Hesper Rego, PhD
Associate Professor TermCards
Appointments
Contact Info
Microbial Pathogenesis
295 Congress Ave, BCMM 336D/337
New Haven, CT 06519
United States
About
Titles
Associate Professor Term
Biography
Hesper trained as physicist in both her undergraduate studies (Caltech, B.S. Physics, 2005), and her graduate studies (UCSF, PhD, Biophysics, 2011). She did her graduate work with the late Mats Gustafsson at UCSF and Janelia Farm. In his group, she developed a nonlinear form of Structured-Illumination Microscopy. Afterwards, wanting to explore a biological phenomenon she did her postdoctoral work with Eric Rubin at the Harvard School of Public Health where she became fascinated by the ability of genetically identical organisms to display different phenotypes. This phenomenon is especially important for the treatment of tuberculosis, a disease caused by the bacterial pathogen Mycobacterium tuberculosis. She is excited to start a research group at the intersection of these two areas: the application of advanced light microscopy techniques to investigate the strategies mycobacteria use to survive the stresses imposed by antibiotics and host.
Appointments
Microbial Pathogenesis
Associate Professor on TermPrimary
Other Departments & Organizations
Education & Training
- Postdoctoral Fellow
- Harvard School of Public Health (2016)
- PhD
- University of California, San Francisco, Biophysics (2011)
- BS
- California Institute of Technology, Physics (2005)
Research
Overview
Medical Subject Headings (MeSH)
- View Lab Website
Rego Lab
Research at a Glance
Yale Co-Authors
Publications Timeline
Research Interests
Lin Shao, PhD
Chunyan Wang, PhD
María Lara-Tejero, DVM, PhD
TuKiet Lam, PhD, BS
Weiwei (Wendy) Wang
Imaging, Three-Dimensional
Single-Cell Analysis
Publications
Featured Publications
An essential periplasmic protein coordinates lipid trafficking and is required for asymmetric polar growth in mycobacteria
Gupta K, Gwin C, Rahlwes K, Biegas K, Wang C, Park J, Liu J, Swarts B, Morita Y, Rego E. An essential periplasmic protein coordinates lipid trafficking and is required for asymmetric polar growth in mycobacteria. ELife 2022, 11: e80395. PMID: 36346214, PMCID: PMC9678360, DOI: 10.7554/elife.80395.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsPeriplasmic proteinsPolar growthNew cell wall materialOld poleQuantitative time-lapse imagingAsymmetric polar growthCell wall synthesisCell envelope compositionCell wall materialTime-lapse imagingCellular asymmetryEssential proteinsBacterial geneticsEssential transporterSingle geneWall synthesisLipid traffickingPopulation of cellsPlasma membraneTMM transportUnknown functionBroad functionsMycolic acidsTrehalose monomycolateEnvelope compositionItaconate 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 ConceptsMaturing Mycobacterium smegmatis peptidoglycan requires non-canonical crosslinks to maintain shape
Baranowski C, Welsh M, Sham L, Eskandarian H, Lim H, Kieser K, Wagner J, McKinney J, Fantner G, Ioerger T, Walker S, Bernhardt T, Rubin E, Rego E. Maturing Mycobacterium smegmatis peptidoglycan requires non-canonical crosslinks to maintain shape. ELife 2018, 7: e37516. PMID: 30324906, PMCID: PMC6231781, DOI: 10.7554/elife.37516.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsPenicillin-binding proteinsAsymmetric polar growthRod-shaped bacteriaPolar growthPolar elongationShape maintenanceCell wallGenetic relationshipsDrug targetsUnusual crosslinksD-transpeptidasesSingle cellsPeptidoglycanCellsCrosslinksProteinMycobacteriaBacteriaPathogensTypes of crosslinksElongationGrowthMaintenanceTargetDeletion of a mycobacterial divisome factor collapses single-cell phenotypic heterogeneity
Rego E, Audette R, Rubin E. Deletion of a mycobacterial divisome factor collapses single-cell phenotypic heterogeneity. Nature 2017, 546: 153-157. PMID: 28569798, PMCID: PMC5567998, DOI: 10.1038/nature22361.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsNonlinear structured-illumination microscopy with a photoswitchable protein reveals cellular structures at 50-nm resolution
Rego EH, Shao L, Macklin JJ, Winoto L, Johansson GA, Kamps-Hughes N, Davidson MW, Gustafsson MG. Nonlinear structured-illumination microscopy with a photoswitchable protein reveals cellular structures at 50-nm resolution. Proceedings Of The National Academy Of Sciences Of The United States Of America 2011, 109: e135-e143. PMID: 22160683, PMCID: PMC3271870, DOI: 10.1073/pnas.1107547108.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsStructured-illumination microscopyUltralow light intensitiesSuperresolution imaging methodExcited statesFluorophore excited stateStructured illumination microscopyLight intensityRequired nonlinearityResolution extensionHigh light intensityActin cytoskeletonCellular structureReversible photoswitchingNuclear poresNonlinear responseIllumination intensitySuch nonlinear responsesPhotoswitchable proteinsSpatial resolutionFluorescent proteinBiological samplesSix-orderImaging methodMicroscopyPolystyrene beadsSuper-resolution 3D microscopy of live whole cells using structured illumination
Shao L, Kner P, Rego EH, Gustafsson MG. Super-resolution 3D microscopy of live whole cells using structured illumination. Nature Methods 2011, 8: 1044-1046. PMID: 22002026, DOI: 10.1038/nmeth.1734.Peer-Reviewed Original ResearchCitationsAltmetricA nucleoid-associated protein is involved in the emergence of antibiotic resistance by promoting the frequent exchange of the replicative DNA polymerase in Mycobacterium smegmatis
Ng W, Rego E. A nucleoid-associated protein is involved in the emergence of antibiotic resistance by promoting the frequent exchange of the replicative DNA polymerase in Mycobacterium smegmatis. MSphere 2024, 9: e00122-24. PMID: 38591887, PMCID: PMC11237743, DOI: 10.1128/msphere.00122-24.Peer-Reviewed Original ResearchCitationsAltmetricConceptsNucleoid-associated proteinsReplicative DNA polymerasesBypass DNA lesionsDNA replicationDNA polymeraseAntibiotic resistanceDamaged DNAExpression of error-prone DNA polymerasesReplicative polymerasesHigh-fidelity replicative polymerasesQuantitative fluorescence imaging techniqueError-prone DNA synthesisDNA lesionsError-prone DNA polymerasesHorizontal gene transferEmergence of antibiotic resistanceDNA-damaging agentsRepair damaged DNAResistance to rifampinRobust cell growthGrowth defectLsr2Replication forksBacterial speciesChromosomal mutations
2024
Phenotypic Heterogeneity in Pathogens.
Sherry J, Rego E. Phenotypic Heterogeneity in Pathogens. Annual Review Of Genetics 2024 PMID: 39083846, DOI: 10.1146/annurev-genet-111523-102459.Peer-Reviewed Original ResearchAltmetricConceptsPhenotypic heterogeneityGenetically identical populationSalmonella typhimurium</i>Genetic diversityPathogen diversityPathogen populationsBacterial pathogensPathogen subpopulationsGenetic heterogeneityInvading pathogensHost organismFluctuating environmentsInfectious disease progressionPathogensIdentical populationsTreatment escapeInfection outcomesHeterogeneous subpopulationsDisease progressionInfecting organismDiversityCausative linkGeneticsSubpopulationsPhenotype
2022
Mycobacterial serine/threonine phosphatase PstP is phosphoregulated and localized to mediate control of cell wall metabolism
Shamma F, Rego E, Boutte C. Mycobacterial serine/threonine phosphatase PstP is phosphoregulated and localized to mediate control of cell wall metabolism. Molecular Microbiology 2022, 118: 47-60. PMID: 35670057, PMCID: PMC10070032, DOI: 10.1111/mmi.14951.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsCell wall metabolismWall metabolismCell wall-related proteinsSerine/threonine proteinCell wall regulationPhosphomimetic mutationReversible phosphorylationThreonine phosphataseEnvironmental stressRegulatory proteinsCell wallCorresponding mutationMycobacterial cell wallAntibiotic toleranceNovel substrateFhaAProteinPstPMycobacterium smegmatisWag31Certain substratesPeptidoglycanPhosphorylationRegulationMajor mechanismCell Wall Damage Reveals Spatial Flexibility in Peptidoglycan Synthesis and a Nonredundant Role for RodA in Mycobacteria
Melzer E, Kado T, García-Heredia A, Gupta K, Meniche X, Morita Y, Sassetti C, Rego E, Siegrist M. Cell Wall Damage Reveals Spatial Flexibility in Peptidoglycan Synthesis and a Nonredundant Role for RodA in Mycobacteria. Journal Of Bacteriology 2022, 204: e00540-21. PMID: 35543537, PMCID: PMC9210966, DOI: 10.1128/jb.00540-21.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsPenicillin binding proteinsCell wall damagePeptidoglycan synthesisPeptidoglycan assemblyClass A Penicillin-Binding ProteinsNascent cell wallCell wall integrityCell wall assemblyCell-wall peptidoglycanCell wall synthesisRod-shaped bacteriaMycobacterium smegmatisPolar growthInternal turgorModel organismsMreB homologsNew inhibition strategyRod complexWall synthesisWall peptidoglycanWall integrityAnimal pathogensCell wallPathway functionSubcellular distribution
Academic Achievements & Community Involvement
honor Pew Biomedical Scholar
National AwardPew Charitable TrustsDetails08/01/2018United Stateshonor Searle Scholar Award
National AwardDetails07/01/2018United Stateshonor Kingsley Award in Medical Research
Yale School of Medicine AwardDetails08/01/2016United Stateshonor Career Awards at the Scientific Interfaces
National AwardBurroughs Wellcome FundDetails10/01/2014United Stateshonor Ruth L. Kirschstein National Service Award
National AwardDetails07/01/2014United States
News
News
Get In Touch
Contacts
Microbial Pathogenesis
295 Congress Ave, BCMM 336D/337
New Haven, CT 06519
United States
Locations
Boyer Center for Molecular Medicine
Academic Office
295 Congress Avenue, Rm BCMM 336D
New Haven, CT 06510
Boyer Center for Molecular Medicine
Lab
295 Congress Avenue, Rm BCMM 337
New Haven, CT 06510