2025
Mutations in the SWEET15 Sugar Transporter Gene Affect Response of Citrus to Huanglongbing Disease and Citrus Canker
Khadgi A, Zayed O, Sagawa C, Zhang F, Seymour D, Irish V. Mutations in the SWEET15 Sugar Transporter Gene Affect Response of Citrus to Huanglongbing Disease and Citrus Canker. Molecular Plant Pathology 2025, 26: e70094. PMID: 40369935, PMCID: PMC12078760, DOI: 10.1111/mpp.70094.Peer-Reviewed Original ResearchConceptsSecretion systemCitrus cankerSusceptibility genesEffector proteinsType III secretion systemSec secretion systemIII secretion systemBacterial secretion systemsBacterial diseasesXanthomonas citri pvSusceptibility to citrus cankerCitrus cultivarsCandidatus Liberibacter asiaticusSusceptibility gene expressionPlant immunityInfected plantsBacterial pathogensSucrose transportGene activationLiberibacter asiaticusPromote pathogenesisExported TransportersSWEET15Lemon plantsCanker
2023
The sorting platform in the type III secretion pathway: From assembly to function
Soto J, Lara‐Tejero M. The sorting platform in the type III secretion pathway: From assembly to function. BioEssays 2023, 45: e2300078. PMID: 37329195, DOI: 10.1002/bies.202300078.Peer-Reviewed Original ResearchConceptsSecretion pathwayType III secretion pathwayType III secretion systemSyringe-like apparatusHost-pathogen interfaceEukaryotic organismsComplex nanomachinesSecretion systemCytosolic complexAssembly pathwaySpecialized nanomachinesMolecular mechanismsSoluble proteinCytosolic componentsChamber-like structuresPrecise coordinationT3SSPathwayRecent findingsProteinNanomachinesSpecific setSortingNovel strategyOrganisms
2022
Assembly and architecture of the type III secretion sorting platform
Soto J, Galán J, Lara-Tejero M. Assembly and architecture of the type III secretion sorting platform. Proceedings Of The National Academy Of Sciences Of The United States Of America 2022, 119: e2218010119. PMID: 36512499, PMCID: PMC9907115, DOI: 10.1073/pnas.2218010119.Peer-Reviewed Original ResearchConceptsType III secretion machinesType III secretion systemTarget eukaryotic cellsType III secretionSecretion of proteinsBacterial nanomachinesSecretion machineEukaryotic cellsExport pathwayImportant bacterial pathogensSecretion systemBacterial structureAntivirulence strategiesCoordinated mechanismFunctional complexityBacterial pathogensGenetic deletionStructure modelingProtein deliveryAssemblyRational developmentCross-linking strategyAssembly processProteinDeletion
2021
Composition and Biophysical Properties of the Sorting Platform Pods in the Shigella Type III Secretion System
Tachiyama S, Skaar R, Chang Y, Carroll BL, Muthuramalingam M, Whittier SK, Barta ML, Picking WL, Liu J, Picking WD. Composition and Biophysical Properties of the Sorting Platform Pods in the Shigella Type III Secretion System. Frontiers In Cellular And Infection Microbiology 2021, 11: 682635. PMID: 34150677, PMCID: PMC8211105, DOI: 10.3389/fcimb.2021.682635.Peer-Reviewed Original ResearchConceptsType III secretion systemCytoplasmic sorting platformSorting platformSecretion systemTwo-hybrid analysisCryo-electron tomography dataC-terminal domainShigella type III secretion systemFull-length copiesBiophysical propertiesDistinct biophysical propertiesSpa47 ATPaseT3SS injectisomeEffector proteinsSecretion substratesDistinct complexesIntracellular nicheBasal bodiesPrimary virulence factorSpa33Host cellsHeterotrimerPrecise makeupVirulence factorsMxiK
2020
The Structures of SctK and SctD from Pseudomonas aeruginosa Reveal the Interface of the Type III Secretion System Basal Body and Sorting Platform
Muthuramalingam M, Whittier SK, Lovell S, Battaile KP, Tachiyama S, Johnson DK, Picking WL, Picking WD. The Structures of SctK and SctD from Pseudomonas aeruginosa Reveal the Interface of the Type III Secretion System Basal Body and Sorting Platform. Journal Of Molecular Biology 2020, 432: 166693. PMID: 33122003, PMCID: PMC10550303, DOI: 10.1016/j.jmb.2020.10.027.Peer-Reviewed Original ResearchConceptsInner membrane ringBasal bodiesCytoplasmic domainSorting platformFirst high-resolution structureType III secretion systemCytoplasmic sorting platformTwo-hybrid analysisGram-negative bacterial pathogensProtein family membersNormal cellular functionHigh-resolution structuresAtomic resolution modelsHelix-rich structureEukaryotic cellsT3SS apparatusAdaptor proteinCellular functionsSecretion systemMembrane ringMechanistic interfaceTip complexExternal needleRadial spokesProteinHfq and sRNA 179 Inhibit Expression of the Pseudomonas aeruginosa cAMP-Vfr and Type III Secretion Regulons
Janssen KH, Corley JM, Djapgne L, Cribbs JT, Voelker D, Slusher Z, Nordell R, Regulski EE, Kazmierczak BI, McMackin EW, Yahr TL. Hfq and sRNA 179 Inhibit Expression of the Pseudomonas aeruginosa cAMP-Vfr and Type III Secretion Regulons. MBio 2020, 11: 10.1128/mbio.00363-20. PMID: 32546612, PMCID: PMC7298702, DOI: 10.1128/mbio.00363-20.Peer-Reviewed Original ResearchMeSH KeywordsBacterial ProteinsCyclic AMP Receptor ProteinCyclic AMP-Dependent Protein KinasesGene Expression Regulation, BacterialGene LibraryHost Factor 1 ProteinPromoter Regions, GeneticPseudomonas aeruginosaRegulonRNA, BacterialRNA, Small UntranslatedTranscription, GeneticType III Secretion SystemsVirulence FactorsConceptsSmall noncoding RNAsType III secretion systemSecretion systemNoncoding RNAsGene expressionTranscription factorsExpression libraryGac/Rsm systemType VI secretion systemT3SS gene expressionCAMP-responsive transcription factorRNA-binding proteinVirulence factorsGram-negative opportunistic pathogenRNA chaperonesGlobal regulatorT3SS regulonMutant lackingTarget mRNAsCritical virulence factorImportant virulence factorMRNA targetsHfqRegulonRsm system
2019
The cytoplasmic domain of MxiG interacts with MxiK and directs assembly of the sorting platform in the Shigella type III secretion system
Tachiyama S, Chang Y, Muthuramalingam M, Hu B, Barta ML, Picking WL, Liu J, Picking WD. The cytoplasmic domain of MxiG interacts with MxiK and directs assembly of the sorting platform in the Shigella type III secretion system. Journal Of Biological Chemistry 2019, 294: 19184-19196. PMID: 31699894, PMCID: PMC6916477, DOI: 10.1074/jbc.ra119.009125.Peer-Reviewed Original ResearchConceptsInner membrane ringType III secretion systemCytoplasmic domainSecretion systemCytoplasmic sorting platformForkhead-associated (FHA) domainShigella type III secretion systemDiverse bacterial pathogensDisruption of interactionsSpa47 ATPaseStructure-function relationshipsExtracellular needleEffector recognitionGram-negative bacteriaEukaryotic cellsT3SS apparatusVirulence effectorsMembrane ringSorting platformInsertional mutagenesisGenetic methodsHomologous interactionsMxiKTip complexBasal bodiesThe Type III Secretion System Sorting Platform
Lara-Tejero M. The Type III Secretion System Sorting Platform. Current Topics In Microbiology And Immunology 2019, 427: 133-142. PMID: 31183608, DOI: 10.1007/82_2019_167.Peer-Reviewed Original ResearchConceptsSecretion machineSecretion systemType III secretion injectisomeSecretion processType III secretion systemLarge cytoplasmic complexesProtein secretion machinesHost plasma membraneProtein translocasesCytoplasmic complexSecretion pathwayNeedle complexSorting platformPlasma membraneHost cellsProteinTranslocasesInjectisomeComplexesEffectorsPathwayComplex substructureSubstrateMembraneAssembly
2018
Cryo-electron tomography of periplasmic flagella in Borrelia burgdorferi reveals a distinct cytoplasmic ATPase complex
Qin Z, Tu J, Lin T, Norris SJ, Li C, Motaleb MA, Liu J. Cryo-electron tomography of periplasmic flagella in Borrelia burgdorferi reveals a distinct cytoplasmic ATPase complex. PLOS Biology 2018, 16: e3000050. PMID: 30412577, PMCID: PMC6248999, DOI: 10.1371/journal.pbio.3000050.Peer-Reviewed Original ResearchConceptsCryo-electron tomographyPeriplasmic flagellaATPase complexFlagellar C-ringType III secretion systemCytoplasmic ATPase complexLyme disease spirochete Borrelia burgdorferiMotility of spirochetesExport apparatusSecretion systemStructural insightsBorrelia burgdorferiFlagellaSpirochete Borrelia burgdorferiPathogenic spirochetesC-ringNovel therapeutic strategiesUnique mechanismDistinct morphologiesB. burgdorferiComplexesMultiple spokesAssemblyTherapeutic strategiesBurgdorferiUsing disruptive insertional mutagenesis to identify the in situ structure‐function landscape of the Shigella translocator protein IpaB
Barta ML, Tachiyama S, Muthuramalingam M, Arizmendi O, Villanueva CE, Ramyar KX, Geisbrecht BV, Lovell S, Battaile KP, Picking WL, Picking WD. Using disruptive insertional mutagenesis to identify the in situ structure‐function landscape of the Shigella translocator protein IpaB. Protein Science 2018, 27: 1392-1406. PMID: 29672980, PMCID: PMC6153406, DOI: 10.1002/pro.3428.Peer-Reviewed Original ResearchConceptsTip complexInsertional mutagenesisTranslocator protein IpaBBacterial type III secretion systemType III secretion systemC-terminal halfN-terminal halfInsertion mutantsT3SS apparatusCellular functionsLatter mutantSecretion inductionMammalian cellsSecretion systemTC functionHost membraneBasal bodiesBacteriophage T4 lysozymeTertiary structureImpaired interactionIpaBPore formationT4 lysozymeBacterial surfaceMutants
2016
The Salmonella Effector Protein SopA Modulates Innate Immune Responses by Targeting TRIM E3 Ligase Family Members
Kamanova J, Sun H, Lara-Tejero M, Galán JE. The Salmonella Effector Protein SopA Modulates Innate Immune Responses by Targeting TRIM E3 Ligase Family Members. PLOS Pathogens 2016, 12: e1005552. PMID: 27058235, PMCID: PMC4825927, DOI: 10.1371/journal.ppat.1005552.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBacterial ProteinsCell LineDisease Models, AnimalGene Knockout TechniquesHost-Parasite InteractionsHumansImmunity, InnateImmunoprecipitationMass SpectrometryMiceReal-Time Polymerase Chain ReactionSalmonella InfectionsSalmonella typhimuriumSignal TransductionUbiquitin-Protein LigasesConceptsInflammatory responseImmune responseSalmonella typhimurium infectionInnate immune receptorsInnate immune responseHECT-type E3 ligaseTyphimurium infectionAnimal modelsIntestinal epitheliumIntestinal tractImmune receptorsInflammationStimulationTRIM56Type III secretion systemMDA5Pathogenicity island 1Family membersEfficient stimulationSalmonella typhimuriumIsland 1ResponseE3 ubiquitin ligasesInfectionSecretion systemNAIP proteins are required for cytosolic detection of specific bacterial ligands in vivo
Rauch I, Tenthorey JL, Nichols RD, Al Moussawi K, Kang JJ, Kang C, Kazmierczak BI, Vance RE. NAIP proteins are required for cytosolic detection of specific bacterial ligands in vivo. Journal Of Experimental Medicine 2016, 213: 657-665. PMID: 27045008, PMCID: PMC4854734, DOI: 10.1084/jem.20151809.Peer-Reviewed Original ResearchConceptsSpecific bacterial proteinsNAIP proteinsNeedle proteinBacterial proteinsGenetic evidenceSpecific bacterial ligandsBacterial ligandsBacterial type III secretion systemInner rod proteinType III secretion systemT3SS needle proteinStrong biochemical evidenceCytosolic flagellinFlagellin detectionRod proteinsSecretion systemDetection of flagellinCRISPR/Diverse functionsCytosolic detectionNAIP1ProteinBiochemical evidenceNAIPsFlagellinA Family of Salmonella Type III Secretion Effector Proteins Selectively Targets the NF-κB Signaling Pathway to Preserve Host Homeostasis
Sun H, Kamanova J, Lara-Tejero M, Galán JE. A Family of Salmonella Type III Secretion Effector Proteins Selectively Targets the NF-κB Signaling Pathway to Preserve Host Homeostasis. PLOS Pathogens 2016, 12: e1005484. PMID: 26933955, PMCID: PMC4775039, DOI: 10.1371/journal.ppat.1005484.Peer-Reviewed Original ResearchConceptsNF-κBHost homeostasisNF-κB Signaling PathwayHost innate immune responsePro-inflammatory cytokinesInnate immune responseType III secretion effector proteinsHost tissue damageIntestinal inflammationSalmonella typhimurium strainsImmune responseAnimal modelsInflammationRelB transcription factorPathogen replicationMicrobial infectionsTyphimurium strainsEffector proteinsSignaling pathwaysType III secretion systemInfectionBacterial pathogensBacteria Salmonella typhimuriumSignal transduction pathwaysSalmonella typhimurium
2014
Bacterial Type III Secretion Systems: Specialized Nanomachines for Protein Delivery into Target Cells
Galán JE, Lara-Tejero M, Marlovits TC, Wagner S. Bacterial Type III Secretion Systems: Specialized Nanomachines for Protein Delivery into Target Cells. Annual Review Of Microbiology 2014, 68: 1-24. PMID: 25002086, PMCID: PMC4388319, DOI: 10.1146/annurev-micro-092412-155725.Peer-Reviewed Original ResearchConceptsEukaryotic cellsEffector proteinsBacterial envelopeType III secretion systemTarget eukaryotic cellsComplex nanomachinesNovel antimicrobial strategiesPathogen's benefitCellular functionsSecretion systemNeedle complexBacterial pathogenesisCytoplasmic componentsSpecialized nanomachinesSpecific substratesProteinPlantsCentral roleProtein deliveryAntimicrobial strategiesBacteriaNanomachinesTarget cellsCentral componentCellsNMR Model of PrgI–SipD Interaction and Its Implications in the Needle-Tip Assembly of the Salmonella Type III Secretion System
Rathinavelan T, Lara-Tejero M, Lefebre M, Chatterjee S, McShan AC, Guo DC, Tang C, Galan JE, De Guzman RN. NMR Model of PrgI–SipD Interaction and Its Implications in the Needle-Tip Assembly of the Salmonella Type III Secretion System. Journal Of Molecular Biology 2014, 426: 2958-2969. PMID: 24951833, PMCID: PMC4108505, DOI: 10.1016/j.jmb.2014.06.009.Peer-Reviewed Original ResearchConceptsType III secretion systemTip proteinSecretion systemRecent atomic structuresN-terminal αNeedle tip complexSalmonella type III secretion systemDomain bindsHelical hairpinVirulence proteinsFusion proteinHuman cellsSteric clashesSipDProteinPathogenic bacteriaNMR modelsRecent NMRPrgIPrgI.Needle apparatusPRE methodSpecific regionsStructural componentsAssembly
2013
Engineering the type III secretion system in non-replicating bacterial minicells for antigen delivery
Carleton HA, Lara-Tejero M, Liu X, Galán JE. Engineering the type III secretion system in non-replicating bacterial minicells for antigen delivery. Nature Communications 2013, 4: 1590. PMID: 23481398, PMCID: PMC3693737, DOI: 10.1038/ncomms2594.Peer-Reviewed Original ResearchConceptsBacterial minicellsPresentation pathwayVaccine developmentClass IAntigen-specific CD8Antigen delivery platformSalmonella typhimurium type III secretion systemDelivery platformType III secretion systemCellular immunotherapyT cellsAntigen deliveryImmune responseHeterologous antigensProtein antigensSecretion systemCertain populationsAntigenNanoparticlesDeliveryNanomachinesCD8ImmunotherapyPathwayNovel approach
2011
A Sorting Platform Determines the Order of Protein Secretion in Bacterial Type III Systems
Lara-Tejero M, Kato J, Wagner S, Liu X, Galán JE. A Sorting Platform Determines the Order of Protein Secretion in Bacterial Type III Systems. Science 2011, 331: 1188-1191. PMID: 21292939, PMCID: PMC3859126, DOI: 10.1126/science.1201476.Peer-Reviewed Original ResearchConceptsSecretion systemSorting platformType III protein secretion systemBacterial type III protein secretion systemsType III protein secretionProtein secretionType III secretion systemCytoplasmic sorting platformProtein secretion systemType III systemSalmonella enterica serovar TyphimuriumNovel antimicrobial strategiesEukaryotic cellsEffector proteinsEnterica serovar TyphimuriumCellular processesSerovar TyphimuriumImportant pathogenProteinAntimicrobial strategiesChaperonesSecretionPathogensMechanismSubstrate
2009
Salmonella Typhimurium Type III Secretion Effectors Stimulate Innate Immune Responses in Cultured Epithelial Cells
Bruno VM, Hannemann S, Lara-Tejero M, Flavell RA, Kleinstein SH, Galán JE. Salmonella Typhimurium Type III Secretion Effectors Stimulate Innate Immune Responses in Cultured Epithelial Cells. PLOS Pathogens 2009, 5: e1000538. PMID: 19662166, PMCID: PMC2714975, DOI: 10.1371/journal.ppat.1000538.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBacterial ProteinsBlotting, WesternCell LineColitisEpithelial CellsGene ExpressionGene Expression ProfilingGuanine Nucleotide Exchange FactorsHumansImmunity, InnateMiceMitogen-Activated Protein Kinase KinasesMyotonin-Protein KinaseNF-kappa BOligonucleotide Array Sequence AnalysisProtein Serine-Threonine KinasesReverse Transcriptase Polymerase Chain ReactionSalmonella InfectionsSalmonella typhimuriumSignal TransductionTranscription, GeneticConceptsInnate immune receptorsInnate immune responseIntestinal inflammationImmune responseEpithelial cellsBacterial productsIntestinal inflammatory pathologyImmune receptorsCultured epithelial cellsEnteric pathogen Salmonella typhimuriumInnate immune systemIntestinal epithelial cellsInflammatory pathologyInflammatory responseType III secretion effectorsImmune systemSalmonella typhimuriumNF-kappaBMitogen-activated protein kinaseEnteric pathogensPathogen Salmonella typhimuriumPathologyReceptorsInflammationType III secretion systemSalmonella enterica Serovar Typhimurium Pathogenicity Island 1-Encoded Type III Secretion System Translocases Mediate Intimate Attachment to Nonphagocytic Cells
Lara-Tejero M, Galán JE. Salmonella enterica Serovar Typhimurium Pathogenicity Island 1-Encoded Type III Secretion System Translocases Mediate Intimate Attachment to Nonphagocytic Cells. Infection And Immunity 2009, 77: 2635-2642. PMID: 19364837, PMCID: PMC2708559, DOI: 10.1128/iai.00077-09.Peer-Reviewed Original ResearchConceptsType III secretion systemPathogenicity island 1Secretion systemMammalian cellsIntimate associationIsland 1Host cellsBacterial contactBacterial surfaceIntimate attachmentS. typhimurium mutantsProtein translocasesBacterial proteinsMolecular basisTTSS componentsTarget cellsNonphagocytic cellsTyphimurium mutantsImmunofluorescence microscopyDifferent bacteriaTranslocasesSalmonella entericaSipBBacteriaProteinDiversification of a Salmonella Virulence Protein Function by Ubiquitin-Dependent Differential Localization
Patel JC, Hueffer K, Lam TT, Galán JE. Diversification of a Salmonella Virulence Protein Function by Ubiquitin-Dependent Differential Localization. Cell 2009, 137: 283-294. PMID: 19379694, PMCID: PMC2673707, DOI: 10.1016/j.cell.2009.01.056.Peer-Reviewed Original ResearchConceptsEffector proteinsCellular functionsType III secretion systemBacterial effector proteinsUbiquitin-dependent mannerDifferent cellular compartmentsHost cellular machinerySame enzymatic activityVesicular traffickingCellular machineryProtein functionSecretion systemCellular compartmentsBacterial internalizationFunctional repertoirePlasma membraneRegulated mannerAkt activationHost cellsDifferential localizationBacterial replicationVirulence factorsEnzymatic activityBacterial pathogensProtein
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