2024
Dysregulation of FLVCR1a-dependent mitochondrial calcium handling in neural progenitors causes congenital hydrocephalus
Bertino F, Mukherjee D, Bonora M, Bagowski C, Nardelli J, Metani L, Venturini D, Chianese D, Santander N, Salaroglio I, Hentschel A, Quarta E, Genova T, McKinney A, Allocco A, Fiorito V, Petrillo S, Ammirata G, De Giorgio F, Dennis E, Allington G, Maier F, Shoukier M, Gloning K, Munaron L, Mussano F, Salsano E, Pareyson D, di Rocco M, Altruda F, Panagiotakos G, Kahle K, Gressens P, Riganti C, Pinton P, Roos A, Arnold T, Tolosano E, Chiabrando D. Dysregulation of FLVCR1a-dependent mitochondrial calcium handling in neural progenitors causes congenital hydrocephalus. Cell Reports Medicine 2024, 5: 101647. PMID: 39019006, PMCID: PMC11293339, DOI: 10.1016/j.xcrm.2024.101647.Peer-Reviewed Original ResearchConceptsCongenital hydrocephalusCalcium handlingNeural progenitor cellsMitochondrial calcium handlingMouse neural progenitor cellsFLVCR1 geneMitochondrial calcium levelsVentricular dilatationLive birthsCalcium levelsProgenitor cellsClinical challengeVentricle enlargementPathogenetic mechanismsSevere formCortical neurogenesisNeural progenitorsFLVCR1aMitochondria-associated membranesHydrocephalusMiceFLVCR1CH genesMolecular mechanismsMetabolic activity
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 receptors
2022
SARS-CoV-2 Variants Increase Kinetic Stability of Open Spike Conformations as an Evolutionary Strategy
Yang Z, Han Y, Ding S, Shi W, Zhou T, Finzi A, Kwong PD, Mothes W, Lu M. SARS-CoV-2 Variants Increase Kinetic Stability of Open Spike Conformations as an Evolutionary Strategy. MBio 2022, 13: e03227-21. PMID: 35164561, PMCID: PMC8844933, DOI: 10.1128/mbio.03227-21.Peer-Reviewed Original ResearchConceptsSevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variantsAngiotensin-converting enzyme 2 receptorHuman angiotensin-converting enzyme 2 (ACE2) receptorVirus entryEnzyme 2 (ACE2) receptorTarget of antibodiesCOVID-19 vaccineSARS-CoV-2S variantsVirus particlesSARS-CoV-2 adaptationConvalescent patientsAntibody therapyAntibody responseImmune evasionE484KD614GSpike glycoproteinHarbor mutationsHuman hostVaccineS glycoproteinPrimary targetSoluble trimersHACE2
2021
SARS-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 proteinELISAAnimal Models of COVID-19. I. Comparative Virology and Disease Pathogenesis
Zeiss CJ, Compton S, Veenhuis RT. Animal Models of COVID-19. I. Comparative Virology and Disease Pathogenesis. ILAR Journal 2021, 62: ilab007-. PMID: 33836527, PMCID: PMC8083356, DOI: 10.1093/ilar/ilab007.Peer-Reviewed Original ResearchConceptsSARS-CoV-2SARS-CoVViral sheddingImmune responseSpontaneous modelAnimal modelsDisease pathogenesisSARS-CoV-2 infectionCOVID-19Severe acute respiratory syndrome coronavirusAcute respiratory syndrome coronavirusChimeric SARS-CoVRole of comorbiditiesCoronavirus disease 2019 (COVID-19) pandemicShort-term immune responseWild-type miceSeverity of diseaseOrgan-specific pathologySARS-CoV-2 virusDisease 2019 pandemicAfrican green monkeysTest therapeuticsVaccine approachesNonfatal diseaseTissue involvement
2020
Cytidine Monophosphate N-Acetylneuraminic Acid Synthetase and Solute Carrier Family 35 Member A1 Are Required for Reovirus Binding and Infection
Urbanek K, Sutherland DM, Orchard RC, Wilen CB, Knowlton JJ, Aravamudhan P, Taylor GM, Virgin HW, Dermody TS. Cytidine Monophosphate N-Acetylneuraminic Acid Synthetase and Solute Carrier Family 35 Member A1 Are Required for Reovirus Binding and Infection. Journal Of Virology 2020, 95: 10.1128/jvi.01571-20. PMID: 33087464, PMCID: PMC7944449, DOI: 10.1128/jvi.01571-20.Peer-Reviewed Original ResearchConceptsSialic acid expressionMicroglial cellsCell surface expressionReovirus-induced cell deathReovirus infectionSialic acidMurine microglial BV2 cellsReovirus-induced diseaseMember A1Microglial BV2 cellsSurface expressionMurine microglial cellsCell deathReovirus bindingBV2 cellsViral tropismInfectionHost genesLow-level bindingCell surface receptorsHost factorsCell surfaceReceptorsSialic acid synthesisSurface receptorsReal-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 recognitionMultisystem Imaging Manifestations of COVID-19, Part 1: Viral Pathogenesis and Pulmonary and Vascular System Complications
Revzin MV, Raza S, Warshawsky R, D'Agostino C, Srivastava NC, Bader AS, Malhotra A, Patel RD, Chen K, Kyriakakos C, Pellerito JS. Multisystem Imaging Manifestations of COVID-19, Part 1: Viral Pathogenesis and Pulmonary and Vascular System Complications. RadioGraphics 2020, 40: 1574-1599. PMID: 33001783, PMCID: PMC7534458, DOI: 10.1148/rg.2020200149.Peer-Reviewed Educational MaterialsMeSH KeywordsAngiographyAngiotensin-Converting Enzyme 2BetacoronavirusCoronavirus InfectionsCOVID-19Cytokine Release SyndromeDisease ProgressionFibrin Fibrinogen Degradation ProductsHumansInflammationLungPandemicsPeptidyl-Dipeptidase APneumonia, ViralPulmonary ArteryReceptors, VirusRespiratory Distress SyndromeSARS-CoV-2Symptom AssessmentThromboembolismThrombosisThrombotic MicroangiopathiesTomography, X-Ray ComputedUltrasonographyConceptsKey imaging featuresImaging featuresCOVID-19COVID-19-associated deathsPregnancy-related manifestationsCoronavirus disease 2019Effective patient managementWorld Health OrganizationVascular complicationsClinical presentationRelated complicationsImaging manifestationsMultisystemic involvementPathologic manifestationsPatient managementImage-based reviewDisease 2019Online supplemental materialImaging hallmarksCentral vascular systemOrgan systemsRespiratory systemInfectionMusculoskeletal systemHealth OrganizationCD300LF Polymorphisms of Inbred Mouse Strains Confer Resistance to Murine Norovirus Infection in a Cell Type-Dependent Manner
Furlong K, Biering SB, Choi J, Wilen CB, Orchard RC, Wobus CE, Nelson CA, Fremont DH, Baldridge MT, Randall G, Hwang S. CD300LF Polymorphisms of Inbred Mouse Strains Confer Resistance to Murine Norovirus Infection in a Cell Type-Dependent Manner. Journal Of Virology 2020, 94: 10.1128/jvi.00837-20. PMID: 32581099, PMCID: PMC7431780, DOI: 10.1128/jvi.00837-20.Peer-Reviewed Original ResearchConceptsBone marrow-derived macrophagesCell type-dependent mannerType-dependent mannerCell typesMacrophage-like cellsRobust experimental systemMNV infectionRelated murine norovirusSpecific cell typesCorresponding mutantsMarrow-derived macrophagesMurine norovirus infectionEntry factorsMurine norovirusCD300lfCause of gastroenteritisNonpermissive cellsProteinaceous receptorsConfer resistanceHuman cellsHost cellsDifferent allelesAmino acidsC57BL/6J allelePermissive cellsExpression of SARS-CoV-2 receptor ACE2 and coincident host response signature varies by asthma inflammatory phenotype
Camiolo M, Gauthier M, Kaminski N, Ray A, Wenzel SE. Expression of SARS-CoV-2 receptor ACE2 and coincident host response signature varies by asthma inflammatory phenotype. Journal Of Allergy And Clinical Immunology 2020, 146: 315-324.e7. PMID: 32531372, PMCID: PMC7283064, DOI: 10.1016/j.jaci.2020.05.051.Peer-Reviewed Original ResearchMeSH KeywordsAdolescentAdultAngiotensin-Converting Enzyme 2AsthmaBetacoronavirusBiomarkersBronchiBronchoalveolar Lavage FluidCohort StudiesCoronavirus InfectionsCOVID-19EosinophilsFemaleGene Expression ProfilingHumansInterferon Type IInterferon-gammaMaleMiddle AgedPandemicsPeptidyl-Dipeptidase APneumonia, ViralProtein Interaction MappingReceptors, VirusRisk FactorsSARS-CoV-2Severity of Illness IndexT-LymphocytesTranscriptomeUnited StatesConceptsCoronavirus disease 2019Severe coronavirus disease 2019Subset of patientsDisease 2019Risk factorsBronchial epitheliumAcute respiratory syndrome coronavirus 2 infectionSevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infectionSevere acute respiratory syndrome coronavirus 2Syndrome coronavirus 2 infectionType 2 inflammatory biomarkersAcute respiratory syndrome coronavirus 2Receptor ACE2SARS-CoV-2 receptor ACE2Respiratory syndrome coronavirus 2Asthma inflammatory phenotypesLarge asthma cohortsLower peripheral bloodT cell-activating factorCoronavirus 2 infectionEnzyme 2 (ACE2) expressionHistory of hypertensionDiagnosis of asthmaBronchoalveolar lavage lymphocytesT cell recruitmentSARS-CoV-2 Receptor ACE2 Is an Interferon-Stimulated Gene in Human Airway Epithelial Cells and Is Detected in Specific Cell Subsets across Tissues
Ziegler C, Allon S, Nyquist S, Mbano I, Miao V, Tzouanas C, Cao Y, Yousif A, Bals J, Hauser B, Feldman J, Muus C, Wadsworth M, Kazer S, Hughes T, Doran B, Gatter G, Vukovic M, Taliaferro F, Mead B, Guo Z, Wang J, Gras D, Plaisant M, Ansari M, Angelidis I, Adler H, Sucre J, Taylor C, Lin B, Waghray A, Mitsialis V, Dwyer D, Buchheit K, Boyce J, Barrett N, Laidlaw T, Carroll S, Colonna L, Tkachev V, Peterson C, Yu A, Zheng H, Gideon H, Winchell C, Lin P, Bingle C, Snapper S, Kropski J, Theis F, Schiller H, Zaragosi L, Barbry P, Leslie A, Kiem H, Flynn J, Fortune S, Berger B, Finberg R, Kean L, Garber M, Schmidt A, Lingwood D, Shalek A, Ordovas-Montanes J, Network H, Banovich N, Barbry P, Brazma A, Desai T, Duong T, Eickelberg O, Falk C, Farzan M, Glass I, Haniffa M, Horvath P, Hung D, Kaminski N, Krasnow M, Kropski J, Kuhnemund M, Lafyatis R, Lee H, Leroy S, Linnarson S, Lundeberg J, Meyer K, Misharin A, Nawijn M, Nikolic M, Ordovas-Montanes J, Pe’er D, Powell J, Quake S, Rajagopal J, Tata P, Rawlins E, Regev A, Reyfman P, Rojas M, Rosen O, Saeb-Parsy K, Samakovlis C, Schiller H, Schultze J, Seibold M, Shalek A, Shepherd D, Spence J, Spira A, Sun X, Teichmann S, Theis F, Tsankov A, van den Berge M, von Papen M, Whitsett J, Xavier R, Xu Y, Zaragosi L, Zhang K. SARS-CoV-2 Receptor ACE2 Is an Interferon-Stimulated Gene in Human Airway Epithelial Cells and Is Detected in Specific Cell Subsets across Tissues. Cell 2020, 181: 1016-1035.e19. PMID: 32413319, PMCID: PMC7252096, DOI: 10.1016/j.cell.2020.04.035.Peer-Reviewed Original ResearchMeSH KeywordsAdolescentAlveolar Epithelial CellsAngiotensin-Converting Enzyme 2AnimalsBetacoronavirusCell LineCells, CulturedChildCoronavirus InfectionsCOVID-19EnterocytesGoblet CellsHIV InfectionsHumansInfluenza, HumanInterferon Type ILungMacaca mulattaMiceMycobacterium tuberculosisNasal MucosaPandemicsPeptidyl-Dipeptidase APneumonia, ViralReceptors, VirusSARS-CoV-2Serine EndopeptidasesSingle-Cell AnalysisTuberculosisUp-RegulationConceptsSARS-CoV-2Interferon-stimulated genesAirway epithelial cellsCell subsetsSingle-cell RNA sequencing datasetsRNA sequencing datasetsSARS-CoV-2 receptor ACE2Human interferon-stimulated genesTransmembrane serine protease 2Human airway epithelial cellsEpithelial cellsSevere acute respiratory syndrome coronavirus clade 2SARS-CoV-2 spike proteinType II pneumocytesSerine protease 2Clade 2Putative targetsNon-human primatesSpecific cell subsetsCo-expressing cellsDisease COVID-19ACE2 expressionLung injuryLung type II pneumocytesAbsorptive enterocytesCD300lf is the primary physiologic receptor of murine norovirus but not human norovirus
Graziano VR, Walker FC, Kennedy EA, Wei J, Ettayebi K, Strine MS, Filler RB, Hassan E, Hsieh LL, Kim AS, Kolawole AO, Wobus CE, Lindesmith LC, Baric RS, Estes MK, Orchard RC, Baldridge MT, Wilen CB. CD300lf is the primary physiologic receptor of murine norovirus but not human norovirus. PLOS Pathogens 2020, 16: e1008242. PMID: 32251490, PMCID: PMC7162533, DOI: 10.1371/journal.ppat.1008242.Peer-Reviewed Original ResearchConceptsMNoV infectionPrimary physiologic receptorPhysiologic receptorHuman norovirusMurine norovirusBona fide receptorHumoral responseVirus infectionEntry receptorReceptor utilizationCell tropismInfectionReceptorsVirus-like particlesFide receptorCD300lfNorovirusHNoVCD300ldMajor determinantProteinaceous receptorsVivoMNoV.MNoVPathogenesis
2019
Bile Salts Alter the Mouse Norovirus Capsid Conformation: Possible Implications for Cell Attachment and Immune Evasion
Sherman MB, Williams AN, Smith HQ, Nelson C, Wilen CB, Fremont DH, Virgin HW, Smith TJ. Bile Salts Alter the Mouse Norovirus Capsid Conformation: Possible Implications for Cell Attachment and Immune Evasion. Journal Of Virology 2019, 93: 10.1128/jvi.00970-19. PMID: 31341042, PMCID: PMC6744230, DOI: 10.1128/jvi.00970-19.Peer-Reviewed Original ResearchConceptsCryo-EM structureP domainCryo-electron microscopy structureHigh-resolution cryo-EM structuresConformational changesImportant biological rolesSmall conformational changesMicroscopy structureHuman Norwalk virusCell attachmentAdjacent subunitsBiological roleIcosahedral capsidCapsid shellRNA virusesCapsid proteinBinding sitesIntrinsic affinityReceptor binding sitesCapsid conformationUnusual structureImmune evasionShell domainTarget cellsReceptorsDual Recognition of Sialic Acid and αGal Epitopes by the VP8* Domains of the Bovine Rotavirus G6P[5] WC3 and of Its Mono-reassortant G4P[5] RotaTeq Vaccine Strains
Alfajaro M, Kim J, Barbé L, Cho E, Park J, Soliman M, Baek Y, Kang M, Kim S, Kim G, Park S, Le Pendu J, Cho K. Dual Recognition of Sialic Acid and αGal Epitopes by the VP8* Domains of the Bovine Rotavirus G6P[5] WC3 and of Its Mono-reassortant G4P[5] RotaTeq Vaccine Strains. Journal Of Virology 2019, 93: 10.1128/jvi.00941-19. PMID: 31243129, PMCID: PMC6714814, DOI: 10.1128/jvi.00941-19.Peer-Reviewed Original ResearchConceptsHisto-blood group antigensRotaTeq vaccineIntestinal epithelial cellsAlternative receptorSialic acidVaccine strainGroup antigensSevere rotavirus diseaseEpithelial cellsHuman intestinal epithelial cellsHuman small intestinal epithelial cellsNatural human infectionBearing strainsSmall intestinal epithelial cellsRotaTeq vaccine strainsMA-104 cellsTight junction proteinsGroup A rotavirusesRotavirus diseaseSevere diarrheaIntestinal enteroidsGroup ASurface sialic acidΑGal epitopesImportant causeNorovirus 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 understanding
2018
Sphingolipid biosynthesis induces a conformational change in the murine norovirus receptor and facilitates viral infection
Orchard RC, Wilen CB, Virgin HW. Sphingolipid biosynthesis induces a conformational change in the murine norovirus receptor and facilitates viral infection. Nature Microbiology 2018, 3: 1109-1114. PMID: 30127493, PMCID: PMC6158067, DOI: 10.1038/s41564-018-0221-8.Peer-Reviewed Original ResearchConceptsSerine palmitoyltransferase complexSphingolipid biosynthesisCellular susceptibilityConformational changesLipid biosynthetic enzymesDe novo sphingolipid biosynthesisHost cellular receptorsSerine palmitoyltransferase activityBiosynthetic enzymesBiosynthetic pathwayMurine norovirus infectionMurine norovirusCD300lfCell surfaceBiosynthesisUnappreciated connectionCellular receptorsExtracellular ceramideReceptor conformationViral infectionSurface expressionTarget cell surfaceViral bindingPalmitoyltransferase activityReceptorsBovine Nebovirus Interacts with a Wide Spectrum of Histo-Blood Group Antigens
Cho E, Soliman M, Alfajaro M, Kim J, Seo J, Park J, Kim D, Baek Y, Kang M, Park S, Le Pendu J, Cho K. Bovine Nebovirus Interacts with a Wide Spectrum of Histo-Blood Group Antigens. Journal Of Virology 2018, 92: 10.1128/jvi.02160-17. PMID: 29467317, PMCID: PMC5899197, DOI: 10.1128/jvi.02160-17.Peer-Reviewed Original ResearchConceptsFucose epitopesTerminal sialic acidHost speciesVirus-like particlesHisto-blood group antigensCell surface carbohydrate moietiesMammalian host speciesEnteric calicivirusesAttachment factorsSialic acidCultured cell linesBovine digestive tractSurface carbohydrate moietiesCell carbohydratesHost rangeType speciesViral generaHBGA recognitionCarbohydrate moietyBiochemical assaysSpecific enzymesCellular receptorsSynthetic histo-blood group antigensReplication cycleSpecies
2016
Porcine amino peptidase N domain VII has critical role in binding and entry of porcine epidemic diarrhea virus
Kamau A, Park J, Park E, Yu J, Rho J, Shin H. Porcine amino peptidase N domain VII has critical role in binding and entry of porcine epidemic diarrhea virus. Virus Research 2016, 227: 150-157. PMID: 27732876, PMCID: PMC7114530, DOI: 10.1016/j.virusres.2016.10.004.Peer-Reviewed Original ResearchConceptsPorcine aminopeptidase NPorcine epidemic diarrhea virusNIH3T3 cellsDomain VIIDiarrhea virusPorcine epidemic diarrhea virus infectionDeletion mutantsMutantsEnteric diseaseDomain IIIIntestinal cellsVero cellsAminopeptidase NTime course testIndirect plaquesTherapeutic developmentCellsBindingPorcineVirusPlexin C1 deficiency permits synaptotagmin 7–mediated macrophage migration and enhances mammalian lung fibrosis
Peng X, Moore M, Mathur A, Zhou Y, Sun H, Gan Y, Herazo‐Maya J, Kaminski N, Hu X, Pan H, Ryu C, Osafo‐Addo A, Homer RJ, Feghali‐Bostwick C, Fares W, Gulati M, Hu B, Lee C, Elias JA, Herzog EL. Plexin C1 deficiency permits synaptotagmin 7–mediated macrophage migration and enhances mammalian lung fibrosis. The FASEB Journal 2016, 30: 4056-4070. PMID: 27609773, PMCID: PMC5102121, DOI: 10.1096/fj.201600373r.Peer-Reviewed Original ResearchConceptsLung fibrosisPlexin C1Macrophage migrationPulmonary fibrosisBone marrow-derived cellsSynaptotagmin-7Idiopathic pulmonary fibrosisInterstitial lung diseaseMarrow-derived cellsTGF-β1 overexpressionFatal conditionLung diseaseMonocyte migrationUnrecognized observationCollagen accumulationFibrosisMice showBoyden chamberGenetic deletionLungMouse macrophagesSemaphorin receptorsMacrophagesC1s deficiencyDeficiencyPorcine Sapelovirus Uses α2,3-Linked Sialic Acid on GD1a Ganglioside as a Receptor
Kim D, Son K, Koo K, Kim J, Alfajaro M, Park J, Hosmillo M, Soliman M, Baek Y, Cho E, Lee J, Kang M, Goodfellow I, Cho K. Porcine Sapelovirus Uses α2,3-Linked Sialic Acid on GD1a Ganglioside as a Receptor. Journal Of Virology 2016, 90: 4067-4077. PMID: 26865725, PMCID: PMC4810533, DOI: 10.1128/jvi.02449-15.Peer-Reviewed Original ResearchConceptsHisto-blood group antigensPorcine sapelovirusReproductive disordersSialic acidGroup antigensTerminal sialic acidSynthetic histo-blood group antigensEfficient drugsGlucosylceramide synthase inhibitorSynthase inhibitorLinkage-specific sialidasesInfectionGD1a gangliosidesReceptorsCell surface glycolipidsPneumoniaPolioencephalomyelitisTherapyCell surface carbohydratesAntigenGD1aHost cellsDisordersDrugsSapelovirus
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