2025
SARS-CoV-2 Receptor Binding Domain (RBD) Protein–Protein Conjugate Induces Similar or Better Antibody Responses as Spike mRNA in Rhesus Macaques
Scaria P, Rowe C, Kosik I, Hu Z, Renn J, Alani N, Kemanli P, Orr-Gonzalez S, Lambert L, Adeyemi K, Doritchamou J, Barnafo E, Rausch K, Muslinkina L, Morrison R, Todd J, Esposito D, Lees A, Yewdell J, Duffy P. SARS-CoV-2 Receptor Binding Domain (RBD) Protein–Protein Conjugate Induces Similar or Better Antibody Responses as Spike mRNA in Rhesus Macaques. Vaccines 2025, 13: 648. PMID: 40573979, PMCID: PMC12197534, DOI: 10.3390/vaccines13060648.Peer-Reviewed Original ResearchVirus neutralizing activityMRNA vaccinesAntibody responseReceptor-binding domainSARS-CoV-2Rhesus macaquesNeutralizing activityIgG subclass profileEnhanced antibody responseReceptor binding inhibitionDevelopment of vaccinesPolyclonal immune seraVaccine platformSubclass profileClinical trialsSARS-CoV-2 spike proteinTarget antigenAntibody avidityVariants of SARS-CoV-2Efficacious vaccinesMultiple time pointsImmune serumEarly vaccinationSARS-CoV-2 receptor-binding domainVaccineSpike specific IgG3 and nucleocapsid IgG response in serum serve as distinguishing immunological markers between SARS-CoV-2 infection and vaccination
Akhtar M, Islam M, Khaton F, Rahman F, Sami T, Tauheed I, Ahmed T, Akter A, Khan I, Khan Z, Kumar Biswas P, Ryan E, Banu S, Shirin T, Chowdhury F, Khan A, Bhuiyan T, Qadri F. Spike specific IgG3 and nucleocapsid IgG response in serum serve as distinguishing immunological markers between SARS-CoV-2 infection and vaccination. Frontiers In Immunology 2025, 16: 1518915. PMID: 40213555, PMCID: PMC11983542, DOI: 10.3389/fimmu.2025.1518915.Peer-Reviewed Original ResearchConceptsCOVID-19 patientsSARS-CoV-2 infectionIgG responsesCOVID-19 vaccinated individualsCOVID-19 vaccineReceptor-binding domainSARS-CoV-2RBD-specific IgG responsesIgG subclass antibody responsesSpecific IgG responsesEarly phase of infectionSubclass antibody responsesNatural infectionPhase of infectionDays of infectionBreakthrough infectionImmunological markersVaccine recipientsNucleocapsid IgGSpike receptor-binding domainAntibody responseIgG subclassesImmunological responseIgG3 subclassPatients
2024
Spatial Engineering of Heterotypic Antigens on a DNA Framework for the Preparation of Mosaic Nanoparticle Vaccines with Enhanced Immune Activation against SARS‐CoV‐2 Variants
Zhang J, Xu Y, Chen M, Wang S, Lin G, Huang Y, Yang C, Yang Y, Song Y. Spatial Engineering of Heterotypic Antigens on a DNA Framework for the Preparation of Mosaic Nanoparticle Vaccines with Enhanced Immune Activation against SARS‐CoV‐2 Variants. Angewandte Chemie International Edition 2024, 63: e202412294. PMID: 39030890, DOI: 10.1002/anie.202412294.Peer-Reviewed Original ResearchNanoparticle vaccineReceptor-binding domainHeterotypic antigensBroad-spectrum neutralizing antibodiesSARS-CoV-2 spike trimerVaccine-induced immunityNanotechnology-based strategiesEnhanced immune activationOmicron receptor-binding domainMosaic vaccinesImmune activationSystematic in vitroNeutralizing antibodiesSARS-CoV-2 variantsMosaic nanoparticlesImmunological investigationsExcessive inflammationAntigen distributionAntigenSpike trimerRBD antigenSARS-CoV-2DNAVaccineAntiviral capabilitiesSpatial Engineering of Heterotypic Antigens on a DNA Framework for the Preparation of Mosaic Nanoparticle Vaccines with Enhanced Immune Activation against SARS‐CoV‐2 Variants
Zhang J, Xu Y, Chen M, Wang S, Lin G, Huang Y, Yang C, Yang Y, Song Y. Spatial Engineering of Heterotypic Antigens on a DNA Framework for the Preparation of Mosaic Nanoparticle Vaccines with Enhanced Immune Activation against SARS‐CoV‐2 Variants. Angewandte Chemie 2024, 136 DOI: 10.1002/ange.202412294.Peer-Reviewed Original ResearchNanoparticle vaccineReceptor-binding domainHeterotypic antigensBroad-spectrum neutralizing antibodiesSARS-CoV-2 spike trimerVaccine-induced immunityNanotechnology-based strategiesEnhanced immune activationOmicron receptor-binding domainMosaic vaccinesImmune activationSystematic in vitroNeutralizing antibodiesSARS-CoV-2 variantsMosaic nanoparticlesImmunological investigationsExcessive inflammationAntigen distributionAntigenSpike trimerRBD antigenSARS-CoV-2DNAVaccineAntiviral capabilitiesTherapeutic nanobodies against SARS-CoV-2 and other pathogenic human coronaviruses
Yang Y, Li F, Du L. Therapeutic nanobodies against SARS-CoV-2 and other pathogenic human coronaviruses. Journal Of Nanobiotechnology 2024, 22: 304. PMID: 38822339, PMCID: PMC11140877, DOI: 10.1186/s12951-024-02573-7.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibodies, NeutralizingAntibodies, ViralBetacoronavirusCoronavirus InfectionsCOVID-19HumansMiddle East Respiratory Syndrome CoronavirusPandemicsPneumonia, ViralSARS-CoV-2Severe acute respiratory syndrome-related coronavirusSingle-Domain AntibodiesSpike Glycoprotein, CoronavirusVirus InternalizationConceptsReceptor-binding domainPathogenic human CoVsHeavy-chain antibodiesSARS-CoV-2Development of nanobiotechnologiesPathogenic human coronavirusesSingle-domain antibodiesSARS-CoV-2 variantsS proteinViral entry processHuman CoVsViral spikeReemerging pathogensEvaluation of therapeutic agentsSARS-CoVVirus pathogenesisVariable domainsNanobodiesViral structuresPandemic potentialMERS-CoVPathogenic coronavirusesViral entryBinding affinityHuman coronavirusesSPIKENET: An Evidence-Based Therapy for Long COVID
Elumalai N, Hussain H, Sampath N, Shamaladevi N, Hajjar R, Druyan B, Rashed A, Ramamoorthy R, Kenyon N, Jayakumar A, Paidas M. SPIKENET: An Evidence-Based Therapy for Long COVID. Viruses 2024, 16: 838. PMID: 38932130, PMCID: PMC11209161, DOI: 10.3390/v16060838.Peer-Reviewed Original ResearchCarcinoembryonic antigen-related cell adhesion molecule 1Murine hepatitis virus-1Post-acute sequelae of COVID-19SARS-CoV-2 variantsSARS-CoV-2Development of severe inflammationCell adhesion molecule 1Long-term complicationsAdhesion molecule 1Multiple organ damagePotential therapeutic benefitMultiple SARS-CoV-2 variantsEvidence-based therapiesSequelae of COVID-19ACE2 receptor-binding domainSevere acute respiratory syndrome coronavirus 2Acute respiratory syndrome coronavirus 2Severe inflammationTissue edemaOrgan damageRespiratory syndrome coronavirus 2Long COVIDMolecule 1Receptor-binding domainSyndrome coronavirus 2
2023
Distinguishing SARS-CoV-2 infection and vaccine responses up to 18 months post-infection using nucleocapsid protein and receptor-binding domain antibodies
Jarlhelt I, Pérez-Alós L, Bayarri-Olmos R, Hansen C, Petersen M, Weihe P, Armenteros J, Madsen J, Nielsen J, Hilsted L, Iversen K, Bundgaard H, Nielsen S, Garred P. Distinguishing SARS-CoV-2 infection and vaccine responses up to 18 months post-infection using nucleocapsid protein and receptor-binding domain antibodies. Microbiology Spectrum 2023, 11: e01796-23. PMID: 37738355, PMCID: PMC10580960, DOI: 10.1128/spectrum.01796-23.Peer-Reviewed Original ResearchSARS-CoV-2 infectionLong-term humoral immunitySARS-CoV-2 IgCOVID-19 vaccineInfection-induced immunityAntibody responseReceptor-binding domainSARS-CoV-2Viral spike proteinHumoral immunityImmune responseSARS-CoV-2 antibody responseInfected individualsInfection-induced immune responsesReceptor-binding domain antibodiesSpecific IgLong-term immune responseDurability of immunitySpike proteinProtective antibody responsesSandwich ELISACOVID-19 infectionGeneralized mixed modelNew significant increaseS proteinDesigning and developing a sensitive and specific SARS-CoV-2 RBD IgG detection kit for identifying positive human samples
Raoufi E, Hosseini F, Onagh B, Salehi-Shadkami M, Mehrali M, Mohsenzadegan M, Ho J, Bigdelou B, Sepand M, Webster T, Zanganeh S, Farajollahi M. Designing and developing a sensitive and specific SARS-CoV-2 RBD IgG detection kit for identifying positive human samples. Clinica Chimica Acta 2023, 542: 117279. PMID: 36871661, PMCID: PMC9985519, DOI: 10.1016/j.cca.2023.117279.Peer-Reviewed Original ResearchConceptsReceptor-binding domainPichia pastorisIon-exchange chromatographyShake flask cultivationRecombinant receptor-binding domainSARS-CoV-2 spike proteinBioreactor cultivationsIndirect enzyme-linked immunoassayBinding domainSARS-CoV-2Target proteinsProtein productionTarget genesAntigenic regionsEnzyme-linked immunoassaySpike proteinProteinReceptor binding domain antigensDetection kitEpitope analysisHuman samplesEnzyme-linked immunoassay testImmunological developmentCultivationHuman serum
2022
Molecular basis for antiviral activity of two pediatric neutralizing antibodies targeting SARS-CoV-2 Spike RBD
Chen Y, Prévost J, Ullah I, Romero H, Lisi V, Tolbert W, Grover J, Ding S, Gong S, Beaudoin-Bussières G, Gasser R, Benlarbi M, Vézina D, Anand S, Chatterjee D, Goyette G, Grunst M, Yang Z, Bo Y, Zhou F, Béland K, Bai X, Zeher A, Huang R, Nguyen D, Sherburn R, Wu D, Piszczek G, Paré B, Matthies D, Xia D, Richard J, Kumar P, Mothes W, Côté M, Uchil P, Lavallée V, Smith M, Pazgier M, Haddad E, Finzi A. Molecular basis for antiviral activity of two pediatric neutralizing antibodies targeting SARS-CoV-2 Spike RBD. IScience 2022, 26: 105783. PMID: 36514310, PMCID: PMC9733284, DOI: 10.1016/j.isci.2022.105783.Peer-Reviewed Original ResearchReceptor-binding domainSARS-CoV-2 patientsK18-hACE2 micePlasma neutralization activitySARS-CoV-2 variantsSARS-CoV-2 spike receptor-binding domainSpike receptor-binding domainProphylactic administrationNAb responsesPediatric patientsPotent NAbsLethal challengeNeutralizing antibodiesNeutralization activityDelta VOCEffector activityAntiviral mechanismAntiviral activityClinical interventionsPatientsNAbsAntibodiesEpitopesMolecular determinantsMolecular basisSupported Natural Membranes on Microspheres for Protein–Protein Interaction Studies
Cheppali S, Dharan R, Katzenelson R, Sorkin R. Supported Natural Membranes on Microspheres for Protein–Protein Interaction Studies. ACS Applied Materials & Interfaces 2022, 14: 49532-49541. PMID: 36306148, DOI: 10.1021/acsami.2c13095.Peer-Reviewed Original ResearchMembrane proteinsProtein-protein interaction studiesPlasma membraneMembrane-related biological processesProtein-membrane interaction studiesSpike proteinEukaryotic plasma membraneProtein of SARS-CoV-2Cell-cell communicationSpike protein of SARS-CoV-2Interaction studiesReceptor-binding domainBinding domainMembrane biologyBiological processesNatural membranesMembrane model systemsMembrane componentsMembrane bilayerNative membrane componentsProteinExtracellular vesiclesCorrect orientationBiophysical questionsHuman receptorLRRC15 inhibits SARS-CoV-2 cellular entry in trans
Song J, Chow RD, Peña-Hernández MA, Zhang L, Loeb SA, So EY, Liang OD, Ren P, Chen S, Wilen CB, Lee S. LRRC15 inhibits SARS-CoV-2 cellular entry in trans. PLOS Biology 2022, 20: e3001805. PMID: 36228039, PMCID: PMC9595563, DOI: 10.1371/journal.pbio.3001805.Peer-Reviewed Original ResearchConceptsExpression of LRRC15Receptor-binding domainViral entryAcute respiratory syndrome coronavirus 2 infectionSevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infectionSARS-CoV-2 cellular entrySyndrome coronavirus 2 infectionSARS-CoV-2 entrySpike-mediated entryCoronavirus 2 infectionCOVID-19 patientsCellular entry factorsSARS-CoV-2Attachment factorsACE2-negative cellsEnzyme 2Receptor angiotensinEntry factorsProtective roleLRRC15Spike proteinSame cell typeCRISPR activation screensACE2Cellular entry
2021
Structural basis and mode of action for two broadly neutralizing antibodies against SARS-CoV-2 emerging variants of concern
Li W, Chen Y, Prévost J, Ullah I, Lu M, Gong SY, Tauzin A, Gasser R, Vézina D, Anand SP, Goyette G, Chaterjee D, Ding S, Tolbert WD, Grunst MW, Bo Y, Zhang S, Richard J, Zhou F, Huang RK, Esser L, Zeher A, Côté M, Kumar P, Sodroski J, Xia D, Uchil PD, Pazgier M, Finzi A, Mothes W. Structural basis and mode of action for two broadly neutralizing antibodies against SARS-CoV-2 emerging variants of concern. Cell Reports 2021, 38: 110210. PMID: 34971573, PMCID: PMC8673750, DOI: 10.1016/j.celrep.2021.110210.Peer-Reviewed Original ResearchVariants of concernProtective immune responseReceptor-binding domainImmune responseImmunogen designSevere acute respiratory syndrome coronavirus 2Acute respiratory syndrome coronavirus 2Respiratory syndrome coronavirus 2Syndrome coronavirus 2Mode of actionSARS-CoV-2 spikeSARS-CoV-2Vaccine immunogen designAntibody therapyCoronavirus 2Β-coronavirusMonoclonal antibodiesS1 subunitS2 subunitAntibodiesTherapyVariantsSARS-CoV-2 Antibodies Mediate Complement and Cellular Driven Inflammation
Jarlhelt I, Nielsen S, Jahn C, Hansen C, Pérez-Alós L, Rosbjerg A, Bayarri-Olmos R, Skjoedt M, Garred P. SARS-CoV-2 Antibodies Mediate Complement and Cellular Driven Inflammation. Frontiers In Immunology 2021, 12: 767981. PMID: 34804055, PMCID: PMC8596567, DOI: 10.3389/fimmu.2021.767981.Peer-Reviewed Original ResearchConceptsSARS-CoV-2-specific antibodiesSARS-CoV-2 receptor-binding domainReceptor-binding domainComplement activationAntibody responseInflammatory responseSARS-CoV-2 antibody responseDisease severitySevere acute respiratory syndrome coronavirus 2Fc gamma receptor engagementAcute respiratory syndrome coronavirus 2COVID-19 disease severitySARS-CoV-2 antibodiesSARS-CoV-2 infectionRespiratory syndrome coronavirus 2Pro-inflammatory cytokines TNFAntibody-mediated complement activationProminent complement activationSpecific antibodiesSyndrome coronavirus 2COVID-19 severitySerious public health threatCoronavirus disease 2019Classical complement pathway activationClassical complement activationSARS-CoV-2 Neutralizing Antibody Responses towards Full-Length Spike Protein and the Receptor-Binding Domain
Bayarri-Olmos R, Idorn M, Rosbjerg A, Pérez-Alós L, Hansen C, Johnsen L, Helgstrand C, Zosel F, Bjelke J, Öberg F, Søgaard M, Paludan S, Bak-Thomsen T, Jardine J, Skjoedt M, Garred P. SARS-CoV-2 Neutralizing Antibody Responses towards Full-Length Spike Protein and the Receptor-Binding Domain. The Journal Of Immunology 2021, 207: 878-887. PMID: 34301847, DOI: 10.4049/jimmunol.2100272.Peer-Reviewed Original ResearchMeSH KeywordsAngiotensin-Converting Enzyme 2AnimalsAntibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralAntigens, ViralCoronavirus Nucleocapsid ProteinsCOVID-19COVID-19 SerotherapyCOVID-19 VaccinesEnzyme-Linked Immunosorbent AssayHumansImmunizationImmunization, PassiveImmunoglobulin AImmunoglobulin GImmunoglobulin MMiceNeutralization TestsProtein DomainsReceptors, VirusSARS-CoV-2Spike Glycoprotein, CoronavirusConceptsPlaque reduction neutralization testReceptor-binding domainReduction neutralization testNeutralization testFull-length spike proteinSARS-CoV-2 transmissionSARS-CoV-2 receptor-binding domainViral neutralization testSARS-CoV-2Levels of AbsIgG titersVaccine strategiesAntibody responsePreclinical modelsConvalescent seraImmune responseMouse modelNeutralization potencyVirus neutralizationFull spikesImmunization strategiesMurine mAbsImmunization resultsSpike proteinELISACD209L/L-SIGN and CD209/DC-SIGN Act as Receptors for SARS-CoV‑2
Amraei R, Yin W, Napoleon M, Suder E, Berrigan J, Zhao Q, Olejnik J, Chandler K, Xia C, Feldman J, Hauser B, Caradonna T, Schmidt A, Gummuluru S, Mühlberger E, Chitalia V, Costello C, Rahimi N. CD209L/L-SIGN and CD209/DC-SIGN Act as Receptors for SARS-CoV‑2. ACS Central Science 2021, 7: 1156-1165. PMID: 34341769, PMCID: PMC8265543, DOI: 10.1021/acscentsci.0c01537.Peer-Reviewed Original ResearchSARS-CoV-2 spike receptor-binding domainSARS-CoV-2SARS-CoV-2 entryL-SIGNSARS-CoV-2 infectionCD209/DC-SIGNSpike receptor-binding domainAntiviral drug developmentReceptor-binding domainCell typesHuman endothelial cellsDC-SIGNAlternative receptorLow expressionEndothelial cellsImmunofluorescence stainingCD209Virus entryACE2Disease-relevant cell typesProminent expressionCD209LKidney epitheliumReceptorsDrug developmentSARS-CoV-2 exacerbates proinflammatory responses in myeloid cells through C-type lectin receptors and Tweety family member 2
Lu Q, Liu J, Zhao S, Gomez Castro MF, Laurent-Rolle M, Dong J, Ran X, Damani-Yokota P, Tang H, Karakousi T, Son J, Kaczmarek ME, Zhang Z, Yeung ST, McCune BT, Chen RE, Tang F, Ren X, Chen X, Hsu JCC, Teplova M, Huang B, Deng H, Long Z, Mudianto T, Jin S, Lin P, Du J, Zang R, Su TT, Herrera A, Zhou M, Yan R, Cui J, Zhu J, Zhou Q, Wang T, Ma J, Koralov SB, Zhang Z, Aifantis I, Segal LN, Diamond MS, Khanna KM, Stapleford KA, Cresswell P, Liu Y, Ding S, Xie Q, Wang J. SARS-CoV-2 exacerbates proinflammatory responses in myeloid cells through C-type lectin receptors and Tweety family member 2. Immunity 2021, 54: 1304-1319.e9. PMID: 34048708, PMCID: PMC8106883, DOI: 10.1016/j.immuni.2021.05.006.Peer-Reviewed Original ResearchMeSH KeywordsAngiotensin-Converting Enzyme 2Binding SitesCell LineCOVID-19CytokinesGene Expression RegulationHost-Pathogen InteractionsHumansInflammation MediatorsLectins, C-TypeMembrane ProteinsModels, MolecularMyeloid CellsNeoplasm ProteinsProtein BindingProtein ConformationSARS-CoV-2Single-Domain AntibodiesSpike Glycoprotein, CoronavirusStructure-Activity RelationshipConceptsSARS-CoV-2Proinflammatory responseMyeloid cellsFamily member 2Robust proinflammatory responseC-type lectin receptorsCOVID-19 therapyCOVID-19 severityMember 2SARS-CoV-2 spikeCoronavirus disease 2019Single-cell RNA sequencing analysisReceptor-binding domainImmune hyperactivationImmune cellsDisease 2019Enzyme 2Pulmonary cellsC-type lectinRNA sequencing analysisCanonical receptorLectin receptorsPotential targetPredominant expressionReceptor interactionA Single Immunization with Spike-Functionalized Ferritin Vaccines Elicits Neutralizing Antibody Responses against SARS-CoV‑2 in Mice
Powell A, Zhang K, Sanyal M, Tang S, Weidenbacher P, Li S, Pham T, Pak J, Chiu W, Kim P. A Single Immunization with Spike-Functionalized Ferritin Vaccines Elicits Neutralizing Antibody Responses against SARS-CoV‑2 in Mice. ACS Central Science 2021, 7: 183-199. PMID: 33527087, PMCID: PMC7805605, DOI: 10.1021/acscentsci.0c01405.Peer-Reviewed Original ResearchSARS-CoV-2 spikeSelf-assembling ferritin nanoparticlesElicitation of neutralizing antibodiesFerritin-based vaccinesReceptor-binding domainSARS-CoV-2 vaccinesSingle-dose vaccinationImmunization of miceSubunit vaccine candidateVaccine elicitationCOVID-19 patientsEffective SARS-CoV-2 vaccineNeutralization titersClinical trialsConvalescent plasmaPublic health prioritySpike receptor-binding domainAntibody responseNanoparticle platformPseudovirus assayVaccine candidatesMonoclonal antibodiesSARS-CoV-2Ferritin nanoparticlesMiceSARS-CoV-2 Antibody Responses Are Correlated to Disease Severity in COVID-19 Convalescent Individuals
Hansen C, Jarlhelt I, Pérez-Alós L, Hummelshøj Landsy L, Loftager M, Rosbjerg A, Helgstrand C, Bjelke J, Egebjerg T, Jardine J, Sværke Jørgensen C, Iversen K, Bayarri-Olmos R, Garred P, Skjoedt M. SARS-CoV-2 Antibody Responses Are Correlated to Disease Severity in COVID-19 Convalescent Individuals. The Journal Of Immunology 2021, 206: ji2000898. PMID: 33208457, DOI: 10.4049/jimmunol.2000898.Peer-Reviewed Original ResearchMeSH KeywordsAdolescentAdultAgedAged, 80 and overAntibodies, NeutralizingAntibodies, ViralConvalescenceCOVID-19Enzyme-Linked Immunosorbent AssayFemaleHumansImmunoglobulin AImmunoglobulin GImmunoglobulin MMaleMiddle AgedReverse Transcriptase Polymerase Chain ReactionSARS-CoV-2Severity of Illness IndexYoung AdultConceptsReceptor-binding domainAb responsesSARS-CoV-2 antibody responseDisease severitySARS-CoV-2 AbsPrevious COVID-19 infectionCOVID-19 convalescent individualsFuture vaccination strategiesCOVID-19 infectionCOVID-19 immunityConvalescent individualsAntibody responseVaccination strategiesLarge population screeningPopulation screeningSandwich ELISAHealthcare systemCOVID-19 pandemicDiagnostic toolELISASeverityAssaysResponseDepth diagnosticsPathogenesisThe SARS-CoV-2 Y453F mink variant displays a pronounced increase in ACE-2 affinity but does not challenge antibody neutralization
Bayarri-Olmos R, Rosbjerg A, Johnsen L, Helgstrand C, Bak-Thomsen T, Garred P, Skjoedt M. The SARS-CoV-2 Y453F mink variant displays a pronounced increase in ACE-2 affinity but does not challenge antibody neutralization. Journal Of Biological Chemistry 2021, 296: 100536. PMID: 33716040, PMCID: PMC7948531, DOI: 10.1016/j.jbc.2021.100536.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SubstitutionAngiotensin-Converting Enzyme 2AnimalsAntibodies, NeutralizingAntibodies, ViralConvalescenceCOVID-19DenmarkGene ExpressionHEK293 CellsHost-Pathogen InteractionsHumansImmune SeraImmunity, InnateMinkModels, MolecularMutationPandemicsProtein BindingProtein Structure, SecondaryRecombinant ProteinsSARS-CoV-2Spike Glycoprotein, CoronavirusVirus InternalizationConceptsReceptor-binding domainSevere acute respiratory syndrome coronavirus 2Angiotensin-converting enzyme 2 receptorAcute respiratory syndrome coronavirus 2Respiratory syndrome coronavirus 2Human angiotensin-converting enzyme 2 (ACE2) receptorPotential immune evasionSyndrome coronavirus 2Enzyme 2 (ACE2) receptorSpike gene mutationsBiolayer interferometry analysisVaccine strategiesCoronavirus 2Humoral immunityAntibody responseViral controlImmune responseMouse modelImmune evasionAntibody neutralizationReceptor adaptationOriginal WuhanSpike proteinGene mutationsGenetic variants
2020
The kinetics of humoral response and its relationship with the disease severity in COVID-19
Ren L, Zhang L, Chang D, Wang J, Hu Y, Chen H, Guo L, Wu C, Wang C, Wang Y, Wang Y, Wang G, Yang S, Dela Cruz CS, Sharma L, Wang L, Zhang D, Wang J. The kinetics of humoral response and its relationship with the disease severity in COVID-19. Communications Biology 2020, 3: 780. PMID: 33311543, PMCID: PMC7733479, DOI: 10.1038/s42003-020-01526-8.Peer-Reviewed Original ResearchConceptsHumoral responseDisease severityReceptor-binding domainAntibody titersSpike proteinSevere acute respiratory syndrome coronavirus 2Acute respiratory syndrome coronavirus 2COVID-19Respiratory syndrome coronavirus 2Titers of NAbsGeometric mean titersCOVID-19 patientsSyndrome coronavirus 2Coronavirus disease 2019Disease courseMean titersCoronavirus 2Antibody responseIgG antibodiesRisk factorsIg levelsImmunoglobulin ADisease 2019Severe casesModerate infections
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