2024
30 years of HIV therapy: Current and future antiviral drug targets
Nuwagaba J, Li J, Ngo B, Sutton R. 30 years of HIV therapy: Current and future antiviral drug targets. Virology 2024, 603: 110362. PMID: 39705895, PMCID: PMC11788039, DOI: 10.1016/j.virol.2024.110362.Peer-Reviewed Original ResearchConceptsHIV-1HIV-1 cureCCR5 co-receptorInhibit HIV-1 replicationHIV-1 RNAHIV-1 replicationTarget reverse transcriptaseHIV-1 TatViral long terminal repeatFunctional cureAntiretroviral therapyHIV therapyNovel therapiesDrug resistanceLong terminal repeatDrug interactionsTherapeutic strategiesTherapeutic gapLifelong adherenceCo-receptorViral entryTherapyHAARTReverse transcriptaseDrugTherapeutic 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 coronavirusesA naturally isolated symbiotic bacterium suppresses flavivirus transmission by Aedes mosquitoes
Zhang L, Wang D, Shi P, Li J, Niu J, Chen J, Wang G, Wu L, Chen L, Yang Z, Li S, Meng J, Ruan F, He Y, Zhao H, Ren Z, Wang Y, Liu Y, Shi X, Wang Y, Liu Q, Li J, Wang P, Wang J, Zhu Y, Cheng G. A naturally isolated symbiotic bacterium suppresses flavivirus transmission by Aedes mosquitoes. Science 2024, 384: eadn9524. PMID: 38669573, DOI: 10.1126/science.adn9524.Peer-Reviewed Original ResearchConceptsColony forming unitsFlavivirus envelope proteinCommensal microbiotaIrreversible conformational changesGlucose dehydrogenaseMosquito gutConformational changesGut lumenPrevent viral infectionGutBacteriumFlavivirus transmissionEnvelope proteinsVector competencePrevent viral entryViral entryRefractory to infectionDengue virusForming unitsField mosquitoesTransmission of dengue virusFlavivirusesMosquitoesSemifield conditionsAdult mosquitoes
2023
The KDM6A-KMT2D-p300 axis regulates susceptibility to diverse coronaviruses by mediating viral receptor expression
Wei J, Alfajaro M, Cai W, Graziano V, Strine M, Filler R, Biering S, Sarnik S, Patel S, Menasche B, Compton S, Konermann S, Hsu P, Orchard R, Yan Q, Wilen C. The KDM6A-KMT2D-p300 axis regulates susceptibility to diverse coronaviruses by mediating viral receptor expression. PLOS Pathogens 2023, 19: e1011351. PMID: 37410700, PMCID: PMC10325096, DOI: 10.1371/journal.ppat.1011351.Peer-Reviewed Original ResearchConceptsMouse hepatitis virusReceptor expressionTherapeutic targetMERS-CoVMajor SARS-CoV-2 variantsPrimary human airwaySARS-CoV-2 variantsNovel therapeutic targetViral receptor expressionSARS-CoV-2Histone methyltransferase KMT2DIntestinal epithelial cellsCoronavirus SusceptibilityDiverse coronavirusesHistone demethylase KDM6ADPP4 expressionCoronavirus receptorsHost determinantsHepatitis virusHuman airwaysSARS-CoVSmall molecule inhibitionViral entryPotential drug targetsViral receptorsTemsavir blocks the immunomodulatory activities of HIV-1 soluble gp120
Richard J, Prévost J, Bourassa C, Brassard N, Boutin M, Benlarbi M, Goyette G, Medjahed H, Gendron-Lepage G, Gaudette F, Chen H, Tolbert W, Smith A, Pazgier M, Dubé M, Clark A, Mothes W, Kaufmann D, Finzi A. Temsavir blocks the immunomodulatory activities of HIV-1 soluble gp120. Cell Chemical Biology 2023, 30: 540-552.e6. PMID: 36958337, PMCID: PMC10198848, DOI: 10.1016/j.chembiol.2023.03.003.Peer-Reviewed Original ResearchConceptsAntibody-dependent cellular cytotoxicityUninfected bystander CD4Gp120-CD4 interactionCytokine burstBystander CD4Immunomodulatory activityMultiple immune cellsHIV-1 attachment inhibitorsOverall antigenicityADCC responsesClinical benefitSoluble gp120Immune cellsCellular cytotoxicityAttachment inhibitorsCD4 interactionGp120 bindsCD4Gp120Viral entryEnvelope glycoproteinCD4 downregulationTemsavirCellsAntigenicitySARS-CoV-2 leverages airway epithelial protective mechanism for viral infection
Greaney A, Raredon M, Kochugaeva M, Niklason L, Levchenko A. SARS-CoV-2 leverages airway epithelial protective mechanism for viral infection. IScience 2023, 26: 106175. PMID: 36788793, PMCID: PMC9912025, DOI: 10.1016/j.isci.2023.106175.Peer-Reviewed Original ResearchSingle-cell RNA sequencing datasetsCell-cell communicationRNA sequencing datasetsViral infectionSevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2) viral infectionEarly SARS-CoV-2 infectionSequencing datasetsSARS-CoV-2 infectionRepair mechanismsEarly viral entryTissue repair mechanismsMature ciliated cellsAlternative therapeutic approachSARS-CoV-2 virusResponse mechanismsFeedforward loopCell precursorsRapid differentiationViral entryBronchial epitheliumTherapeutic approachesBarrier tissuesKey mechanismCiliated cellsInfection
2022
LRRC15 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 entryTargeted protein S-nitrosylation of ACE2 inhibits SARS-CoV-2 infection
Oh C, Nakamura T, Beutler N, Zhang X, Piña-Crespo J, Talantova M, Ghatak S, Trudler D, Carnevale L, McKercher S, Bakowski M, Diedrich J, Roberts A, Woods A, Chi V, Gupta A, Rosenfeld M, Kearns F, Casalino L, Shaabani N, Liu H, Wilson I, Amaro R, Burton D, Yates J, Becker C, Rogers T, Chatterjee A, Lipton S. Targeted protein S-nitrosylation of ACE2 inhibits SARS-CoV-2 infection. Nature Chemical Biology 2022, 19: 275-283. PMID: 36175661, PMCID: PMC10127945, DOI: 10.1038/s41589-022-01149-6.Peer-Reviewed Original ResearchConceptsSARS-CoV-2 infectionViral entrySevere acute respiratory syndrome coronavirus 2Acute respiratory syndrome coronavirus 2Respiratory syndrome coronavirus 2Coronavirus disease 2019 (COVID-19) pandemicSyndrome coronavirus 2Prevention of infectionSARS-CoV-2 spike proteinDisease 2019 pandemicSpread of infectionCoronavirus 2Channel blockadeS-nitrosylationEnzyme 2Binding of ACE2InfectionSpike proteinACE2Envelope proteinProtein S-nitrosylationIon channelsNon-toxic compoundsNovel avenuesAngiotensinVE607 stabilizes SARS-CoV-2 Spike in the “RBD-up” conformation and inhibits viral entry
Ding S, Ullah I, Gong SY, Grover J, Mohammadi M, Chen Y, Vézina D, Beaudoin-Bussières G, Verma VT, Goyette G, Gaudette F, Richard J, Yang D, Smith AB, Pazgier M, Côté M, Abrams C, Kumar P, Mothes W, Uchil P, Finzi A, Baron C. VE607 stabilizes SARS-CoV-2 Spike in the “RBD-up” conformation and inhibits viral entry. IScience 2022, 25: 104528. PMID: 35677392, PMCID: PMC9164512, DOI: 10.1016/j.isci.2022.104528.Peer-Reviewed Original ResearchSARS-CoV-2 infectionAuthentic SARS-CoV-2K18-hACE2 miceS-ACE2 interactionsDevelopment of immunotherapySARS-CoV-2 spikeSARS-CoV-2SARS-CoV-1Prophylactic treatmentLow micromolar concentrationsViral replicationACE2 receptorPseudoviral particlesViral entrySpike glycoproteinPotential targetCOVID-19Drug developmentInfectionACE2 interfaceHost cellsMicromolar concentrationsReceptorsTreatmentRBDSemi-Mechanistic Pharmacokinetic-Pharmacodynamic Model of Camostat Mesylate-Predicted Efficacy against SARS-CoV-2 in COVID-19
Kosinsky Y, Peskov K, Stanski DR, Wetmore D, Vinetz J. Semi-Mechanistic Pharmacokinetic-Pharmacodynamic Model of Camostat Mesylate-Predicted Efficacy against SARS-CoV-2 in COVID-19. Microbiology Spectrum 2022, 10: e02167-21. PMID: 35412356, PMCID: PMC9047529, DOI: 10.1128/spectrum.02167-21.Peer-Reviewed Original ResearchConceptsFOY-251SARS-CoV-2 cell entryCamostat mesylateInhibition of TMPRSS2Viral loadClinical trialsCOVID-19Viral entrySerine protease inhibitorSpike proteinCell entryMultiple clinical trialsPharmacokinetic-pharmacodynamic modelSARS-CoV-2 viral entryPK/PDSARS-CoV-2Protease inhibitorsOne-compartmentCell surface serine proteaseViral entry inhibitionTMPRSS2 inhibitionViral surface spike proteinsAcute exacerbationSemi-mechanistic pharmacokinetic-pharmacodynamic modelsSARS-CoV-2 coronavirusExtracellular vimentin is an attachment factor that facilitates SARS-CoV-2 entry into human endothelial cells
Amraei R, Xia C, Olejnik J, White M, Napoleon M, Lotfollahzadeh S, Hauser B, Schmidt A, Chitalia V, Mühlberger E, Costello C, Rahimi N. Extracellular vimentin is an attachment factor that facilitates SARS-CoV-2 entry into human endothelial cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 119: e2113874119. PMID: 35078919, PMCID: PMC8833221, DOI: 10.1073/pnas.2113874119.Peer-Reviewed Original ResearchConceptsSARS-CoV-2 infectionHuman endothelial cellsSARS-CoV-2 entrySARS-CoV-2S-protein interactionEndothelial cellsIdentification of vimentinShRNA-mediated knockdownIntermediate filament proteinsBinding of vimentinHEK-293 cellsAttachment factorsViral entrySARS-CoV-2 S proteinDevelopment of therapeuticsExtracellular vimentinS protein receptorInfectious SARS-CoV-2Host cellsCellular componentsCoexpression of vimentinFilament proteinsPrimary entry receptorSARS-CoV-2 spike proteinS protein
2021
Investigating Lipid-Modulating Agents for Prevention or Treatment of COVID-19 JACC State-of-the-Art Review
Talasaz AH, Sadeghipour P, Aghakouchakzadeh M, Dreyfus I, Kakavand H, Ariannejad H, Gupta A, Madhavan MV, Van Tassell BW, Jimenez D, Monreal M, Vaduganathan M, Fanikos J, Dixon DL, Piazza G, Parikh SA, Bhatt DL, Lip GYH, Stone GW, Krumholz HM, Libby P, Goldhaber SZ, Bikdeli B. Investigating Lipid-Modulating Agents for Prevention or Treatment of COVID-19 JACC State-of-the-Art Review. Journal Of The American College Of Cardiology 2021, 78: 1635-1654. PMID: 34649702, PMCID: PMC8504484, DOI: 10.1016/j.jacc.2021.08.021.Peer-Reviewed Original ResearchConceptsLipid-modulating agentsEndothelial activationLow high-density lipoprotein cholesterolCOVID-19High-density lipoprotein cholesterolLipid modulating agentsHigh triglyceride levelsMultiorgan manifestationsStatin trialsLipoprotein cholesterolSystemic inflammationTriglyceride levelsJACC StateWorse outcomesInflammatory responsePatient managementRCTsCoronavirus diseaseViral entrySystematic searchLipid raft disruptionTrialsPatientsRaft disruptionPreventionFunctional landscape of SARS-CoV-2 cellular restriction
Martin-Sancho L, Lewinski MK, Pache L, Stoneham CA, Yin X, Becker ME, Pratt D, Churas C, Rosenthal SB, Liu S, Weston S, De Jesus PD, O'Neill AM, Gounder AP, Nguyen C, Pu Y, Curry HM, Oom AL, Miorin L, Rodriguez-Frandsen A, Zheng F, Wu C, Xiong Y, Urbanowski M, Shaw ML, Chang MW, Benner C, Hope TJ, Frieman MB, García-Sastre A, Ideker T, Hultquist JF, Guatelli J, Chanda SK. Functional landscape of SARS-CoV-2 cellular restriction. Molecular Cell 2021, 81: 2656-2668.e8. PMID: 33930332, PMCID: PMC8043580, DOI: 10.1016/j.molcel.2021.04.008.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, CDBinding SitesCell Line, TumorChlorocebus aethiopsEndoplasmic ReticulumGene Expression RegulationGolgi ApparatusGPI-Linked ProteinsHEK293 CellsHost-Pathogen InteractionsHumansImmunity, InnateInterferon Regulatory FactorsInterferon Type IMolecular Docking SimulationProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsSARS-CoV-2Signal TransductionVero CellsViral ProteinsVirus InternalizationVirus ReleaseVirus ReplicationConceptsAcute respiratory syndrome coronavirus 2 infectionSevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infectionSARS-CoV-1 infectionSyndrome coronavirus 2 infectionSevere coronavirus disease 2019SARS-CoV-2 infectionCoronavirus 2 infectionInnate immune controlCoronavirus disease 2019Potential therapeutic strategySARS-CoV-2BST2/tetherinImmune controlSet of ISGsDisease 2019Host determinantsTherapeutic strategiesViral infectionAntiviral ISGsDisease severityViral replicationInterferon responseViral entryIFN controlInfection
2020
Real-Time Conformational Dynamics of SARS-CoV-2 Spikes on Virus Particles
Lu M, Uchil PD, Li W, Zheng D, Terry DS, Gorman J, Shi W, Zhang B, Zhou T, Ding S, Gasser R, Prévost J, Beaudoin-Bussières G, Anand SP, Laumaea A, Grover JR, Liu L, Ho DD, Mascola JR, Finzi A, Kwong PD, Blanchard SC, Mothes W. Real-Time Conformational Dynamics of SARS-CoV-2 Spikes on Virus Particles. Cell Host & Microbe 2020, 28: 880-891.e8. PMID: 33242391, PMCID: PMC7664471, DOI: 10.1016/j.chom.2020.11.001.Peer-Reviewed Original ResearchConceptsSingle-molecule fluorescence resonance energy transferReceptor-binding domainSevere acute respiratory syndrome coronavirus 2Acute respiratory syndrome coronavirus 2Respiratory syndrome coronavirus 2Conformational dynamicsSyndrome coronavirus 2SARS-CoV-2 spikeCoronavirus disease 2019Distinct conformational statesMechanism of neutralizationHuman receptor angiotensinVirus particlesConvalescent plasmaCoronavirus 2Disease 2019Enzyme 2Fluorescence resonance energy transferReceptor angiotensinVaccine developmentImmunogen designViral entryConformational changesDistinct conformationsS recognitionCOVID‐19 and the heart: An update for clinicians
Goha A, Mezue K, Edwards P, Nunura F, Baugh D, Madu E. COVID‐19 and the heart: An update for clinicians. Clinical Cardiology 2020, 43: 1216-1222. PMID: 32533585, PMCID: PMC7323229, DOI: 10.1002/clc.23406.Peer-Reviewed Original ResearchConceptsPrognosis of COVID-19 diseaseAdverse cardiac effectsPre-existing cardiovascular diseaseOptimal patient managementAcute myocardial injuryRisk of morbidityAcute coronary syndromeManifestations of COVID-19Cardiovascular manifestations of COVID-19Cardiovascular manifestationsCardiac effectsEffects of medicationVenous thromboembolismCoronary syndromeHeart failureMyocardial injuryPatient managementRAA systemClinical syndromeCardiovascular diseaseViral entrySARS-CoV-2COVID-19 diseaseHeartCOVID-19
2019
Norovirus Attachment and Entry
Graziano VR, Wei J, Wilen CB. Norovirus Attachment and Entry. Viruses 2019, 11: 495. PMID: 31151248, PMCID: PMC6630345, DOI: 10.3390/v11060495.Peer-Reviewed Original ResearchConceptsHisto-blood group antigensNorovirus attachmentMajority of casesMajor human pathogenViral life cycleImmune interactionsViral gastroenteritisCell tropismGroup antigensViral entryKey mediatorHuman norovirusBile saltsViral genome releaseMurine norovirusReceptorsMinor capsid protein VP2Capsid protein VP2Human pathogensMolecular mechanismsNorovirusSignificant determinantsProtein VP2Important future directionsCurrent understandingThe Polar Region of the HIV-1 Envelope Protein Determines Viral Fusion and Infectivity by Stabilizing the gp120-gp41 Association
Lu W, Chen S, Yu J, Behrens R, Wiggins J, Sherer N, Liu S, Xiong Y, Xiang S, Wu L. The Polar Region of the HIV-1 Envelope Protein Determines Viral Fusion and Infectivity by Stabilizing the gp120-gp41 Association. Journal Of Virology 2019, 93: 10.1128/jvi.02128-18. PMID: 30651369, PMCID: PMC6430531, DOI: 10.1128/jvi.02128-18.Peer-Reviewed Original ResearchConceptsHIV-1 fusionHIV-1 infectivityPR mutationsHIV-1 membrane fusionViral entryHIV-1 Env precursorEnv trimersMembrane fusionHIV-1 envelope proteinHIV-1 isolatesViral fusionHIV-1 Env trimersHIV-1 EnvGp120-gp41 associationTransmembrane unitViral envelope glycoproteinsHIV-1Cell-cell fusionViral fusogenicityPolar amino acidsEnv expressionVirus bindingEnvelope glycoproteinFusion inhibitorsTarget cells
2017
Sendai virus recruits cellular villin to remodel actin cytoskeleton during fusion with hepatocytes
Chandra S, Kalaivani R, Kumar M, Srinivasan N, Sarkar D. Sendai virus recruits cellular villin to remodel actin cytoskeleton during fusion with hepatocytes. Molecular Biology Of The Cell 2017, 28: 3801-3814. PMID: 29074568, PMCID: PMC5739296, DOI: 10.1091/mbc.e17-06-0400.Peer-Reviewed Original ResearchConceptsMembrane fusionQuantitative mass spectrometryTwo-dimensional differentialViral envelope glycoproteinsSendai viral envelopesEarly molecular eventsHost cell proteinsActin cytoskeletonThreonine 206Actin dynamicsSendai virusAnimal cellsMolecular eventsCellular membranesHost cellsCell proteinsFusion-mediated deliveryNovel mechanismBiochemical analysisVillinEnvelope glycoproteinGel electrophoresisViral envelopeProteinViral entry
2014
Conformational dynamics of single HIV-1 envelope trimers on the surface of native virions
Munro JB, Gorman J, Ma X, Zhou Z, Arthos J, Burton DR, Koff WC, Courter JR, Smith AB, Kwong PD, Blanchard SC, Mothes W. Conformational dynamics of single HIV-1 envelope trimers on the surface of native virions. Science 2014, 346: 759-763. PMID: 25298114, PMCID: PMC4304640, DOI: 10.1126/science.1254426.Peer-Reviewed Original Research
2010
A C-Type Lectin Collaborates with a CD45 Phosphatase Homolog to Facilitate West Nile Virus Infection of Mosquitoes
Cheng G, Cox J, Wang P, Krishnan MN, Dai J, Qian F, Anderson JF, Fikrig E. A C-Type Lectin Collaborates with a CD45 Phosphatase Homolog to Facilitate West Nile Virus Infection of Mosquitoes. Cell 2010, 142: 714-725. PMID: 20797779, PMCID: PMC2954371, DOI: 10.1016/j.cell.2010.07.038.Peer-Reviewed Original ResearchConceptsWest Nile virusWNV infectionWest Nile virus infectionArthropod-borne flavivirusBlood-feeding processVirus infectionHuman CD45Viral disseminationC-type lectinInfectionViral entryViral attachmentMosquito homologCalcium-dependent mannerNile virusMolecular understandingVivo experimentsSame pathwayNatural vector
This site is protected by hCaptcha and its Privacy Policy and Terms of Service apply