Research article

The role of electric charge in SARS-CoV-2 and other viral infections

  • Received: 02 February 2024 Revised: 07 May 2024 Accepted: 14 May 2024 Published: 23 May 2024
  • This study analyzed the role of electric charge in human viral infections. Examples of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), dengue, Ebola, influenza A, and respiratory syncytial virus (RSV) are presented. Charge distribution in SARS-CoV-2 and electrostatic interactions of SARS-CoV-2 with its receptor, angiotensin-converting enzyme 2 (ACE2), were evaluated, and the mean time required for respired SARS-CoV-2 virus attachment was evaluated. The virus–cell attachment modality of all of the above viruses was calculated. The impact of electric charge on other viral-related processes, such as replication of virion material, release, and immune response, was also discussed. Special charge conditions in virus treatments were also indicated.

    Citation: Piotr H. Pawłowski, Piotr Zielenkiewicz. The role of electric charge in SARS-CoV-2 and other viral infections[J]. AIMS Biophysics, 2024, 11(2): 166-188. doi: 10.3934/biophy.2024011

    Related Papers:

  • This study analyzed the role of electric charge in human viral infections. Examples of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), dengue, Ebola, influenza A, and respiratory syncytial virus (RSV) are presented. Charge distribution in SARS-CoV-2 and electrostatic interactions of SARS-CoV-2 with its receptor, angiotensin-converting enzyme 2 (ACE2), were evaluated, and the mean time required for respired SARS-CoV-2 virus attachment was evaluated. The virus–cell attachment modality of all of the above viruses was calculated. The impact of electric charge on other viral-related processes, such as replication of virion material, release, and immune response, was also discussed. Special charge conditions in virus treatments were also indicated.



    加载中


    Conflict of interest



    The authors declare that there are no conflicts of interest.

    Author contributions



    PH Pawłowski: Conceived and designed the theoretical models, analyzed data, and drafted the manuscript. P Zielenkiewicz: Critical feedback, data analysis, and revised the manuscript.

    [1] Viral Infections. Physiopedia (2022) . Available from: http:///index.php?title=Viral_Infections&oldid=290753
    [2] Betts MJ, Russell RB (2003) Amino acid properties and consequences of subsitutions. Bioinformatics for Geneticists.Wiley 289-316. https://doi.org/10.1002/0470867302.ch14
    [3] Lipfert J, Doniach S, Das R, et al. (2014) Understanding nucleic acid-ion interactions. Annu Rev Biochem 83: 813-841. https://doi.org/10.1146/annurev-biochem-060409-092720
    [4] Ma Y, Poole K, Goyette J, et al. (2017) Introducing membrane charge and membrane potential to T cell signaling. Front Immunol 8: 1513. https://doi.org/10.3389/fimmu.2017.01513
    [5] Zhao X, Ma X, Dupius JH, et al. (2022) Negatively charged phospholipids accelerate the membrane fusion activity of the plant-specific insert domain of an aspartic protease. J Biol Chem 298: 101430. https://doi.org/10.1016/j.jbc.2021.101430
    [6] Cruz-Chu ER, Malafeev A, Pajarskas T, et al. (2014) Structure and response to flow of the glycocalyx layer. Biophys J 106: 232-242. https://doi.org/10.1016/j.bpj.2013.09.060
    [7] Debye P, Hückel E (1923) The theory of electrolytes. I. Lowering of freezing point and related phenomena (PDF). Physikalische Zeitschrift 24: 185-206.
    [8] Michen B, Graule T (2010) Isoelectric points of viruses. J Appl Microbiol 109: 388-397. https://doi.org/10.1111/j.1365-2672.2010.04663.x
    [9] Heffron J, Mayer BK (2021) Virus isoelectric point estimation: theories and methods. J Appl Environ Microb 87: e02319-e02320. https://doi.org/10.1128/AEM.02319-20
    [10] Luisetto M, Tarro G, Edbey K, et al. (2021) Coronavirus COVID-19 surface properties: electrical charges status. Int J Clin Microbiol Biochem Technol 4: 016-027. https://doi.org/10.12688/f1000research.108667.2
    [11] Cavezzi A, Menicagli R, Troiani E, et al. (2022) COVID-19, cation dysmetabolism, sialic acid, CD147, ACE2, viroporins, hepcidin and ferroptosis: a possible unifying hypothesis. F1000Res 11: 102. https://doi.org/10.12688/f1000research.108667.2
    [12] Northwestern University.“Research exposes new vulnerability for SARS-CoV-2: Electrostatic interactions enhance the spike protein's bond to host cells.”. ScienceDaily (2020) . Available from: https://www.sciencedaily.com/releases/2020/08/200811120227.htm
    [13] Leung WWF, Sun Q (2020) Electrostatic charged nanofiber filter for filtering airborne novel coronavirus (COVID-19) and nano-aerosols. Sep Purif Technol 250: 116886. https://doi.org/10.1016/j.seppur.2020.116886
    [14] Corrêa Giron C, Laaksonen A, Barroso da Silva FL (2020) On the interactions of the receptor-binding domain of SARS-CoV-1 and SARS-CoV-2 spike proteins with monoclonal antibodies and the receptor ACE2. Virus Res 285: 198021. https://doi.org/10.1016/j.virusres.2020.198021
    [15] Chavda VP, Bezbaruah R, Deka K, et al. (2022) The delta and omicron variants of SARS-CoV-2: What we know so far. Vaccines 10: 1926. https://doi.org/10.3390/vaccines10111926
    [16] Carabelli AM, Peacock TP, Thorne LG, et al. (2023) SARS-CoV-2 variant biology: immune escape, transmission and fitness. Nat Rev Microbiol 21: 162-177. https://doi.org/10.1038/s41579-022-00841-7
    [17] Chavda VP, Patel AB, Vaghasiya DD (2022) SARS-CoV-2 variants and vulnerability at the global level. J Med Virol 94: 2986-3005. https://doi.org/10.1002/jmv.27717
    [18] Chavda VP, Ghali ENHK, Yallapu MM, et al. (2022) Therapeutics to tackle Omicron outbreak. Immunotherapy 14: 833-838. https://doi.org/10.2217/imt-2022-0064
    [19] Chavda VP, Vuppu S, Mishra T, et al. (2022) Recent review of COVID-19 management: diagnosis, treatment and vaccination. Pharmacol Rep 74: 1120-1148. https://doi.org/10.1007/s43440-022-00425-5
    [20] Polatoğlu I, Oncu-Oner T, Dalman I, et al. (2023) COVID-19 in early 2023: Structure, replication mechanism, variants of SARS-CoV-2, diagnostic tests, and vaccine & drug development studies. MedComm 4: e228. https://doi.org/10.1002/mco2.228
    [21] Basu D, Chavda VP, Mehta AA (2022) Therapeutics for COVID-19 and post COVID-19 complications: an update. Curr Res Pharmacol Drug Discov 3: 100086. https://doi.org/10.1016/j.crphar.2022.100086
    [22] Lancet T (2023) The COVID-19 pandemic in 2023: far from over. Lancet 401: 79. https://doi.org/10.1016/s0140-6736(23)00050-8
    [23] Arbeitman CR, Rojas P, Ojeda-May P, et al. (2021) The SARS-CoV-2 spike protein is vulnerable to moderate electric fields. Nat Commun 12: 5407. https://doi.org/10.1038/s41467-021-25478-7
    [24] Božič A, Podgornik R (2024) Changes in total charge on spike protein of SARS-CoV-2 in emerging lineages. Bioinformatics Adv 4: vbae053. https://doi.org/10.1093/bioadv/vbae053
    [25] Javidpour L, Božič A, Naji A, et al. (2020) Electrostatic interaction between SARS-CoV-2 virus and charged electret fibre. Soft Matter 17: 4296-4303. https://doi.org/10.1039/D1SM00232E
    [26] Zhang Z, Zhang J, Wang J (2022) Surface charge changes in spike RBD mutations of SARS-CoV-2 and its variant strains alter the virus evasiveness via HSPGs: a review and mechanistic hypothesis. Front Public Health 10: 952916. https://doi.org/10.3389/fpubh.2022.952916
    [27] Bar-On YM, Flamholz A, Phillips R, et al. (2020) SARS-CoV-2 (COVID-19) by the numbers. elife 9: e57309. https://doi.org/10.7554/eLife.57309
    [28] Berman HM, Westbrook J, Feng Z, et al. (2000) The protein data bank. Nucleic Acids Res 28: 235-242. https://doi.org/10.1093/nar/28.1.235
    [29] Sayers EW, Bolton EE, Brister JR, et al. (2022) Database resources of the national center for biotechnology information. Nucleic Acids Res 50: D20-D26. https://doi.org/10.1093/nar/gkab1112
    [30] Jiao LG, Zan LR, Zhu L, et al. (2019) Accurate computation of screened Coulomb potential integrals in numerical Hartree–Fock programs. Comput Phys Commun 244: 217-227. https://doi.org/10.1016/j.cpc.2019.06.001
    [31] SARS-CoV-2 variants of concern and variants under investigation in England Technical briefing 15. Public Health England (2021) . Available from: https://assets.publishing.service.gov.uk/government/uploads/system/uploads/attachment_data/file/993879/Variants_of_Concern_VOC_Technical_Briefing_15.pdf
    [32] SARS-CoV-2 variants of concern and variants under investigation in England Technical briefing 23. Public Health England, PHE2 (2021) . Available from: https://assets.publishing.service.gov.uk/government/uploads/system/uploads/attachment_data/file/1018547/Technical_Briefing_23_21_09_16.pdf
    [33] Adamczyk Z, Batys P, Barbasz J (2021) SARS-CoV-2 virion physicochemical characteristics pertinent to abiotic substrate attachment. Curr Opin Colloid Interface Sci 55: 101466. https://doi.org/10.1016/j.cocis.2021.101466
    [34] Berger O, Edholm O, Jähnig F (1997) Molecular dynamics simulations of a fluid bilayer of dipalmitoylphosphatidylcholine at full hydration, constant pressure, and constant temperature. Biophys J 72: 2002-2013. https://doi.org/10.1016/S0006-3495(97)78845-3
    [35] Krebs F, Scheller C, Grove-Heike K (2021) Isoelectric point determination by imaged CIEF of commercially available SARS-CoV-2 proteins and the hACE2 receptor. Electrophoresis 42: 687-692. https://doi.org/10.1002/elps.202100015
    [36] Pawłowski PH (2021) SARS-CoV-2 variant Omicron (B.1.1.529) is in a rising trend of mutations increasing the positive electric charge in crucial regions of the spike protein S. Acta Biochim Pol 69: 263-264. https://doi.org/10.18388/abp.2020_6072
    [37] Cotten M, Phan M (2022) Evolution to increased positive charge on the viral spike protein may be part of the adaptation of SARS-CoV-2 to human transmission. iScience 26: 106230. https://doi.org/10.1016/j.isci.2023.106230
    [38] Lu Y, Zhao T, Lu M, et al. (2021) The analyses of high infectivity mechanism of SARS-CoV-2 and its variants. COVID 1: 666-673. https://doi.org/10.3390/covid1040054
    [39] Pawłowski PH (2021) Additional positive electric residues in the crucial spike glycoprotein S regions of the new SARS-CoV-2 variants. Infect Drug Resist 14: 5099-5105. https://doi.org/10.2147/IDR.S342068
    [40] Bromage E The risks-know them-avoid them (2020). Available from: https://www.erinbromage.com/post/the-risks-know-them-avoid-them
    [41] Islam MA, Ford Versypt AN (2022) Mathematical modeling of impacts of patient differences on COVID-19 lung fibrosis outcomes. bioRxiv [Preprint] . https://doi.org/10.1101/2022.11.06.515367
    [42] Coulomb CA (1785) Premier mémoire sur l'électricité et le magnétisme" [First dissertation on electricity and magnetism]. Histoire de l'Académie Royale des Sciences [History of the Royal Academy of Sciences] (in French) : 569-577. https://www.academie-sciences.fr/pdf/dossiers/Coulomb/Coulomb_pdf/Mem1785_p569.pdf
    [43] Kobayashi Y, Suzuki Y (2012) Compensatory evolution of net-charge in influenza A virus hemagglutinin. PLoS One 7: e40422. https://doi.org/10.1371/journal.pone.0040422
    [44] Xia S, Liu M, Wang C, et al. (2020) Inhibition of SARS-CoV-2 (previously 2019-nCoV) infection by a highly potent pan-coronavirus fusion inhibitor targeting its spike protein that harbors a high capacity to mediate membrane fusion. Cell Res 30: 343-355. https://doi.org/10.1038/s41422-020-0305-x
    [45] Brunton B, Rogers K, Phillips EK, et al. (2019) TIM-1 serves as a receptor for Ebola virus in vivo, enhancing viremia and pathogenesis. PLoS Negl Trop Dis 13: e0006983. https://doi.org/10.1371/journal.pntd.0006983
    [46] Fahimi H, Allahyari H, Hassan ZM, et al. (2014) Dengue virus type-3 envelope protein domain III; expression and immunogenicity. Iran J Basic Med Sci 11: 836-843.
    [47] Saad-Roy CM, Arinaminpathy N, Wingreen NS, et al. (2020) Implications of localized charge for human influenza A H1N1 hemagglutinin evolution: insights from deep mutational scans. PLoS Comput Biol 16: e1007892. https://doi.org/10.1371/journal.pcbi.1007892
    [48] Feng Z, Xu L, Xie Z (2022) Receptors for respiratory syncytial virus infection and host factors regulating the life cycle of respiratory syncytial virus. Front Cell Infect Microbiol 12: 858629. https://doi.org/10.3389/fcimb.2022.858629
    [49] Petrache HI, Tristram-Nagle S, Gawrisch K, et al. (2004) Structure and fluctuations of charged phosphatidylserine bilayers in the absence of salt. Biophys J 86: 1574-1586. https://doi.org/10.1016/S0006-3495(04)74225-3
    [50] Varki A, Schauer R (2009) Sialic Acids. Essentials of Glycobiology. Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press.
    [51] Lupala CS, Lil X, Lei J, et al. (2021) Computational simulations reveal the binding dynamics between human ACE2 and the receptor binding domain of SARS-CoV-2 spike protein. Quant Biol 9: 61-72. https://doi.org/10.15302/J-QB-020-0231
    [52] Pawłowski PH (2021) Charged amino acids may promote coronavirus SARS-CoV-2 fusion with the host cell. AIMS Biophys 8: 111-121. https://doi.org/10.3934/biophy.2021008
    [53] Romano M, Ruggiero A, Squeglia F, et al. (2020) A structural view of SARS-CoV-2 RNA replication machinery: RNA synthesis, proofreading and final capping. Cells 9: 1267. https://doi.org/10.3390/cells9051267
    [54] Silva JRA, Urban J, Araújo E, et al. (2022) Exploring the catalytic mechanism of the RNA cap modification by nsp16-nsp10 complex of SARS-CoV-2 through a QM/MM approach. Int J Mol Sci 23: 300. https://doi.org/10.3390/ijms23010300
    [55] Kirchdoerfer RN, Ward AB (2019) Structure of the SARS-CoV nsp12 polymerase bound to nsp7 and nsp8 co-factors. Nat Commun 10: 2342. https://doi.org/10.1038/s41467-019-10280-3
    [56] Subissi L, Posthuma CC, Collet A, et al. (2014) One severe acute respiratory syndrome coronavirus protein complex integrates processive RNA polymerase and exonuclease activities. Proc Natl Acad Sc USA 111: E3900-E3909. https://doi.org/10.1073/pnas.1323705111
    [57] Bianchi M, Borsetti A, Ciccozzi M, et al. (2021) SARS-Cov-2 ORF3a: mutability and function. Int J Biol Macromol 15: 820-826. https://doi.org/10.1016/j.ijbiomac.2020.12.142
    [58] Scheller C, Krebs F, Minkner R, et al. (2020) Physicochemical properties of SARS-CoV-2 for drug targeting, virus inactivation and attenuation, vaccine formulation and quality control. Electrophoresis 41: 1137-1151. https://doi.org/10.1002/elps.202000121
    [59] Bohan D, Ert HV, Ruggio N, et al. (2021) Phosphatidylserine receptors enhance SARS-CoV-2 infection. PLoS Pathog 17: e1009743. https://doi.org/10.1371/journal.ppat.1009743
    [60] Alberts B, Johnson A, Lewis J, et al. (2002) Molecular Biology of the Cell. New York: Garland Science.
    [61] Jalloh S, Olejnik J, Berrigan J, et al. (2022) CD169-mediated restrictive SARS-CoV-2 infection of macrophages induces pro-inflammatory responses. PLoS pathogens 18: e1010479. https://doi.org/10.1371/journal.ppat.1010479
    [62] Watanabe Y, Allen JD, Wrapp D, et al. (2020) Site-specific glycan analysis of the SARS-CoV-2 spike. Science 369: 330-333. https://doi.org/10.1126/science.abb9983
    [63] von Glasow R, Sander R (2001) Variation of sea salt aerosol pH with relative humidity. Geophys Res Lett 28: 247-250. https://doi.org/10.1029/2000GL012387
    [64] Field RD, Moelis N, Salzmann J, et al. (2021) Inhaled water and salt suppress respiratory droplet generation and COVID-19 incidence and death on US coastlines. Mol Front J 5.01n02: 17-29. https://doi.org/10.1142/S2529732521400058
    [65] Duran-Meza AL, Villagrana-Escareño MV, Ruiz-García J, et al. (2021) Controlling the surface charge of simple viruses. PLoS One 16: e0255820. https://doi.org/10.1371/journal.pone.0255820
    [66] Vega-Acosta JR, Cadena-Nava RD, Gelbart WM, et al. (2014) Electrophoretic mobilities of a viral capsid, its capsid protein, and their relation to viral assembly. J Phys Chem B 118: 1984-1989. https://doi.org/10.1021/jp407379t
    [67] Bockstahler LE, Kaesberg P (1962) The molecular weight and other biophysical properties of bromegrass mosaic virus. Biophys J 2: 1962. https://doi.org/10.1016/s0006-3495(62)86836-2
    [68] Johnson MW, Wagner GW, Bancroft JB (1973) A titrimetric and electrophoretic study of cowpea chlorotic mottle virus and its protein. J Gen Virol 19: 263-273. https://doi.org/10.1099/0022-1317-19-2-263
    [69] van der Schoot P, Bruinsma R (2005) Electrostatics and the assembly of an RNA virus. Phys Rev E 71: 061928. https://doi.org/10.1103/PhysRevE.71.061928
    [70] Belyi VA, Muthukumar M (2006) Electrostatic origin of the genome packing in viruses. Proc Natl Acad Sci 103: 17174-17178. https://doi.org/10.1073/pnas.0608311103
    [71] Hagan MF (2009) A theory for viral capsid assembly around electrostatic cores. J Chem Phys 130: 114902. https://doi.org/10.1063/1.3086041
    [72] Lorenzo-Leal AC, Vimalanathan S, Bach H (2022) Adherence of SARS-CoV-2 delta variant to a surgical mask and N95 respirators. Future Sci OA 8: FSO808. https://doi.org/10.2144/fsoa-2022-0025
    [73] Javidpour L, Božič A, Najili A, et al. (2021) Electrostatic interaction between SARS-CoV-2 virus and charged electret fibre. Soft Matter 17: 4296-4203. https://doi.org/10.1039/D1SM00232E
    [74] Ren C, Haghighat F, Feng Z, et al. (2023) Impact of ionizers on prevention of airborne infection in classroom. Build Simul 16: 749-764. https://doi.org/10.1007/s12273-022-0959-z
    [75] Fantini J, Azzaz F, Chahinian H, et al. (2023) Electrostatic surface potential as a key parameter in virus transmission and evolution: How to manage future virus pandemics in the post-COVID-19 era. Viruses 15: 284. https://doi.org/10.3390/v15020284
    [76] Wood JP, Magnuson M, Touati A, et al. (2021) Hook Evaluation of electrostatic sprayers and foggers for the application of disinfectants in the era of SARS-CoV-2. PLoS One 16: e0257434. https://doi.org/10.1371/journal.pone.0257434
    [77] Kalra RS, Kandimalla R (2021) Engaging the spikes: heparan sulfate facilitates SARS-CoV-2 spike protein binding to ACE2 and potentiates viral infection. Sig Transduct Target Ther 6: 39. https://doi.org/10.1038/s41392-021-00470-1
    [78] Pawłowski P, Szutowicz I, Marszałek P, et al. (1993) Bioelectrorheological model of the cell. 5. Electrodestruction of cellular membrane in alternating electric field. Biophys J 65: 541-549. https://doi.org/10.1016/S0006-3495(93)81056-7
    [79] Igakura T, Stinchcombe JC, Goon PK, et al. (2003) Spread of HTLV-I between lymphocytes by virus-induced polarization of the cytoskeleton. Science 299: 1713-1716. https://doi.org/10.1126/science.1080115
  • Reader Comments
  • © 2024 the Author(s), licensee AIMS Press. This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0)
通讯作者: 陈斌, bchen63@163.com
  • 1. 

    沈阳化工大学材料科学与工程学院 沈阳 110142

  1. 本站搜索
  2. 百度学术搜索
  3. 万方数据库搜索
  4. CNKI搜索

Metrics

Article views(510) PDF downloads(50) Cited by(0)

Article outline

Figures and Tables

Figures(9)  /  Tables(2)

Other Articles By Authors

/

DownLoad:  Full-Size Img  PowerPoint
Return
Return

Catalog