María Lara-Tejero, DVM, PhD
Associate ProfessorDownloadHi-Res Photo
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Microbial Pathogenesis
Primary
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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
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.
Jun Liu, PhD
Wenwei Li
Hesper Rego, PhD
Joerg Bewersdorf, PhD
Jorge Galán, PhD, DVM
Lin Shao, PhD
32Publications
4,256Citations
Type III Secretion Systems
Host-Pathogen Interactions
Salmonella
Publications
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 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 ResearchCitationsAltmetric
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 ResearchCitationsAltmetricAlternate 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 ResearchCitationsAltmetricMeSH 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 ResearchCitationsAltmetricMeSH 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 typhiThe 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 ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsSecretion machineSecretion systemType III secretion injectisomeSecretion processType III secretion systemLarge cytoplasmic complexesProtein secretion machinesHost plasma membraneProtein translocasesCytoplasmic complexSecretion pathwayNeedle complexSorting platformPlasma membraneHost cellsProteinTranslocasesInjectisomeComplexesEffectorsPathwayComplex substructureSubstrateMembraneAssemblyThe Injectisome, a Complex Nanomachine for Protein Injection into Mammalian Cells
Lara-Tejero M, Galán JE. The Injectisome, a Complex Nanomachine for Protein Injection into Mammalian Cells. EcoSal Plus 2019, 8: 10.1128/ecosalplus.esp-0039-2018. PMID: 30942149, PMCID: PMC6450406, DOI: 10.1128/ecosalplus.esp-0039-2018.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsEffector proteinsGram-negative bacteriaSecretion systemBacterial envelopeType III protein secretion systemProtein secretion systemHost cellular functionsEukaryotic plasma membraneEukaryotic cell membranesHost cell cytosolMultiprotein nanomachineEukaryotic hostsComplex nanomachinesImportant bacterial pathogensCellular functionsMammalian cellsNeedle complexOuter membranePlasma membraneCell cytosolInjectisomeCell membraneProteinBacterial pathogensCentral roleRole of SpaO in the assembly of the sorting platform of a Salmonella type III secretion system
Lara-Tejero M, Qin Z, Hu B, Butan C, Liu J, Galán JE. Role of SpaO in the assembly of the sorting platform of a Salmonella type III secretion system. PLOS Pathogens 2019, 15: e1007565. PMID: 30668610, PMCID: PMC6358110, DOI: 10.1371/journal.ppat.1007565.Peer-Reviewed Original ResearchCitationsAltmetric
2018
Visualization of the type III secretion mediated Salmonella–host cell interface using cryo-electron tomography
Park D, Lara-Tejero M, Waxham MN, Li W, Hu B, Galán JE, Liu J. Visualization of the type III secretion mediated Salmonella–host cell interface using cryo-electron tomography. ELife 2018, 7: e39514. PMID: 30281019, PMCID: PMC6175578, DOI: 10.7554/elife.39514.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsCryo-electron tomographyEffector translocationBacterial-host cell contactType III protein secretion systemProtein secretion systemHost cell interfaceProtein secretion machinesCell membraneComplex host-pathogen interactionsType III secretionHost-pathogen interactionsHost cell membraneTarget cell membraneNegative bacterial pathogensTranslocon poreSecretion machineEffector proteinsSecretion systemHost cellsBacterial pathogensCell contactCell interfaceIntimate associationTranslocationBacteriaPeptidoglycan editing by a specific ld-transpeptidase controls the muramidase-dependent secretion of typhoid toxin
Geiger T, Pazos M, Lara-Tejero M, Vollmer W, Galán JE. Peptidoglycan editing by a specific ld-transpeptidase controls the muramidase-dependent secretion of typhoid toxin. Nature Microbiology 2018, 3: 1243-1254. PMID: 30250245, PMCID: PMC7464686, DOI: 10.1038/s41564-018-0248-x.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsProtein export mechanismProtein secretion mechanismsTyphoid toxinEssential virulence factorBacterial poleMammalian cellsPeptidoglycan layerMost bacterial pathogensOuter membraneExport mechanismSecretion mechanismToxin secretionBacterial speciesTranslocation processTrans sideVirulence factorsBacterial pathogensExtracellular spaceTransport pathwaysTarget cellsToxinTyphoid feverCellsSubsequent releaseSecretion
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.