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 ResearchMeSH KeywordsAngiotensin-Converting Enzyme 2COVID-19HumansMembrane ProteinsProtein BindingSARS-CoV-2Spike Glycoprotein, CoronavirusConceptsExpression 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
2020
UFMylation inhibits the proinflammatory capacity of interferon-γ–activated macrophages
Balce DR, Wang YT, McAllaster MR, Dunlap BF, Orvedahl A, Hykes BL, Droit L, Handley SA, Wilen CB, Doench JG, Orchard RC, Stallings CL, Virgin HW. UFMylation inhibits the proinflammatory capacity of interferon-γ–activated macrophages. Proceedings Of The National Academy Of Sciences Of The United States Of America 2020, 118: e2011763118. PMID: 33372156, PMCID: PMC7817147, DOI: 10.1073/pnas.2011763118.Peer-Reviewed Original ResearchConceptsGenome-wide CRISPR knockout screenCRISPR knockout screensEndoplasmic reticulum stress responseRegulation of responsesReticulum stress responseKnockout screensTranscriptional responseGenetic roadmapIFN-γ responsesTumor necrosis factorNegative regulatorMolecular linkUfmylation pathwayUnexpected roleStress responseMacrophage cell lineIFN-γ activationIntracellular pathogensProinflammatory capacityConjugation systemInfluenza infectionCellular immunityIFN-γ effectsNecrosis factorImmune response
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 cellsReceptors
2012
HIV: Cell Binding and Entry
Wilen CB, Tilton JC, Doms RW. HIV: Cell Binding and Entry. Cold Spring Harbor Perspectives In Medicine 2012, 2: a006866. PMID: 22908191, PMCID: PMC3405824, DOI: 10.1101/cshperspect.a006866.Peer-Reviewed Original ResearchConceptsHIV entryViral tropismPrimary cellular receptor CD4Human immunodeficiency virus (HIV) replicationAbility of HIVImmunodeficiency virus replicationHost immune responseHuman immune systemCellular receptor CD4Immune responseCellular coreceptorTherapeutic interventionsImmune systemReceptor CD4Virus replicationHIVCell bindingHost cell cytoplasmTropismHost cell membraneTrigger fusionCell cytoplasmCD4Major rolePathogenesis