María Lara-Tejero, DVM, PhD
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Microbial Pathogenesis
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Associate Professor
Biography
Dr. Lara-Tejero received her DVM from University Complutense in Madrid, Spain in 1995, and a PhD in Microbiology from Yale University in 2001, receiving the Nat L. Sternberg Prize for outstanding PhD Thesis in the field of prokaryotic biology. She pursued postdoctoral training in Immunobiology at Memorial Sloan Kettering Institute in New York City as an Irvington Fellow. She joined the Yale University School of Medicine in 2004, where she is currently and Associate Professor of Microbial Pathogenesis. Her laboratory focuses on the study of the pathogenesis of Salmonella enterica. More specifically, her laboratory employs multidisciplinary approaches to study type III secretion machines, which deliver bacterial effector proteins into target host cells to induce pathogenicity.
Last Updated on April 07, 2025.
Appointments
Microbial Pathogenesis
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- Microbial Pathogenesis
Education & Training
- Postdoctoral training
- MSKCC (2004)
- PhD
- Yale University (2001)
- DVM
- Complutense University of Madrid (1995)
Research
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Overview
Medical Research Interests
Host-Pathogen Interactions; Microbiology; Salmonella; Type III Secretion Systems
ORCID
0000-0002-1339-0859- View Lab Website
Galán/Lara-Tejero Lab
Research at a Glance
Yale Co-Authors
Frequent collaborators of María Lara-Tejero's published research.
Publications Timeline
A big-picture view of María Lara-Tejero's research output by year.
Research Interests
Research topics María Lara-Tejero is interested in exploring.
Jorge Galán, PhD, DVM
Jun Liu, PhD
Wenwei Li
Chunxiang Wu
Fulan Guan, PhD
Heng Zhao
49Publications
6,647Citations
Type III Secretion Systems
Host-Pathogen Interactions
Salmonella
Publications
2026
Interplay between SpaO variants shapes the architecture of the Salmonella type III secretion sorting platform.
Soto J, Wang T, Galán J, Lara-Tejero M. Interplay between SpaO variants shapes the architecture of the Salmonella type III secretion sorting platform. MBio 2026, e0015526. PMID: 41758121, DOI: 10.1128/mbio.00155-26.Peer-Reviewed Original ResearchAltmetricConceptsType III secretion systemIII secretion systemSalmonella entericaSecretion systemSorting platformVirulence-associated type III secretion systemHost cellsSPI-1 T3SSTranslocate effector proteinsShort variantCore scaffold proteinNative cellular environmentInjectisome assemblyBacterial effectorsEffector deliveryEffector translocationAntivirulence strategiesEffector proteinsDocking motifVirulence arsenalScaffold proteinN-terminalTranslocation assayT3SSInjectisomeOligomeric assembly of the gatekeeper InvE orchestrates hierarchical type III protein secretion in Salmonella Typhimurium
Wang T, Zhu L, Guo E, Wu C, Schueder F, Lara-Tejero M, Galán J. Oligomeric assembly of the gatekeeper InvE orchestrates hierarchical type III protein secretion in Salmonella Typhimurium. Proceedings Of The National Academy Of Sciences Of The United States Of America 2026, 123: e2530441123. PMID: 41587314, PMCID: PMC12878844, DOI: 10.1073/pnas.2530441123.Peer-Reviewed Original ResearchAltmetricMeSH Keywords and ConceptsConceptsType III protein secretionType III secretion systemSPI-1 T3SSIII secretion systemBlue-native electrophoresisOligomers in vivoHigher-order contactsHigher-order oligomersGram-negative bacteriaEffector secretionEffector translocationCharge-reversal mutationSecretion systemOligomeric assembliesSalmonella typhimuriumProtein secretionAntiparallel dimerSuperresolution microscopyT3SSTranslocaseVirulenceDimerization faceInvOligomerizationTetramerStructural insights into the assembly and evolution of a complex bacterial flagellar motor
Feng X, Tachiyama S, He J, Zhu S, Zhao H, Botting J, Liu Y, Chen Y, Hua C, Lara-Tejero M, Baker M, Gao X, Liu J, Gao B. Structural insights into the assembly and evolution of a complex bacterial flagellar motor. Nature Microbiology 2026, 11: 770-785. PMID: 41513997, DOI: 10.1038/s41564-025-02248-5.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsFlagellar motorPilus componentsSalmonella entericaPhylogenetic analysisMS ringBacterial flagellaCampylobacter jejuniFlagellated bacteriaStator complexBacterial flagellar motorStructural insightsComplex adaptationsE ringBacteriaCo-optionCage-like structureFlgICampylobacterotaEntericaFlagellaAssemblyHomodimerJejuniCampylobacter
2025
Typhoid toxin causes neuropathology by disrupting the blood–brain barrier
Zhao H, Catarino J, Stack G, Albizu A, Lara-Tejero M, Horvath T, Galán J. Typhoid toxin causes neuropathology by disrupting the blood–brain barrier. Nature Microbiology 2025, 10: 1340-1351. PMID: 40341334, DOI: 10.1038/s41564-025-02000-z.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsTyphoid toxinTyphoid feverBlood-brain barrierBlood brain barrier disruption in vivoDisruption in vivoManifestations of typhoid feverVirulence factorsSalmonella typhiCatalytic subunitBlood-brain barrier permeability changesToxin actionLife-threatening complicationsSevere neurological manifestationsTyphoidIn vitro modelToxinNeurological complicationsGlial cellsTherapeutic interventionsFeverToxin exposureVirulenceComplicationsNeuropathologyEncephalopathy
2024
Tetrameric PilZ protein stabilizes stator ring in complex flagellar motor and is required for motility in Campylobacter jejuni
Chen Y, Tachiyama S, Li Y, Feng X, Zhao H, Wu Y, Guo Y, Lara-Tejero M, Hua C, Liu J, Gao B. Tetrameric PilZ protein stabilizes stator ring in complex flagellar motor and is required for motility in Campylobacter jejuni. Proceedings Of The National Academy Of Sciences Of The United States Of America 2024, 122: e2412594121. PMID: 39793078, PMCID: PMC11725899, DOI: 10.1073/pnas.2412594121.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsFlagellar motorPilZ domain-containing proteinsBound cyclic di-GMPCyclic di-GMPC-di-GMPDomain-containing proteinsStator unitsDi-GMPFamily proteinsSuperfamily proteinsBacterial flagellaRing assemblyCellular pathwaysCampylobacter jejuniCryoelectron tomographyCampylobacter jejuni.Subtomogram averagingPilZProteinFlagellaPhylumAncestorMotilityJejuniStructural components
2023
Parkinson’s disease kinase LRRK2 coordinates a cell-intrinsic itaconate-dependent defence pathway against intracellular Salmonella
Lian H, Park D, Chen M, Schueder F, Lara-Tejero M, Liu J, Galán J. Parkinson’s disease kinase LRRK2 coordinates a cell-intrinsic itaconate-dependent defence pathway against intracellular Salmonella. Nature Microbiology 2023, 8: 1880-1895. PMID: 37640963, PMCID: PMC10962312, DOI: 10.1038/s41564-023-01459-y.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsLeucine-rich repeat kinase 2Loss of LRRK2Host defense mechanismsKinase leucine-rich repeat kinase 2Parkinson's disease-associated leucine-rich repeat kinase 2Host defense pathwaysBacterial pathogen SalmonellaRepeat kinase 2Salmonella infectionSalmonella-containing vacuolesCell-intrinsic defenseIntracellular pathogensIntracellular SalmonellaFirst lineSalmonella replicationSalmonella mutantsKinase 2Pathogen SalmonellaDefense mechanismsSalmonellaHost mitochondriaDefense pathwaysDeliveryDefense responsesCellsThe 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 ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsSecretion 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 ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsType 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 processProteinDeletionTyphoid toxin sorting and exocytic transport from Salmonella Typhi-infected cells
Chang SJ, Hsu YT, Chen Y, Lin YY, Lara-Tejero M, Galan JE. Typhoid toxin sorting and exocytic transport from Salmonella Typhi-infected cells. ELife 2022, 11: e78561. PMID: 35579416, PMCID: PMC9142146, DOI: 10.7554/elife.78561.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsCellular machineryType III protein secretion systemSpecific cellular machineryVesicle carriersProtein secretion systemExtracellular spaceTyphoid toxinEssential virulence factorExocytic transportGTPase Sar1Syntaxin 4Unusual biologySecretion systemPlasma membraneIntracellular transportRemarkable adaptationSpecific effectorsHost cellsIntracellular pathogensVirulence factorsMachineryCooptionVacuolesToxinSpecific environment
2020
Itaconate is an effector of a Rab GTPase cell-autonomous host defense pathway against Salmonella
Chen M, Sun H, Boot M, Shao L, Chang SJ, Wang W, Lam TT, Lara-Tejero M, Rego EH, Galán JE. Itaconate is an effector of a Rab GTPase cell-autonomous host defense pathway against Salmonella. Science 2020, 369: 450-455. PMID: 32703879, PMCID: PMC8020367, DOI: 10.1126/science.aaz1333.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and Concepts
Academic Achievements & Community Involvement
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Honors
honor Irvington Institute for Immunological Research Post-doctoral Fellowship
09/12/2003National AwardIrvington Institute for Immunological ResearchDetailsUnited Stateshonor 2001 Nat L. Stemberg Thesis Prize for outstanding Ph.D. thesis in the filed of prokaryotic and bacteriophage molecular genetics
08/03/2001National AwardNat L. Sternberg Thesis Prize Endowment FundDetailsUnited Stateshonor Award for outstanding research
09/15/2000Yale University AwardMicrobiology Program at Yale UniversityDetailsUnited States
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- (A) Surface view of the 3D reconstruction of the single-particle cryo-EM map of the needle complex (NC) substructure with the atomic structures of the different NC components docked. OR1, outer ring 1; OR2, outer ring 2; IR1, inner ring 1; IR2, inner ring 2. (B) Central section of an overall cryo-ET structure of the complete injectisome in situ. Of note is the location of IR2 in the cytosolic side of the bacterial envelope. IM, inner membrane; OM, outer membrane. (C) Molecular model of the organization of the injectisome in situ, with available atomic structures fitted into the model.
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