María Lara-Tejero, DVM, PhD
Associate ProfessorCards
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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.
Appointments
Microbial Pathogenesis
Associate Professor on TermPrimary
Other Departments & Organizations
Education & Training
- Postdoctoral training
- MSKCC (2004)
- PhD
- Yale University (2001)
- DVM
- Complutense University of Madrid (1995)
Research
Overview
Medical Research Interests
ORCID
0000-0002-1339-0859- View Lab Website
Galán/Lara-Tejero Lab
Research at a Glance
Yale Co-Authors
Publications Timeline
Research Interests
Jorge Galán, PhD, DVM
Jun Liu, PhD
Wenwei Li
Fulan Guan, PhD
Hesper Rego, PhD
Joerg Bewersdorf, PhD
Type III Secretion Systems
Host-Pathogen Interactions
Salmonella
Publications
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 ResearchMeSH 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 ResearchMeSH 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 ResearchMeSH 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 ResearchMeSH 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 ResearchMeSH Keywords and ConceptsMechanisms of substrate recognition by a typhoid toxin secretion-associated muramidase
Geiger T, Lara-Tejero M, Xiong Y, Galán JE. Mechanisms of substrate recognition by a typhoid toxin secretion-associated muramidase. ELife 2020, 9: e53473. PMID: 31958059, PMCID: PMC6996933, DOI: 10.7554/elife.53473.Peer-Reviewed Original Research
2019
High-resolution view of the type III secretion export apparatus in situ reveals membrane remodeling and a secretion pathway
Butan C, Lara-Tejero M, Li W, Liu J, Galán JE. High-resolution view of the type III secretion export apparatus in situ reveals membrane remodeling and a secretion pathway. Proceedings Of The National Academy Of Sciences Of The United States Of America 2019, 116: 24786-24795. PMID: 31744874, PMCID: PMC6900529, DOI: 10.1073/pnas.1916331116.Peer-Reviewed Original ResearchThe Injectisome, a Complex Nanomachine for Protein Injection into Mammalian Cells
Lara-tejero M, Galán J. The Injectisome, a Complex Nanomachine for Protein Injection into Mammalian Cells. 2019, 245-259. DOI: 10.1128/9781683670285.ch20.Peer-Reviewed Original ResearchConceptsSecretion machineType III protein secretion systemType III secretion machinesProtein secretion systemTarget eukaryotic cellsCell biological processesType III systemMultiprotein nanomachineEukaryotic hostsComplex nanomachinesGram-negative bacteriaPlant pathogensSymbiotic interactionsEukaryotic cellsEffector proteinsSecretion systemMammalian cellsImportant humanBiological processesStructural organizationInjectisomeBacteriaCurrent knowledgeCentral rolePrimary functionAlternate subunit assembly diversifies the function of a bacterial toxin
Fowler CC, Stack G, Jiao X, Lara-Tejero M, Galán JE. Alternate subunit assembly diversifies the function of a bacterial toxin. Nature Communications 2019, 10: 3684. PMID: 31417089, PMCID: PMC6695444, DOI: 10.1038/s41467-019-11592-0.Peer-Reviewed Original ResearchMeSH Keywords and ConceptsInvestigation of the role of typhoid toxin in acute typhoid fever in a human challenge model
Gibani MM, Jones E, Barton A, Jin C, Meek J, Camara S, Galal U, Heinz E, Rosenberg-Hasson Y, Obermoser G, Jones C, Campbell D, Black C, Thomaides-Brears H, Darlow C, Dold C, Silva-Reyes L, Blackwell L, Lara-Tejero M, Jiao X, Stack G, Blohmke CJ, Hill J, Angus B, Dougan G, Galán J, Pollard AJ. Investigation of the role of typhoid toxin in acute typhoid fever in a human challenge model. Nature Medicine 2019, 25: 1082-1088. PMID: 31270506, PMCID: PMC6892374, DOI: 10.1038/s41591-019-0505-4.Peer-Reviewed Original ResearchMeSH Keywords and ConceptsConceptsHuman challenge modelTyphoid toxinChallenge modelTyphoid feverAcute typhoid feverDuration of bacteremiaFurther clinical dataS. typhiAcute infectionOral challengeClinical syndromeChronic infectionBacterial carriageClinical dataSevere diseaseTN groupFever symptomsHealthy volunteersDisease pathogenesisTyphoid infectionTyphoid diseaseColony-forming unitsHost-restricted pathogenInfectionSalmonella typhi
Academic Achievements & Community Involvement
honor Irvington Institute for Immunological Research Post-doctoral Fellowship
National AwardIrvington Institute for Immunological ResearchDetails09/12/2003United Stateshonor 2001 Nat L. Stemberg Thesis Prize for outstanding Ph.D. thesis in the filed of prokaryotic and bacteriophage molecular genetics
National AwardNat L. Sternberg Thesis Prize Endowment FundDetails08/03/2001United Stateshonor Award for outstanding research
Yale University AwardMicrobiology Program at Yale UniversityDetails09/15/2000United States
News & Links
Media
- (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.