{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,13]],"date-time":"2026-10-13T03:46:55Z","timestamp":1791863215922,"version":"4.3.4"},"reference-count":146,"publisher":"MDPI AG","issue":"2","license":[{"start":{"date-parts":[[2023,1,19]],"date-time":"2023-01-19T00:00:00Z","timestamp":1674086400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100006021","name":"Direction G\u00e9n\u00e9rale de l\u2019Armement","doi-asserted-by":"publisher","award":["2020007"],"award-info":[{"award-number":["2020007"]}],"id":[{"id":"10.13039\/501100006021","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Viruses"],"abstract":"<jats:p>Virus-cell interactions involve fundamental parameters that need to be considered in strategies implemented to control viral outbreaks. Among these, the surface electrostatic potential can give valuable information to deal with new epidemics. In this article, we describe the role of this key parameter in the hemagglutination of red blood cells and in the co-evolution of synaptic receptors and neurotransmitters. We then establish the functional link between lipid rafts and the electrostatic potential of viruses, with special emphasis on gangliosides, which are sialic-acid-containing, electronegatively charged plasma membrane components. We describe the common features of ganglioside binding domains, which include a wide variety of structures with little sequence homology but that possess key amino acids controlling ganglioside recognition. We analyze the role of the electrostatic potential in the transmission and intra-individual evolution of HIV-1 infections, including gatekeeper and co-receptor switch mechanisms. We show how to organize the epidemic surveillance of influenza viruses by focusing on mutations affecting the hemagglutinin surface potential. We demonstrate that the electrostatic surface potential, by modulating spike-ganglioside interactions, controls the hemagglutination properties of coronaviruses (SARS-CoV-1, MERS-CoV, and SARS-CoV-2) as well as the structural dynamics of SARS-CoV-2 evolution. We relate the broad-spectrum antiviral activity of repositioned molecules to their ability to disrupt virus-raft interactions, challenging the old concept that an antibiotic or anti-parasitic cannot also be an antiviral. We propose a new concept based on the analysis of the electrostatic surface potential to develop, in real time, therapeutic and vaccine strategies adapted to each new viral epidemic.<\/jats:p>","DOI":"10.3390\/v15020284","type":"journal-article","created":{"date-parts":[[2023,1,19]],"date-time":"2023-01-19T03:45:16Z","timestamp":1674099916000},"page":"284","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":29,"title":["Electrostatic Surface Potential as a Key Parameter in Virus Transmission and Evolution: How to Manage Future Virus Pandemics in the Post-COVID-19 Era"],"prefix":"10.3390","volume":"15","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-8653-5521","authenticated-orcid":false,"given":"Jacques","family":"Fantini","sequence":"first","affiliation":[{"name":"Department of Biology, Faculty of Medicine, University of Aix-Marseille, INSERM UMR_S 1072, 13015 Marseille, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fodil","family":"Azzaz","sequence":"additional","affiliation":[{"name":"Department of Biology, Faculty of Medicine, University of Aix-Marseille, INSERM UMR_S 1072, 13015 Marseille, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Henri","family":"Chahinian","sequence":"additional","affiliation":[{"name":"Department of Biology, Faculty of Medicine, University of Aix-Marseille, INSERM UMR_S 1072, 13015 Marseille, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nouara","family":"Yahi","sequence":"additional","affiliation":[{"name":"Department of Biology, Faculty of Medicine, University of Aix-Marseille, INSERM UMR_S 1072, 13015 Marseille, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2023,1,19]]},"reference":[{"key":"ref_1","unstructured":"Fantini, J., and Yahi, N. (2015). Brain Lipids in Synaptic Function and Neurological Disease: Clues to Innovative Therapeutic Strategies for Brain Disorders, Academic Press."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"861","DOI":"10.1038\/nrm2021","article-title":"Do we underestimate the importance of water in cell biology?","volume":"7","author":"Chaplin","year":"2006","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1007\/112_0602","article-title":"Dimensions of systems biology","volume":"157","author":"Huang","year":"2006","journal-title":"Rev. Physiol. Biochem. Pharmacol."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1016\/S0022-5193(75)80115-9","article-title":"Protein synthesis rhythm","volume":"55","author":"Brodsky","year":"1975","journal-title":"J. Theor. Biol."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"20180674","DOI":"10.1098\/rspa.2018.0674","article-title":"The origins of quantum biology","volume":"474","author":"McFadden","year":"2018","journal-title":"Proc. R. Soc. A"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"3754","DOI":"10.1073\/pnas.79.12.3754","article-title":"Electrostatic potential molecular surfaces","volume":"79","author":"Weiner","year":"1982","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1016\/j.jinf.2021.06.001","article-title":"Structural dynamics of SARS-CoV-2 variants: A health monitoring strategy for anticipating Covid-19 outbreaks","volume":"83","author":"Fantini","year":"2021","journal-title":"J. Infect."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/j.virol.2008.06.014","article-title":"Primary HIV-1 R5 isolates from end-stage disease display enhanced viral fitness in parallel with increased gp120 net charge","volume":"379","author":"Repits","year":"2008","journal-title":"Virology"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"1929","DOI":"10.1038\/s41598-018-20225-3","article-title":"Electrostatic variation of haemagglutinin as a hallmark of the evolution of avian influenza viruses","volume":"8","author":"Heidari","year":"2018","journal-title":"Sci. Rep."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1186\/1742-4690-10-130","article-title":"Modelling binding between CCR5 and CXCR4 receptors and their ligands suggests the surface electrostatic potential of the co-receptor to be a key player in the HIV-1 tropism","volume":"10","author":"Kalinina","year":"2013","journal-title":"Retrovirology"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"1144","DOI":"10.1126\/science.7761829","article-title":"Classical electrostatics in biology and chemistry","volume":"268","author":"Honig","year":"1995","journal-title":"Science"},{"key":"ref_12","doi-asserted-by":"crossref","unstructured":"L\u00f3pez de Victoria, A., Kieslich, C.A., Rizos, A.K., Krambovitis, E., and Morikis, D. (2012). Clustering of HIV-1 subtypes based on gp120 V3 loop electrostatic properties. BMC Biophys., 5.","DOI":"10.1186\/2046-1682-5-3"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1002\/jmr.577","article-title":"The Poisson\u2013Boltzmann equation for biomolecular electrostatics: A tool for structural biology","volume":"15","author":"Fogolari","year":"2002","journal-title":"J. Mol. Recognit."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"7684","DOI":"10.1021\/j100382a068","article-title":"Calculating total electrostatic energies with the nonlinear Poisson-Boltzmann equation","volume":"94","author":"Sharp","year":"1990","journal-title":"J. Phys. Chem."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1002\/wcms.19","article-title":"The electrostatic potential: An overview","volume":"1","author":"Murray","year":"2011","journal-title":"Wiley Interdiscip. Rev. Comput. Mol. Sci."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"W270","DOI":"10.1093\/nar\/gkn314","article-title":"PBEQ-Solver for online visualization of electrostatic potential of biomolecules","volume":"36","author":"Jo","year":"2008","journal-title":"Nucleic Acids Res."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1016\/S0010-4655(98)00016-2","article-title":"Continuum solvation model: Computation of electrostatic forces from numerical solutions to the Poisson-Boltzmann equation","volume":"111","author":"Im","year":"1998","journal-title":"Comput. Phys. Commun."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1016\/j.sbi.2007.05.008","article-title":"Nucleic acid solvation: From outside to insight","volume":"17","author":"Auffinger","year":"2007","journal-title":"Curr. Opin. Struct. Biol."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1017\/S1462399402005392","article-title":"Lipid rafts: Structure, function and role in HIV, Alzheimer\u2019s and prion diseases","volume":"4","author":"Fantini","year":"2002","journal-title":"Expert Rev. Mol. Med."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"1748","DOI":"10.1002\/pro.3906","article-title":"Progress toward Alzheimer\u2019s disease treatment: Leveraging the Achilles\u2019 heel of A\u03b2 oligomers?","volume":"29","author":"Fantini","year":"2020","journal-title":"Protein Sci. A Publ. Protein Soc."},{"key":"ref_21","doi-asserted-by":"crossref","unstructured":"Fontes, A., Fernandes, H., Barjas-Castro, M., de Thomaz, A., de Ysasa Pozzo, L., Barbosa, L., and Cesar, C. (2006). Red Blood Cell Membrane Viscoelasticity, Agglutination, and Zeta Potential Measurements with Double Optical Tweezers, SPIE.","DOI":"10.1117\/12.646682"},{"key":"ref_22","first-page":"184","article-title":"Effects of Proteases and Neuraminidase on RBC Surface Charge and Agglutination: A Klinetic Study 1","volume":"28","author":"Luner","year":"1975","journal-title":"Vox Sang."},{"key":"ref_23","first-page":"250","article-title":"Hemagglutination and the closest distance of approach of normal, neuraminidase-and papain-treated erythrocytes","volume":"47","author":"Absolom","year":"1984","journal-title":"Vox Sang."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"3325","DOI":"10.1016\/j.jmb.2016.05.020","article-title":"Gangliosides of the Vertebrate Nervous System","volume":"428","author":"Schnaar","year":"2016","journal-title":"J. Mol. Biol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"461","DOI":"10.1152\/physrev.00033.2013","article-title":"Sialic acids in the brain: Gangliosides and polysialic acid in nervous system development, stability, disease, and regeneration","volume":"94","author":"Schnaar","year":"2014","journal-title":"Physiol. Rev."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1016\/bs.apcsb.2021.08.003","article-title":"Ganglioside binding domains in proteins: Physiological and pathological mechanisms","volume":"128","author":"Azzaz","year":"2022","journal-title":"Adv. Protein Chem. Struct. Biol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1038\/s41586-019-0881-4","article-title":"Structural insights into the activation of metabotropic glutamate receptors","volume":"566","author":"Koehl","year":"2019","journal-title":"Nature"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"691","DOI":"10.1002\/open.202000108","article-title":"Variations in proteins dielectric constants","volume":"9","author":"Amin","year":"2020","journal-title":"ChemistryOpen"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"190","DOI":"10.1093\/embo-reports\/kvd025","article-title":"Membrane raft microdomains mediate lateral assemblies required for HIV-1 infection","volume":"1","author":"Lacalle","year":"2000","journal-title":"EMBO Rep"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"557","DOI":"10.1038\/nri1129","article-title":"Pathogens: Raft hijackers","volume":"3","year":"2003","journal-title":"Nat. Rev. Immunol."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"631274","DOI":"10.3389\/fmicb.2021.631274","article-title":"Membrane rafts: Portals for viral entry","volume":"12","author":"Ripa","year":"2021","journal-title":"Front. Microbiol."},{"key":"ref_32","doi-asserted-by":"crossref","unstructured":"Omasta, B., and Tomaskova, J. (2022). Cellular Lipids\u2014Hijacked Victims of Viruses. Viruses, 14.","DOI":"10.3390\/v14091896"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"655","DOI":"10.1194\/jlr.R200021-JLR200","article-title":"Lipid rafts: Bringing order to chaos","volume":"44","author":"Pike","year":"2003","journal-title":"J. Lipid Res."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"429","DOI":"10.1016\/0163-7827(94)90026-4","article-title":"Gangliosides as influenza virus receptors. Variation of influenza viruses and their recognition of the receptor sialo-sugar chains. Prog. Lipid Res. 1994, 33, 429\u2013457","volume":"33","author":"Suzuki","year":"1994","journal-title":"Prog. Lipid Res."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"5406","DOI":"10.1073\/pnas.78.9.5406","article-title":"Specific gangliosides function as host cell receptors for Sendai virus","volume":"78","author":"Markwell","year":"1981","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"12846","DOI":"10.1128\/JVI.01311-07","article-title":"N-glycolyl GM1 ganglioside as a receptor for simian virus 40","volume":"81","author":"Smith","year":"2007","journal-title":"J. Virol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"2590","DOI":"10.1016\/j.jmb.2018.06.024","article-title":"Virus\u2013receptor interactions: The key to cellular invasion","volume":"430","author":"Maginnis","year":"2018","journal-title":"J. Mol. Biol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"9079","DOI":"10.1128\/JVI.72.11.9079-9091.1998","article-title":"Structure and function of a ganglioside receptor for porcine rotavirus","volume":"72","author":"Rolsma","year":"1998","journal-title":"J. Virol."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"7967","DOI":"10.1074\/jbc.273.14.7967","article-title":"Specific interaction of HIV-1 and HIV-2 surface envelope glycoproteins with monolayers of galactosylceramide and ganglioside GM3","volume":"273","author":"Hammache","year":"1998","journal-title":"J. Biol. Chem."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"5244","DOI":"10.1128\/JVI.73.6.5244-5248.1999","article-title":"Human erythrocyte glycosphingolipids as alternative cofactors for human immunodeficiency virus type 1 (HIV-1) entry: Evidence for CD4-induced interactions between HIV-1 gp120 and reconstituted membrane microdomains of glycosphingolipids (Gb3 and GM3)","volume":"73","author":"Hammache","year":"1999","journal-title":"J. Virol."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1006\/bbrc.1998.8531","article-title":"Sequential interaction of CD4 and HIV-1 gp120 with a reconstituted membrane patch of ganglioside GM3: Implications for the role of glycolipids as potential HIV-1 fusion cofactors","volume":"246","author":"Hammache","year":"1998","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"6377","DOI":"10.1128\/JVI.74.14.6377-6385.2000","article-title":"Glycosphingolipids promote entry of a broad range of human immunodeficiency virus type 1 isolates into cell lines expressing CD4, CXCR4, and\/or CCR5","volume":"74","author":"Hug","year":"2000","journal-title":"J. Virol."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"320","DOI":"10.1126\/science.1857969","article-title":"Inhibition of entry of HIV-1 in neural cell lines by antibodies against galactosyl ceramide","volume":"253","author":"Harouse","year":"1991","journal-title":"Science"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"4848","DOI":"10.1128\/jvi.66.8.4848-4854.1992","article-title":"Galactosyl ceramide (or a closely related molecule) is the receptor for human immunodeficiency virus type 1 on human colon epithelial HT29 cells","volume":"66","author":"Yahi","year":"1992","journal-title":"J. Virol."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"10957","DOI":"10.1021\/bi060762s","article-title":"Prediction of glycolipid-binding domains from the amino acid sequence of lipid raft-associated proteins: Application to HpaA, a protein involved in the adhesion of Helicobacter pylori to gastrointestinal cells","volume":"45","author":"Fantini","year":"2006","journal-title":"Biochemistry"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"11292","DOI":"10.1074\/jbc.M111679200","article-title":"Identification of a common sphingolipid-binding domain in Alzheimer, prion, and HIV-1 proteins","volume":"277","author":"Mahfoud","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1016\/j.bbrc.2020.10.015","article-title":"Leveraging coronavirus binding to gangliosides for innovative vaccine and therapeutic strategies against COVID-19","volume":"538","author":"Fantini","year":"2021","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_48","doi-asserted-by":"crossref","unstructured":"Fantini, J., Chahinian, H., and Yahi, N. (2022). A Vaccine Strategy Based on the Identification of an Annular Ganglioside Binding Motif in Monkeypox Virus Protein E8L. Viruses, 14.","DOI":"10.3390\/v14112531"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"1027","DOI":"10.1007\/s00018-003-3003-1","article-title":"How sphingolipids bind and shape proteins: Molecular basis of lipid-protein interactions in lipid shells, rafts and related biomembrane domains","volume":"60","author":"Fantini","year":"2003","journal-title":"Cell. Mol. Life Sci. CMLS"},{"key":"ref_50","first-page":"1010","article-title":"HyperChem: A software package for computational chemistry and molecular modeling","volume":"14","author":"Froimowitz","year":"1993","journal-title":"BioTechniques"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1128\/mr.59.1.63-93.1995","article-title":"The human immunodeficiency virus type 1 (HIV-1) CD4 receptor and its central role in promotion of HIV-1 infection","volume":"59","author":"Bour","year":"1995","journal-title":"Microbiol. Rev."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1016\/S0952-7915(97)80110-0","article-title":"Co-receptors for HIV-1 entry","volume":"9","author":"Moore","year":"1997","journal-title":"Curr. Opin. Immunol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1089\/088922204322749567","article-title":"The CCR5 and CXCR4 coreceptors\u2014Central to understanding the transmission and pathogenesis of human immunodeficiency virus type 1 infection","volume":"20","author":"Moore","year":"2004","journal-title":"AIDS Res. Hum. Retrovir."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1016\/j.tim.2005.04.005","article-title":"The HIV coreceptor switch: A population dynamical perspective","volume":"13","author":"Regoes","year":"2005","journal-title":"Trends Microbiol."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"2937","DOI":"10.1097\/00002030-200012220-00016","article-title":"Envelope V3 amino acid sequence predicts HIV-1 phenotype (co-receptor usage and tropism for macrophages)","volume":"14","author":"Briggs","year":"2000","journal-title":"AIDS"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"18","DOI":"10.7150\/thno.5392","article-title":"The puzzling role of CXCR4 in human immunodeficiency virus infection","volume":"3","author":"Vicenzi","year":"2013","journal-title":"Theranostics"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"217","DOI":"10.2174\/1570162033485357","article-title":"HIV-1 coreceptor usage, transmission, and disease progression","volume":"1","author":"Philpott","year":"2003","journal-title":"Curr. HIV Res."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"518","DOI":"10.1002\/mrd.22489","article-title":"The ImageJ ecosystem: An open platform for biomedical image analysis","volume":"82","author":"Schindelin","year":"2015","journal-title":"Mol. Reprod. Dev."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/S1473-3099(10)70186-9","article-title":"Tracking a century of global expansion and evolution of HIV to drive understanding and to combat disease","volume":"11","author":"Tebit","year":"2011","journal-title":"Lancet Infect. Dis."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"13433","DOI":"10.1074\/jbc.M009779200","article-title":"N-linked glycosylation of the HIV type-1 gp120 envelope glycoprotein as a major determinant of CCR5 and CXCR4 coreceptor utilization","volume":"276","author":"Pollakis","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"3135","DOI":"10.1002\/jcc.21886","article-title":"Glycan Reader: Automated sugar identification and simulation preparation for carbohydrates and glycoproteins","volume":"32","author":"Jo","year":"2011","journal-title":"J. Comput. Chem."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"1599","DOI":"10.3389\/fimmu.2019.01599","article-title":"Negative and positive selection pressure during sexual transmission of transmitted founder HIV-1","volume":"10","author":"Nijmeijer","year":"2019","journal-title":"Front. Immunol."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1016\/0304-4165(80)90009-4","article-title":"Composition and function of human cervical mucus","volume":"630","author":"Wolf","year":"1980","journal-title":"Biochim. Et Biophys. Acta (BBA)-Gen. Subj."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"S6","DOI":"10.1186\/1479-5876-9-S1-S6","article-title":"Selective transmission of R5 HIV-1 variants: Where is the gatekeeper?","volume":"9","author":"Grivel","year":"2011","journal-title":"J. Transl. Med."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"1948","DOI":"10.1128\/JVI.74.4.1948-1960.2000","article-title":"Selective interactions of polyanions with basic surfaces on human immunodeficiency virus type 1 gp120","volume":"74","author":"Moulard","year":"2000","journal-title":"J. Virol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1006\/viro.1998.9216","article-title":"Sulfatide inhibits HIV-1 entry into CD4\u2212\/CXCR4+ cells","volume":"246","author":"Fantini","year":"1998","journal-title":"Virology"},{"key":"ref_67","first-page":"1663","article-title":"HIV-1 transmission across the vaginal epithelium","volume":"11","author":"Fantini","year":"1997","journal-title":"AIDS"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1002\/jmv.20478","article-title":"Selective sequestration of X4 isolates by human genital epithelial cells: Implication for virus tropism selection process during sexual transmission of HIV","volume":"77","author":"Berlier","year":"2005","journal-title":"J. Med. Virol."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"785","DOI":"10.1097\/QAD.0b013e328351426e","article-title":"Selective transmigration of monocyte-associated HIV-1 across a human cervical monolayer and its modulation by seminal plasma","volume":"26","author":"Lawrence","year":"2012","journal-title":"AIDS"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"312","DOI":"10.1038\/nrmicro1387","article-title":"Selective transmission of CCR5-utilizing HIV-1: The\u2019gatekeeper\u2019problem resolved?","volume":"4","author":"Margolis","year":"2006","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"2706","DOI":"10.1128\/JVI.75.6.2706-2709.2001","article-title":"Macrophage tropism of human immunodeficiency virus type 1 facilitates in vivo escape from cytotoxic T-lymphocyte pressure","volume":"75","author":"Schutten","year":"2001","journal-title":"J. Virol."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1006\/viro.1997.8980","article-title":"Differences in chemokine coreceptor usage between genetic subtypes of HIV-1","volume":"241","author":"Tscherning","year":"1998","journal-title":"Virology"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"1311","DOI":"10.1086\/319859","article-title":"Use of drug resistance sequence data for the systematic detection of non-B human immunodeficiency virus type 1 (HIV-1) subtypes: How to create a sentinel site for monitoring the genetic diversity of HIV-1 at a country scale","volume":"183","author":"Yahi","year":"2001","journal-title":"J. Infect. Dis."},{"key":"ref_74","doi-asserted-by":"crossref","unstructured":"Righetto, I., Milani, A., Cattoli, G., and Filippini, F. (2014). Comparative structural analysis of haemagglutinin proteins from type A influenza viruses: Conserved and variable features. BMC Bioinform., 15.","DOI":"10.1186\/s12859-014-0363-5"},{"key":"ref_75","doi-asserted-by":"crossref","unstructured":"Righetto, I., and Filippini, F. (2020). Normal modes analysis and surface electrostatics of haemagglutinin proteins as fingerprints for high pathogenic type A influenza viruses. BMC Bioinform., 21.","DOI":"10.1186\/s12859-020-03563-w"},{"key":"ref_76","doi-asserted-by":"crossref","unstructured":"Jimenez-Alberto, A., Alvarado-Facundo, E., Ribas-Aparicio, R.M., and Castel\u00e1n-Vega, J.A. (2013). Analysis of adaptation mutants in the hemagglutinin of the influenza A (H1N1) pdm09 virus. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0070005"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"426","DOI":"10.1038\/333426a0","article-title":"Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid","volume":"333","author":"Weis","year":"1988","journal-title":"Nature"},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1111\/j.1750-2659.2008.00051.x","article-title":"Sialic acid tissue distribution and influenza virus tropism","volume":"2","author":"Kumlin","year":"2008","journal-title":"Influenza Other Respir. Viruses"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1080\/03079457.2012.759176","article-title":"Expression and distribution of sialic acid influenza virus receptors in wild birds","volume":"42","author":"Franca","year":"2013","journal-title":"Avian Pathol."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"3754","DOI":"10.1128\/JVI.02596-08","article-title":"Role of sialic acid binding specificity of the 1918 influenza virus hemagglutinin protein in virulence and pathogenesis for mice","volume":"83","author":"Qi","year":"2009","journal-title":"J. Virol."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"1","DOI":"10.2147\/JRLCR.S140624","article-title":"Sialic acid receptors: Focus on their role in influenza infection","volume":"10","year":"2018","journal-title":"J. Recept. Ligand Channel Res."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"392","DOI":"10.1038\/nature12144","article-title":"Receptor binding by a ferret-transmissible H5 avian influenza virus","volume":"497","author":"Xiong","year":"2013","journal-title":"Nature"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"1458","DOI":"10.1073\/pnas.1218509110","article-title":"Hemagglutinin homologue from H17N10 bat influenza virus exhibits divergent receptor-binding and pH-dependent fusion activities","volume":"110","author":"Zhu","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"2332","DOI":"10.1056\/NEJMp048082","article-title":"Planning for epidemics--the lessons of SARS","volume":"350","author":"Weinstein","year":"2004","journal-title":"N. Engl. J. Med."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"1814","DOI":"10.1056\/NEJMoa1211721","article-title":"Isolation of a novel coronavirus from a man with pneumonia in Saudi Arabia","volume":"367","author":"Zaki","year":"2012","journal-title":"N. Engl. J. Med."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"270","DOI":"10.1038\/s41586-020-2012-7","article-title":"A pneumonia outbreak associated with a new coronavirus of probable bat origin","volume":"579","author":"Zhou","year":"2020","journal-title":"Nature"},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"344","DOI":"10.1016\/j.bbrc.2008.02.023","article-title":"Lipid rafts are involved in SARS-CoV entry into Vero E6 cells","volume":"369","author":"Lu","year":"2008","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1016\/j.micinf.2006.10.015","article-title":"Lipid rafts play an important role in the early stage of severe acute respiratory syndrome-coronavirus life cycle","volume":"9","author":"Li","year":"2007","journal-title":"Microbes Infect."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"E8508","DOI":"10.1073\/pnas.1712592114","article-title":"Identification of sialic acid-binding function for the Middle East respiratory syndrome coronavirus spike glycoprotein","volume":"114","author":"Li","year":"2017","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"1245","DOI":"10.1093\/glycob\/cwab032","article-title":"The role of cell surface sialic acids for SARS-CoV-2 infection","volume":"31","author":"Sun","year":"2021","journal-title":"Glycobiology"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"186","DOI":"10.3389\/fmolb.2020.00186","article-title":"A multi-targeting approach to fight SARS-CoV-2 attachment","volume":"7","author":"Pirone","year":"2020","journal-title":"Front. Mol. Biosci."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1038\/nature12005","article-title":"Dipeptidyl peptidase 4 is a functional receptor for the emerging human coronavirus-EMC","volume":"495","author":"Raj","year":"2013","journal-title":"Nature"},{"key":"ref_93","doi-asserted-by":"crossref","unstructured":"Hatmal, M.M.M., Alshaer, W., Al-Hatamleh, M.A., Hatmal, M., Smadi, O., Taha, M.O., Oweida, A.J., Boer, J.C., Mohamud, R., and Plebanski, M. (2020). Comprehensive structural and molecular comparison of spike proteins of SARS-CoV-2, SARS-CoV and MERS-CoV, and their interactions with ACE2. Cells, 9.","DOI":"10.3390\/cells9122638"},{"key":"ref_94","doi-asserted-by":"crossref","unstructured":"Boschi, C., Scheim, D.E., Bancod, A., Militello, M., Bideau, M.L., Colson, P., Fantini, J., and Scola, B.L. (2022). SARS-CoV-2 Spike Protein Induces Hemagglutination: Implications for COVID-19 Morbidities and Therapeutics and for Vaccine Adverse Effects. Int. J. Mol. Sci., 23.","DOI":"10.1101\/2022.11.24.517882"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1038\/nrmicro3346","article-title":"The sweet spot: Defining virus\u2013sialic acid interactions","volume":"12","author":"Reiss","year":"2014","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_96","doi-asserted-by":"crossref","unstructured":"Gu\u00e9rin, P., Yahi, N., Azzaz, F., Chahinian, H., Sabatier, J.M., and Fantini, J. (2022). Structural Dynamics of the SARS-CoV-2 Spike Protein: A 2-Year Retrospective Analysis of SARS-CoV-2 Variants (from Alpha to Omicron) Reveals an Early Divergence between Conserved and Variable Epitopes. Molecules, 27.","DOI":"10.3390\/molecules27123851"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1038\/s41579-021-00573-0","article-title":"SARS-CoV-2 variants, spike mutations and immune escape","volume":"19","author":"Harvey","year":"2021","journal-title":"Nat. Rev. Microbiol."},{"key":"ref_98","doi-asserted-by":"crossref","unstructured":"Lazarevic, I., Pravica, V., Miljanovic, D., and Cupic, M. (2021). Immune evasion of SARS-CoV-2 emerging variants: What have we learnt so far?. Viruses, 13.","DOI":"10.3390\/v13071192"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1038\/s41423-021-00836-z","article-title":"Increased immune escape of the new SARS-CoV-2 variant of concern Omicron","volume":"19","author":"Hu","year":"2022","journal-title":"Cell. Mol. Immunol."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"e70658","DOI":"10.7554\/eLife.70658","article-title":"Effects of common mutations in the SARS-CoV-2 Spike RBD and its ligand, the human ACE2 receptor on binding affinity and kinetics","volume":"10","author":"Barton","year":"2021","journal-title":"elife"},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"7011","DOI":"10.1038\/s41467-022-34506-z","article-title":"Compensatory epistasis maintains ACE2 affinity in SARS-CoV-2 Omicron BA.1","volume":"13","author":"Moulana","year":"2022","journal-title":"Nat. Commun."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"2019","DOI":"10.1002\/jmv.27577","article-title":"The puzzling mutational landscape of the SARS-2-variant Omicron","volume":"94","author":"Fantini","year":"2022","journal-title":"J. Med. Virol."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"1277","DOI":"10.1002\/jmv.27528","article-title":"The electrostatic potential of the Omicron variant spike is higher than in Delta and Delta-plus variants: A hint to higher transmissibility?","volume":"94","author":"Pascarella","year":"2021","journal-title":"J. Med. Virol."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"eabq4450","DOI":"10.1126\/sciimmunol.abq4450","article-title":"Antigenic cartography of SARS-CoV-2 reveals that Omicron BA.1 and BA.2 are antigenically distinct","volume":"7","author":"Mykytyn","year":"2022","journal-title":"Sci. Immunol."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"371","DOI":"10.1126\/science.1097211","article-title":"Mapping the antigenic and genetic evolution of influenza virus","volume":"305","author":"Smith","year":"2004","journal-title":"Science"},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"14171","DOI":"10.1038\/srep14171","article-title":"Antigenic patterns and evolution of the human influenza A (H1N1) virus","volume":"5","author":"Liu","year":"2015","journal-title":"Sci. Rep."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"2332","DOI":"10.1016\/j.cell.2021.03.028","article-title":"N-terminal domain antigenic mapping reveals a site of vulnerability for SARS-CoV-2","volume":"184","author":"McCallum","year":"2021","journal-title":"Cell"},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"e2392","DOI":"10.1002\/rmv.2392","article-title":"Monkeypox: An international epidemic","volume":"32","author":"Focosi","year":"2022","journal-title":"Rev. Med. Virol."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"140260","DOI":"10.1016\/j.cplett.2022.140260","article-title":"Identification of possible binding modes of SARS-CoV-2 spike N-terminal domain for ganglioside GM1","volume":"812","author":"Das","year":"2022","journal-title":"Chem. Phys. Lett."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"450","DOI":"10.1038\/s41586-020-2571-7","article-title":"Potent neutralizing antibodies against multiple epitopes on SARS-CoV-2 spike","volume":"584","author":"Liu","year":"2020","journal-title":"Nature"},{"key":"ref_111","doi-asserted-by":"crossref","unstructured":"Azzaz, F., Yahi, N., Chahinian, H., and Fantini, J. (2022). The Epigenetic Dimension of Protein Structure Is an Intrinsic Weakness of the AlphaFold Program. Biomolecules, 12.","DOI":"10.3390\/biom12101527"},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"15983","DOI":"10.1038\/s41598-022-20397-z","article-title":"Novel multi epitope-based vaccine against monkeypox virus: Vaccinomic approach","volume":"12","author":"Shantier","year":"2022","journal-title":"Sci. Rep."},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"1742","DOI":"10.1128\/AAC.32.11.1742","article-title":"Sulfated polysaccharides are potent and selective inhibitors of various enveloped viruses, including herpes simplex virus, cytomegalovirus, vesicular stomatitis virus, and human immunodeficiency virus","volume":"32","author":"Baba","year":"1988","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_114","doi-asserted-by":"crossref","unstructured":"Lin, L.-T., Chen, T.-Y., Lin, S.-C., Chung, C.-Y., Lin, T.-C., Wang, G.-H., Anderson, R., Lin, C.-C., and Richardson, C.D. (2013). Broad-spectrum antiviral activity of chebulagic acid and punicalagin against viruses that use glycosaminoglycans for entry. BMC Microbiol., 13.","DOI":"10.1186\/1471-2180-13-187"},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"24349","DOI":"10.1016\/S0021-9258(19)51089-4","article-title":"Suramin inhibits binding of the V3 region of HIV-1 envelope glycoprotein gp120 to galactosylceramide, the receptor for HIV-1 gp120 on human colon epithelial cells","volume":"269","author":"Yahi","year":"1994","journal-title":"J. Biol. Chem."},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"15663","DOI":"10.1021\/bi961205g","article-title":"SPC3, a V3 loop-derived synthetic peptide inhibitor of HIV-1 infection, binds to cell surface glycosphingolipids","volume":"35","author":"Hammache","year":"1996","journal-title":"Biochemistry"},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"4867","DOI":"10.1073\/pnas.92.11.4867","article-title":"SPC3, a synthetic peptide derived from the V3 domain of human immunodeficiency virus type 1 (HIV-1) gp120, inhibits HIV-1 entry into CD4+ and CD4-cells by two distinct mechanisms","volume":"92","author":"Yahi","year":"1995","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"320","DOI":"10.1128\/jvi.69.1.320-325.1995","article-title":"Synthetic multimeric peptides derived from the principal neutralization domain (V3 loop) of human immunodeficiency virus type 1 (HIV-1) gp120 bind to galactosylceramide and block HIV-1 infection in a human CD4-negative mucosal epithelial cell line","volume":"69","author":"Yahi","year":"1995","journal-title":"J. Virol."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"2188","DOI":"10.1021\/jm0011124","article-title":"Amphiphilic anionic analogues of galactosylceramide: Synthesis, anti-HIV-1 activity, and gp120 binding","volume":"44","author":"Greiner","year":"2001","journal-title":"J. Med. Chem."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1016\/S0008-6215(00)00055-0","article-title":"Synthesis of single-and double-chain fluorocarbon and hydrocarbon galactosyl amphiphiles and their anti-HIV-1 activity","volume":"327","author":"Clary","year":"2000","journal-title":"Carbohydr. Res."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1021\/bc034156a","article-title":"Synthesis of novel, multivalent glycodendrimers as ligands for HIV-1 gp120","volume":"15","author":"Kensinger","year":"2004","journal-title":"Bioconjugate Chem."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1016\/j.antiviral.2008.04.004","article-title":"Glycoside analogs of \u03b2-galactosylceramide, a novel class of small molecule antiviral agents that inhibit HIV-1 entry","volume":"80","author":"Garg","year":"2008","journal-title":"Antivir. Res."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"7245","DOI":"10.1074\/jbc.272.11.7245","article-title":"Synthetic soluble analogs of galactosylceramide (GalCer) bind to the V3 domain of HIV-1 gp120 and inhibit HIV-1-induced fusion and entry","volume":"272","author":"Fantini","year":"1997","journal-title":"J. Biol. Chem."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"105949","DOI":"10.1016\/j.ijantimicag.2020.105949","article-title":"Hydroxychloroquine and azithromycin as a treatment of COVID-19: Results of an open-label non-randomized clinical trial","volume":"56","author":"Gautret","year":"2020","journal-title":"Int. J. Antimicrob. Agents"},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"105960","DOI":"10.1016\/j.ijantimicag.2020.105960","article-title":"Structural and molecular modelling studies reveal a new mechanism of action of chloroquine and hydroxychloroquine against SARS-CoV-2 infection","volume":"55","author":"Fantini","year":"2020","journal-title":"Int. J. Antimicrob. Agents"},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"106020","DOI":"10.1016\/j.ijantimicag.2020.106020","article-title":"Synergistic antiviral effect of hydroxychloroquine and azithromycin in combination against SARS-CoV-2: What molecular dynamics studies of virus-host interactions reveal","volume":"56","author":"Fantini","year":"2020","journal-title":"Int. J. Antimicrob. Agents"},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"104228","DOI":"10.1016\/j.micpath.2020.104228","article-title":"In vitro testing of combined hydroxychloroquine and azithromycin on SARS-CoV-2 shows synergistic effect","volume":"145","author":"Andreani","year":"2020","journal-title":"Microb. Pathog."},{"key":"ref_128","doi-asserted-by":"crossref","unstructured":"Jans, D.A., and Wagstaff, K.M. (2020). Ivermectin as a broad-spectrum host-directed antiviral: The real deal?. Cells, 9.","DOI":"10.3390\/cells9092100"},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1016\/j.ijantimicag.2016.07.004","article-title":"Fighting viruses with antibiotics: An overlooked path","volume":"48","author":"Colson","year":"2016","journal-title":"Int. J. Antimicrob. Agents"},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"112682","DOI":"10.1016\/j.biopha.2022.112682","article-title":"Antiviral effects of azithromycin: A narrative review","volume":"147","author":"Khoshnood","year":"2022","journal-title":"Biomed. Pharmacother."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"1153","DOI":"10.1007\/s00210-020-01902-5","article-title":"Ivermectin, antiviral properties and COVID-19: A possible new mechanism of action","volume":"393","author":"Rizzo","year":"2020","journal-title":"Naunyn-Schmiedeberg\u2019s Arch. Pharmacol."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"979","DOI":"10.1016\/j.cmi.2020.05.016","article-title":"Clinical evidence for repurposing chloroquine and hydroxychloroquine as antiviral agents: A systematic review","volume":"26","author":"Rodrigo","year":"2020","journal-title":"Clin. Microbiol. Infect."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1016\/j.antiviral.2017.04.017","article-title":"Polysulfonate suramin inhibits Zika virus infection","volume":"143","author":"Tan","year":"2017","journal-title":"Antivir. Res."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"1254","DOI":"10.1093\/jnci\/81.16.1254","article-title":"AIDS-antiviral sulfolipids from cyanobacteria (blue-green algae)","volume":"81","author":"Gustafson","year":"1989","journal-title":"JNCI J. Natl. Cancer Inst."},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1016\/j.slasd.2021.12.005","article-title":"A high throughput screening assay for inhibitors of SARS-CoV-2 pseudotyped particle entry","volume":"27","author":"Xu","year":"2022","journal-title":"Slas Discov."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"47","DOI":"10.2174\/1566523216666160119093948","article-title":"Pseudotyping viral vectors with emerging virus envelope proteins","volume":"16","author":"Steffen","year":"2016","journal-title":"Curr. Gene Ther."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"3034","DOI":"10.1021\/acsinfecdis.1c00278","article-title":"Antiviral potential of the antimicrobial drug atovaquone against SARS-CoV-2 and emerging variants of concern","volume":"7","author":"Arulanandam","year":"2021","journal-title":"ACS Infect. Dis."},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"2850","DOI":"10.1016\/j.apsb.2021.02.024","article-title":"Repurposing carrimycin as an antiviral agent against human coronaviruses, including the currently pandemic SARS-CoV-2","volume":"11","author":"Yan","year":"2021","journal-title":"Acta Pharm. Sin. B"},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"e12953","DOI":"10.1111\/cpr.12953","article-title":"Direct inhibitory effect on viral entry of influenza A and SARS-CoV-2 viruses by azithromycin","volume":"54","author":"Du","year":"2021","journal-title":"Cell Prolif."},{"key":"ref_140","doi-asserted-by":"crossref","unstructured":"Ou, T., Mou, H., Zhang, L., Ojha, A., Choe, H., and Farzan, M. (2021). Hydroxychloroquine-mediated inhibition of SARS-CoV-2 entry is attenuated by TMPRSS2. PLoS Pathog., 17.","DOI":"10.1371\/journal.ppat.1009212"},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1186\/s12985-016-0607-2","article-title":"Suramin is a potent inhibitor of Chikungunya and Ebola virus cell entry","volume":"13","author":"Beck","year":"2016","journal-title":"Virol. J."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1093\/jac\/dkh399","article-title":"Glycodendritic structures: Promising new antiviral drugs","volume":"54","author":"Rojo","year":"2004","journal-title":"J. Antimicrob. Chemother."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"266","DOI":"10.4103\/1995-7645.318304","article-title":"Ivermectin as an adjunct treatment for hospitalized adult COVID-19 patients: A randomized multi-center clinical trial","volume":"14","author":"Niaee","year":"2021","journal-title":"Asian Pac. J. Trop. Med."},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"03000605211013550","DOI":"10.1177\/03000605211013550","article-title":"Ivermectin in combination with doxycycline for treating COVID-19 symptoms: A randomized trial","volume":"49","author":"Mahmud","year":"2021","journal-title":"J. Int. Med. Res."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"314","DOI":"10.1016\/j.ijid.2021.04.035","article-title":"Positive impact of oral hydroxychloroquine and povidone-iodine throat spray for COVID-19 prophylaxis: An open-label randomized trial","volume":"106","author":"Seet","year":"2021","journal-title":"Int. J. Infect. Dis."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"512","DOI":"10.1038\/s41419-020-2721-8","article-title":"Is hydroxychloroquine beneficial for COVID-19 patients?","volume":"11","author":"Li","year":"2020","journal-title":"Cell Death Dis."}],"container-title":["Viruses"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1999-4915\/15\/2\/284\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T18:10:10Z","timestamp":1760119810000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1999-4915\/15\/2\/284"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,1,19]]},"references-count":146,"journal-issue":{"issue":"2","published-online":{"date-parts":[[2023,2]]}},"alternative-id":["v15020284"],"URL":"https:\/\/doi.org\/10.3390\/v15020284","relation":{},"ISSN":["1999-4915"],"issn-type":[{"value":"1999-4915","type":"electronic"}],"subject":[],"published":{"date-parts":[[2023,1,19]]}}}