Author(s): Irena Cosic, Drasko Cosic, Ivan Loncarevic
Download Full PDF
Read Complete Article
Volume 10 - Mar 2021
With newly discovered UK variant of SARS-CoV-2 virus, which has been shown to be about 70% more infectious and possibly 30% more deadly, there is a need to understand why mutations within this variant are so critical. Here, we have applied the Resonant Recognition Model (RRM) to computationally analyse six the most critical mutations within this UK variant and we have found that these mutations are significantly increasing RRM characteristics related to its viral activity. To test the approach, we have also applied the RRM to three the most critical mutations within the South African variant of SARS-CoV-2 virus and found that those mutations are increasing RRM characteristics related to viral activity, but not as much as UK variant. This is in complete agreement with known viral activities of these SARS-CoV-2 variants. Using the same approach, we have applied the RRM model to predict possible even more critical mutations, which probably have not yet occurred, but may lead to even more virulent mutants of SARS-CoV-2 virus. Both UK variant mutations, as well as RRM predicted mutations, have been presented within 3D structure of spike protein during the interaction with ACE2 receptor. It has been shown that all these mutations are in close proximity of interaction site between spike protein and ACE2 receptor.
UK Variant of SARS-CoV-2, South African Variant of SARS-CoV-2, Prediction of Functional Mutations, Resonant Recognition Model, COVID-19
- World Health Organisation: SARS-CoV-2 Variant – United Kingdom of Great Britain and Northern Ireland. Disease Outbreak News, 21 December 2020.
- World Health Organisation: Statement of WHO Working Group on COVID-19 Animal Models (WHO-COM) About UK and South African SARS-CoV-2 New Variants, 22 December 2020.
- Cosic I: Macromolecular Bioactivity: Is it Resonant Interaction between Macromolecules? -Theory and Applications. IEEE Trans on Biomedical Engineering, 1994; 41, 1101-1114.
- Cosic I: The Resonant Recognition Model of Macromolecular Bioactivity: Theory and Applications. Basel: Birkhauser Verlag, 1997.
- Cosic I: Resonant Recognition Model of Protein-Protein and Protein-DNA Recognition, in Bioinstrumentation and Biosensors. Marcel Dekker Inc New York, 1990; 475-510.
- Cosic I, Nesic D: Prediction of "Hot Spots" in SV40 Enhancer and Relation with Experimental Data. Eur. J. Biochem., 1988; 170, 247-252.
- Cosic I, Hearn MTW: “Hot Spot" Amino Acid Distribution in Ha-ras Oncogene Product p21: Relationship to Guanine Binding Site. J. Molecular Recognition, 1991; 4, 57-62.
- Cosic I, Hearn MTW: Studies on Protein-DNA Interactions Using the Resonant Recognition Model: Application to Repressors and Transforming Proteins. Eur. J. Biochem, 1992; 205, 613-619.
- Cosic I, Hodder AN, Aguilar MI, Hearn MTW: Resonant Recognition Model and protein topography: model studies with myoglobin, haemoglobin and lysozyme. Eur. J. Biochem, 1991; 198, 113-119.
- 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.
- Cosic I, Cosic D, Lazar K: Cancer Related BRCA-1 and BRCA-2 Mutations as Analysed by the Resonant Recognition Model. Journal of Advances in Molecular Biology, 2017; 1(2), doi: 10.22606/jamb.2017.12003.
- 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.
- Cosic I, Paspaliaris V, Cosic D: Analysis of Protein-Receptor on an Example of Leptin-Leptin Receptor Interaction Using the Resonant Recognition Model. Appl. Sci., 2019; 9, 5169, doi: 10.3390/app9235169.
- 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.
- Lan J, Ge J, Yu J, Shan S, Zhou H, Fan S, Zhang Q, Shi X, Wang Q, Zhang L, Wang X: Structure of SARS-CoV-2 Spike Receptor-Binding Domain Bound to ACE2 Receptor. Nature, 2020; doi: 10.1038/s41586-020-2180-5.
- Schmier S, Mostafa A, Haarmann T, Bannert N, Ziebuhr J, Veljkovic V, Dietrich U, Pleschka S: In silico prediction and experimental confirmation of HA residues conferring enhanced human receptor specificity of H5N1 influenza A viruses. Scientific Reports, 2015; 5, doi: 10.1038/srep11434.
- 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.
- 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.
- 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.
- Li F: Receptor recognition and cross-species infections of SARS coronavirus. Antiviral Research, 2013; 100(1), 246–54, doi: 10.1016/j.antiviral.2013.08.014.
- Xu X, Chen P, Wang J, Feng J, Zhou H, Li X et al.: Evolution of the novel coronavirus from the ongoing Wuhan outbreak and modeling of its spike protein for risk of human transmission. Science China. Life Sciences, 2020; 63 (3), 457–460, doi: 10.1007/s11427-020-1637-5.
- Millet JK: Whittaker G.R. Physiological and molecular triggers for SARS-CoV membrane fusion and entry into host cells. Virology, 2018; 517, 3–8. doi: 10.1016/j.virol.2017.12.015.
- 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.
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.