2021
SARS-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 interaction
2015
La Piedad Michoacán Mexico Virus V protein antagonizes type I interferon response by binding STAT2 protein and preventing STATs nuclear translocation
Pisanelli G, Laurent-Rolle M, Manicassamy B, Belicha-Villanueva A, Morrison J, Lozano-Dubernard B, Castro-Peralta F, Iovane G, García-Sastre. A. La Piedad Michoacán Mexico Virus V protein antagonizes type I interferon response by binding STAT2 protein and preventing STATs nuclear translocation. Virus Research 2015, 213: 11-22. PMID: 26546155, PMCID: PMC5538256, DOI: 10.1016/j.virusres.2015.10.027.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell LineHumansInterferon Type IProtein BindingProtein TransportRubulavirusSTAT2 Transcription FactorSwineViral ProteinsConceptsNuclear translocationParamyxoviridae familyIFN α/βSTAT2 proteinRubulavirus genusMost paramyxovirusesV proteinType I interferon responseI interferon responseCellular responsesSTAT2Innate immune responseAmino acidsType I interferonSignificant disease burdenProteinBlue eye diseaseMexico virusInterferon responseProtein levelsSwine cellsIFN responseSTAT1I interferonRespiratory distress
2014
The Interferon Signaling Antagonist Function of Yellow Fever Virus NS5 Protein Is Activated by Type I Interferon
Laurent-Rolle M, Morrison J, Rajsbaum R, Macleod JML, Pisanelli G, Pham A, Ayllon J, Miorin L, Martínez-Romero C, tenOever BR, García-Sastre A. The Interferon Signaling Antagonist Function of Yellow Fever Virus NS5 Protein Is Activated by Type I Interferon. Cell Host & Microbe 2014, 16: 314-327. PMID: 25211074, PMCID: PMC4176702, DOI: 10.1016/j.chom.2014.07.015.Peer-Reviewed Original Research
2013
Dengue Virus Co-opts UBR4 to Degrade STAT2 and Antagonize Type I Interferon Signaling
Morrison J, Laurent-Rolle M, Maestre AM, Rajsbaum R, Pisanelli G, Simon V, Mulder LC, Fernandez-Sesma A, García-Sastre A. Dengue Virus Co-opts UBR4 to Degrade STAT2 and Antagonize Type I Interferon Signaling. PLOS Pathogens 2013, 9: e1003265. PMID: 23555265, PMCID: PMC3610674, DOI: 10.1371/journal.ppat.1003265.Peer-Reviewed Original ResearchConceptsDengue hemorrhagic feverType I interferonDengue feverSTAT2 degradationImmune evasionI interferonDENV NS5Anti-DENV therapeuticsDengue virus infectionDENV NS5 proteinVirus infectionHemorrhagic feverDENV replicationViral replicationAntiviral therapeuticsEfficient viral replicationIFNPotential severityFeverDENVInterferonNS5Competent cellsHost proteinsNS5 protein
2009
NS5 of Dengue Virus Mediates STAT2 Binding and Degradation
Ashour J, Laurent-Rolle M, Shi PY, García-Sastre A. NS5 of Dengue Virus Mediates STAT2 Binding and Degradation. Journal Of Virology 2009, 83: 5408-5418. PMID: 19279106, PMCID: PMC2681973, DOI: 10.1128/jvi.02188-08.Peer-Reviewed Original ResearchConceptsDengue virusInnate immune responseInnate antiviral responseImmune responseInfection resultsIFN responseAntiviral responseDENV proteinsLevel of expressionAntiviral therapeuticsDENV genomeDecreased levelsInterferonPotential targetProtein levelsViral pathogensHost proteasesReduced levelsProteasome activityMultiple mechanismsVirusFacilitate infectionNovel mechanismViral polypeptidesNS5