kipenskaya L.V., Znamenskaya L.V., Leschinskaya I.B., Chernokalskaya E.B., Hartley R.W. // FEBS Lett. 1994, V.354, №3, P.305-306
  13. Ilinskaya O.N., Karamova N.S., Ivanchenko O.B., Kipenskaya L.V. // Mutat. Res. 1996, V.354, №2, P.203-209
  14. Mosmann T. // J. Immunol. Methods. 1983, V.65, №1-2, P.55-63
  15. Anfinsen C.B., Redfield R.R., Choate W.I., Page J., Carrol W.R. // J. Biol. Chem. 1954, V.207, P.201-210
  16. Wegmann T.G., Smithies O., Transfusion. I.O. // Transfusion 1966, V.6, №1, P.67-73
  17. Pleschka S., Stein M., Schoop R., Hudson J.B. // Virology Journal 2009, V.6, №197
  18. Payne A.F., Binduga-Gajewska I., Kauffman E.B., Kramer L.D. // J. Virol. Meth. 2006, V.134, №1-2, P.183-189
  19. Cabrera-Fuentes H.A., Zelenikhin P.V., Kolpakov A.I., Ilinskaya O.N. // J. CTTE . 2012, V.7, №3, P.72-76
  20. Cabrera-Fuentes H.A., Zelenikhin P.V., Kolpakov A.I., Preissner K.T., Ilinskaya O.N. // Proceedings of Kazan State University. Science series. 2010, V.152, №1, P.121-126
  21. Rosenberg H.F., Domachowske J.B. // J. Leukoc. Biol. 2001, V.70, №5, P.691-698
  22. Rosenberg H.F., Domachowske J.B. // Curr. Pharm. Biotechnol. 2008, V.9, №3, P.135-140
  23. Liang S.L., Quirk D., Zhou A. // IUBMB Life. 2006, V.58, №9, P.508-514
  24. Domachowske J.B., Dyer K.D., Adams A.G., Leto T.L., Rosenberg H.F. // Nucleic Acids Res. 1998, V.26, №14, P.3358-3363
  25. Saxena S.K., Gravell M., Wu Y.N., Mikulski S.M., Shogen K., Ardelt W., Youle R.J. // J. Biol. Chem. 1996, V.271, №34, P.20783-20788
  26. Lee Y.H., Wei C.W., Wang J.J., Chiou C.T. // Antiviral Res. 2011, V.89, №3, P.193-198
  27. Cabrera-Fuentes H.A., Zelenikhin P.V., Kolpakov A.I., Preissner K., Ilinskaya O.N. // Comparative toxicity of binase towards tumor and normal cell. (doi 10.1016/j. toxicon.2013.03.015). // Toxicon. 2013
  28. Mitkevich V.A., Tchurikov N.A., Zelenikhin P.V., Petrushanko I.Y., Makarov A.A., Ilinskaya O.N. // FEBS J. 2010, V.277, P.186-196
  29. Arinaminpathy N., Grenfell B. // (doi: 10.1371/journal.pone.0015674). // PLoS One. 2010, V.5, №12, P.e15674
  30. Kobayashi Y., Suzuki Y. // (doi: 10.1371/journal.pone.0040422). // PLoS One. 2012, V.7, №7, P.e40422
  31. Ulyanova V., Vershinina V., Ilinskaya O. // FEBS J. 2011, V.278, №19, P.3633-3643
  32. Alekseeva I.I., Kurinenko B.M., Kleiner G.I., Skuia A.Zh., Penzikova G.A. // Antibiotiki. 1981, V.26, №7, P.527-532

Supplementary files

Supplementary Files
Action
1. JATS XML

Copyright (c) 2013 Shah Mahmud R., Ilinskaya O.N.

Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 International License.

This website uses cookies

You consent to our cookies if you continue to use our website.

About Cookies