2021
Single-cell longitudinal analysis of SARS-CoV-2 infection in human airway epithelium identifies target cells, alterations in gene expression, and cell state changes
Ravindra NG, Alfajaro MM, Gasque V, Huston NC, Wan H, Szigeti-Buck K, Yasumoto Y, Greaney AM, Habet V, Chow RD, Chen JS, Wei J, Filler RB, Wang B, Wang G, Niklason LE, Montgomery RR, Eisenbarth SC, Chen S, Williams A, Iwasaki A, Horvath TL, Foxman EF, Pierce RW, Pyle AM, van Dijk D, Wilen CB. Single-cell longitudinal analysis of SARS-CoV-2 infection in human airway epithelium identifies target cells, alterations in gene expression, and cell state changes. PLOS Biology 2021, 19: e3001143. PMID: 33730024, PMCID: PMC8007021, DOI: 10.1371/journal.pbio.3001143.Peer-Reviewed Original ResearchConceptsSARS-CoV-2 infectionSARS-CoV-2Human bronchial epithelial cellsInterferon-stimulated genesCell state changesAcute respiratory syndrome coronavirus 2 infectionSevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infectionSyndrome coronavirus 2 infectionCell tropismCoronavirus 2 infectionCoronavirus disease 2019Onset of infectionCell-intrinsic expressionCourse of infectionAir-liquid interface culturesHost-viral interactionsBronchial epithelial cellsSingle-cell RNA sequencingCell typesIL-1Disease 2019Human airwaysDevelopment of therapeuticsDrug AdministrationViral replication
2018
Activation of PI3K, Akt, and ERK during early rotavirus infection leads to V-ATPase-dependent endosomal acidification required for uncoating
Soliman M, Seo J, Kim D, Kim J, Park J, Alfajaro M, Baek Y, Cho E, Kwon J, Choi J, Kang M, Park S, Cho K. Activation of PI3K, Akt, and ERK during early rotavirus infection leads to V-ATPase-dependent endosomal acidification required for uncoating. PLOS Pathogens 2018, 14: e1006820. PMID: 29352319, PMCID: PMC5792019, DOI: 10.1371/journal.ppat.1006820.Peer-Reviewed Original ResearchMeSH KeywordsAcidsAnimalsCaco-2 CellsCapsid ProteinsCattleCells, CulturedEndosomesEnzyme ActivationExtracellular Signal-Regulated MAP KinasesHaplorhiniHumansHydrogen-Ion ConcentrationPhosphatidylinositol 3-KinasesProto-Oncogene Proteins c-aktRotavirusRotavirus InfectionsSf9 CellsSignal TransductionVacuolar Proton-Translocating ATPasesVirus UncoatingConceptsMEK/ERK pathwayV-ATPasePI3K/AktSubunit EOuter capsid proteinEndosomal acidificationLate endosomesERK pathwayCapsid proteinPI3KEarly infection eventsMEK/ERKCell surface receptorsImmunoprecipitation assaysPPI3KVirus traffickingProximity ligationMultistep bindingSurface receptorsAktViral progenyViral uncoatingERKRVA strainsEndosomes
2017
Activation of COX-2/PGE2 Promotes Sapovirus Replication via the Inhibition of Nitric Oxide Production
Alfajaro M, Choi J, Kim D, Seo J, Kim J, Park J, Soliman M, Baek Y, Cho E, Kwon J, Kwon H, Park S, Lee W, Kang M, Hosmillo M, Goodfellow I, Cho K. Activation of COX-2/PGE2 Promotes Sapovirus Replication via the Inhibition of Nitric Oxide Production. Journal Of Virology 2017, 91: 10.1128/jvi.01656-16. PMID: 27881647, PMCID: PMC5244346, DOI: 10.1128/jvi.01656-16.Peer-Reviewed Original ResearchConceptsCOX/PGENonsteroidal anti-inflammatory drugsAnti-inflammatory drugsCOX-2Sapovirus infectionAcute gastroenteritisProstaglandin ECOX-1/2 inhibitor indomethacinAntiviral effector mechanismsCOX-2 specific inhibitor NS-398Severe acute gastroenteritisCOX-1 levelsInhibitor NS-398New targetsNitric oxide synthaseProduction of PGENitric oxide productionCOX-2 mRNASmall interfering RNAsPorcine sapovirusMajor etiological agentPotential new targetsInhibitor indomethacinOxide synthaseEffector mechanisms