Possibility to Interfere with Coronavirus RNA Replication Analyzed by Resonant Recognition Model

Possibility to Interfere with Coronavirus RNA Replication Analyzed by Resonant Recognition Model

Loading document ...
Loading page ...


Author(s): Irena Cosic, Drasko Cosic, Ivan Loncarevic

Download Full PDF Read Complete Article

DOI: 10.18483/ijSci.2482 78 527 22-28 Volume 10 - Jun 2021


To be able to design vaccine or even a cure for COVID-19, it is particularly important to understand how SARS-CoV-2, as a single stranded RNA virus, is multiplied within host cells and which factors are controlling this multiplication. Here, we have analyzed the process of coronavirus RNA replication within host cell with the aim to find out the characteristics of this process. For that purpose, we have utilized the Resonant Recognition Model (RRM), which is biophysical model capable of identifying parameters (frequencies) related to specific macromolecular (protein, DNA, RNA) functions and/or interactions. The RRM model is unique with its capability to directly analyze interactions between amino acid macromolecules (proteins) and nucleotide macromolecules (DNA, RNA). Using the RRM model, we have identified parameters that characterize two steps in coronavirus RNA replication i.e., initiation of replication and replication by itself. These parameters can be used in our future research to design peptides, that will be able to interfere with either or both of those processes.


COVID-19, SARS-CoV-2, Coronavirus, Coronavirus RNA Replication, Resonant Recognition Model


  1. Wu F, Zhao S, Yu B, Chen YM, Wang W, Song ZG, Hu Y, Tao ZW, Tian JH, Pei YY, Yuan ML, Zhang YL, Dai FH, Liu Y, Wang QM, Zheng JJ, Xu L, Holmes EC, Zhang YZ: A new coronavirus associated with human respiratory disease in China. Nature, 2020 Feb 3; doi: 10.1038/s41586-020-2008-3.
  2. Makin S: How Coronaviruses Cause Infection from Colds to Deadly Pneumonia. Scientific American 2020 Feb 5.
  3. Simmons G, Zmora P, Gierer S, Heurich A, Pöhlmann S: Proteolytic activation of the SARS-coronavirus spike protein: cutting enzymes at the cutting edge of antiviral research. Antiviral Research, 2013; 100(3), 605–614, doi: 10.1016/j.antiviral.2013.09.028.
  4. Fehr AR, Perlman S: Coronaviruses: an overview of their replication and pathogenesis. Methods in Molecular Biology Springer, 2015; 1282, 1–23, doi: 10.1007/978-1-4939-2438-7_1.
  5. Baralle E, Brownlee GG: AUG is the Only Recognisable Signal Sequence in the 5′ Non-coding Regions of Eukaryotic mRNA. Nature, 1978; 274, 84–87.
  6. Cenik ES, Zamore PD: Argonaute proteins. Current Biology, 2011; 21(12), 446-449, doi: 10.1016/j.cub.2011.05.020.
  7. Ender C, Meister G: Argonaute Proteins at a Glance. Journal of Cell Science, 2010; 123, 1819-1823, doi: 10.1242/jcs.055210.
  8. Adiliaghdam F, Basavappa M, Saunders TL, Harjanto D, Prior JT, Cronkite DA, Papavasiliou N, Jeffrey KL: A Requirement for Argonaute 4 in Mammalian Antiviral Defense. Cell Reports Volume, 2020; 30(6), 1661-2054, doi: 10.1016/j.celrep.2020.01.021.
  9. Hansen JL, Long AM, Schultz SC: Structure of the RNA-dependent RNA polymerase of poliovirus. Structure, 1997; 5(8), 1109–1122, doi: 10.1016/S0969-2126(97)00261-X.
  10. Ahlquist P: RNA-dependent RNA Polymerases, Viruses, and RNA Silencing. Science, 2002; 296(5571), 1270–1273, doi: 10.1126/science.1069132.
  11. Ziebuhr J: The Coronavirus Replicase. Corona Replication and Reverse Genetics, Nature Publishing Group, 2005; 287, 57-94.
  12. Yuan M, Liu H, Wu NC, Lee CCD, Zhu X, Zhao F, Huang D, Yu W, Hua Y, Tien H, Rogers TF, Landais E, Sok D, Jardine JG, Burton DR, Wilson IA: Structural basis of a public antibody response to SARS-CoV-2. Science, 2020; 1-11, doi: 10.1126/science.abd.2321(2020).
  13. Cosic I: Macromolecular Bioactivity: Is it Resonant Interaction between Macromolecules? -Theory and Applications. IEEE Trans on Biomedical Engineering, 1994; 41, 1101-1114.
  14. Cosic I: Virtual spectroscopy for fun and profit. Biotechnology, 1995; 13, 236-238.
  15. Cosic I: The Resonant Recognition Model of Macromolecular Bioactivity: Theory and Applications. Basel: Birkhauser Verlag, 1997.
  16. Cosic I: Resonant Recognition Model of Protein Protein and Protein DNA Recognition, in Bioinstrumentation and Biosensors. ed by Wise D. Marcel Dekker Inc., New York, 1990; 475-510.
  17. Cosic I, Cosic D: Macromolecular Resonances. In: Bandyopadhyay A., Ray K. (eds) Rhythmic Oscillations in Proteins to Human Cognition. Studies in Rhythm Engineering. Springer, Singapore, 2021; 1, 11-45, doi: 10.1007/978-981-15-7253-1_1.
  18. Cosic I, Cosic D, Lazar K: Analysis of Tumor Necrosis Factor Function Using the Resonant Recognition Model. Cell Biochemistry and Biophysics, 2015; doi: 10.1007/s12013-015-0716-3.
  19. Cosic I, Paspaliaris V, Cosic D: Analysis of Protein-Receptor on an Example of Leptin-Leptin Receptor Interaction Using the Resonant Recognition Model. MDPI Appl. Sci., 2019; 9, 5169, doi:10.3390/app9235169.
  20. Cosic I, Cosic D, Loncarevic I: RRM Prediction of Erythrocyte Band3 Protein as Alternative Receptor for SARS-CoV-2. MDPI Appl. Sci., 2020; 10, 4053, doi: 10.3390/app10114053.
  21. Cosic I, Lazar K, Cosic D: Cellular Ageing - Telomere, Telomerase and Progerin analysed using Resonant Recognition Model. MD-Medical Data, 2014; 6(3), 205-209.
  22. Cosic I, Cosic D, Lazar K: Is it possible to predict electromagnetic resonances in proteins, DNA and RNA?. Nonlinear Biomedical Physics, 2015; 3, doi: 10.1140/s40366-015-0020-6.
  23. Cosic I, Cosic D, Loncarevic I: New Concept of Small Molecules Interaction with Proteins – An Application to Potential COVID-19 Drugs. International Journal of Sciences, 2020; 9(9), 16-25, doi: 10.18483/ijSci.2390.
  24. Cosic I, Cosic D, Loncarevic I: Analysis of Ivermectin as Potential Inhibitor of SARS-CoV-2 Using Resonant Recognition Model. International Journal of Sciences, 2021; 10(1), 1-6, doi: 10.18483/ijSci.2433.
  25. Cosic I, Drummond AE, Underwood JR, Hearn MTW: In vitro inhibition of the actions of basic FGF by novel 16 amino acid peptides. Molecular and Cellular Biochemistry, 1994; 130, 1-9.
  26. Krsmanovic V, Biquard JM, Sikorska-Walker M, Cosic I, Desgranges C, Trabaud MA, Whitfield JF, Durkin JP, Achour A, Hearn MT: Investigation Into the Cross-reactivity of Rabbit Antibodies Raised against Nonhomologous Pairs of Synthetic Peptides Derived from HIV-1 gp120 proteins. J.Peptide Res, 1998; 52(5), 410-412.
  27. Hearn MTW, Biquard JM, Cosic I, Krsmanovic V: Peptides Immunologically related to proteins expressed by a viral agent, having a sequence of amino acids ordered by means of protein informational method. US Patent 6, 294, 174 2001.
  28. Achour A, Biquard JM, Krsmanovic V, M’Bika JP, Ficheux D, Sikorska M, Cozzone AJ: Induction of Human Immunodeficiency Virus (HIV-1) Envelope Specific Cell-Mediated Immunity by a Non-Homologus Synthetic Peptide. PLoS ONE, 2007; 11, 1-12, doi: 10.1371/journal.pone.0001214.
  29. Almansour N, Pirogova E, Coloe P, Cosic I Istivan T: Investigation of cytotoxicity of negative control peptides versus bioactive peptides on skin cancer and normal cells: a comparative study. Future Medicinal Chemistry, 2012; 4(12), 1553-1565.
  30. Istivan T, Pirogova E, Gan E, Almansour N, Coloe P, Cosic I: Biological effects of a De Novo designed myxoma virus peptide analogue: Evaluation of cytotoxicity on tumor cells. Public Library of Science (PLoS) ONE, 2011; 6(9), 1-10.

Cite this Article:

International Journal of Sciences is Open Access Journal.
This article is licensed under a Creative Commons Attribution 4.0 International (CC BY 4.0) License.
Author(s) retain the copyrights of this article, though, publication rights are with Alkhaer Publications.

Search Articles

Issue June 2023

Volume 12, June 2023

Table of Contents

World-wide Delivery is FREE

Share this Issue with Friends:

Submit your Paper