Samuel Steiner, PhD
Associate Research ScientistCards
About
Research
Publications
2024
CRISPR-Cas9-based approaches for genetic analysis and epistatic interaction studies in Coxiella burnetii
Steiner S, Roy C. CRISPR-Cas9-based approaches for genetic analysis and epistatic interaction studies in Coxiella burnetii. MSphere 2024, 9: e00523-24. PMID: 39560384, PMCID: PMC11656778, DOI: 10.1128/msphere.00523-24.Peer-Reviewed Original ResearchIntracellular replicationHost cellsDouble mutantGenetic analysisDot/Icm type IVB secretion systemType IVB secretion systemConstruction of double mutantsLoss-of-function mutantsIntracellular replication defectsLysosome-derived vacuoleIVB secretion systemObligate intracellular bacterial pathogenRandom transposon mutagenesisTransposon insertion mutantsCRISPR-Cas9-based technologiesIntracellular bacterial pathogensLoss-of-function mutationsMammalian host cellsIntroduction of premature stop codonsPremature stop codonSilence gene expressionTargeted gene disruptionBase editing approachesEffector mutantsSecretion system
2023
Syntaxin 11 Contributes to the Interferon-Inducible Restriction of Coxiella burnetii Intracellular Infection
Ganesan S, Alvarez N, Steiner S, Fowler K, Corona A, Roy C. Syntaxin 11 Contributes to the Interferon-Inducible Restriction of Coxiella burnetii Intracellular Infection. MBio 2023, 14: e03545-22. PMID: 36728431, PMCID: PMC9972978, DOI: 10.1128/mbio.03545-22.Peer-Reviewed Original ResearchConceptsC. burnetii replicationSNARE proteinsHost cellsSyntaxin-11Cell-autonomous responsesIntracellular pathogensMembrane fusion eventsLysosome-derived organellesDefense mechanismsModel bacterial pathogenMultiple cell typesEukaryotic cellsDefense pathwaysDelivery of cargoReplication of pathogensHuman proteinsFusion eventsDissemination of pathogensFusion pathwayHost proteinsIntrinsic defense mechanismsHost vesiclesHost restriction factorsStable expressionSubcellular organelles
2022
Developmental Transitions Coordinate Assembly of the Coxiella burnetii Dot/Icm Type IV Secretion System
Park D, Steiner S, Shao M, Roy CR, Liu J. Developmental Transitions Coordinate Assembly of the Coxiella burnetii Dot/Icm Type IV Secretion System. Infection And Immunity 2022, 90: e00410-22. PMID: 36190257, PMCID: PMC9584302, DOI: 10.1128/iai.00410-22.Peer-Reviewed Original ResearchConceptsSmall cell variantLarge cell variantDot/Icm type IV secretion systemCell variantIntracellular replicationActive large cell variantHost cellsIntracellular bacterial pathogenType IV secretion systemDot/Icm T4SSObligate intracellular bacterial pathogenC. burnetiiCoxiella burnetiiBiphasic developmental cycleUnique biphasic developmental cycleInfectionNew host cellsSecretion systemBacterial pathogensInfectious formHost vacuoleBurnetiiMorphological changesCellsLater stages
2021
Cover Image: Coxiella burnetii encodes an LvgA‐related protein important for intracellular replication (Cellular Microbiology 06/2021)
Steiner S, Meir A, Roy C. Cover Image: Coxiella burnetii encodes an LvgA‐related protein important for intracellular replication (Cellular Microbiology 06/2021). Cellular Microbiology 2021, 23 DOI: 10.1111/cmi.13351.Peer-Reviewed Original ResearchCoxiella burnetii encodes an LvgA‐related protein important for intracellular replication
Steiner S, Meir A, Roy CR. Coxiella burnetii encodes an LvgA‐related protein important for intracellular replication. Cellular Microbiology 2021, 23: e13331. PMID: 33774901, DOI: 10.1111/cmi.13331.Peer-Reviewed Original ResearchConceptsIntracellular replicationDot/Icm type IVB secretion systemType IVB secretion systemDot/Icm apparatusHost cell cytosolTransposon mutagenesis screenAutophagy protein LC3Lysosome-derived organellesL. pneumophilaSecondary structure predictionChaperone complexBiogenesis defectsEffector proteinsEffector translocationProtein complexesMutagenesis screenSecretion systemLvgACell cytosolNine Mile phase IIProtein LC3MutantsReplication phenotypeProteinStructure prediction
2017
DNA Delivery and Genomic Integration into Mammalian Target Cells through Type IV A and B Secretion Systems of Human Pathogens
Guzmán-Herrador DL, Steiner S, Alperi A, González-Prieto C, Roy CR, Llosa M. DNA Delivery and Genomic Integration into Mammalian Target Cells through Type IV A and B Secretion Systems of Human Pathogens. Frontiers In Microbiology 2017, 8: 1503. PMID: 28878740, PMCID: PMC5572225, DOI: 10.3389/fmicb.2017.01503.Peer-Reviewed Original Research
2015
Cyclic di-GMP acts as a cell cycle oscillator to drive chromosome replication
Lori C, Ozaki S, Steiner S, Böhm R, Abel S, Dubey BN, Schirmer T, Hiller S, Jenal U. Cyclic di-GMP acts as a cell cycle oscillator to drive chromosome replication. Nature 2015, 523: 236-239. PMID: 25945741, DOI: 10.1038/nature14473.Peer-Reviewed Original Research
2012
Allosteric activation of exopolysaccharide synthesis through cyclic di‐GMP‐stimulated protein–protein interaction
Steiner S, Lori C, Boehm A, Jenal U. Allosteric activation of exopolysaccharide synthesis through cyclic di‐GMP‐stimulated protein–protein interaction. The EMBO Journal 2012, 32: 354-368. PMID: 23202856, PMCID: PMC3567491, DOI: 10.1038/emboj.2012.315.Peer-Reviewed Original ResearchConceptsProtein-protein interactionsSecond messenger cInner membrane componentsEscherichia coli biofilmsGMP receptorGMP signalingGMP bindsSynthesis machineryExtracellular matrix componentsMajor extracellular matrix componentsAllosteric activationExopolysaccharide synthesisExopolysaccharide matrixMembrane componentsColi biofilmsGlycosyltransferase activityBacterial pathogensMachineryN-acetylglucosaminePathogenic bacteriaMatrix componentsEnzyme activityGMP concentrationGMPBacteria
2009
Second messenger signalling governs Escherichia coli biofilm induction upon ribosomal stress
Boehm A, Steiner S, Zaehringer F, Casanova A, Hamburger F, Ritz D, Keck W, Ackermann M, Schirmer T, Jenal U. Second messenger signalling governs Escherichia coli biofilm induction upon ribosomal stress. Molecular Microbiology 2009, 72: 1500-1516. PMID: 19460094, DOI: 10.1111/j.1365-2958.2009.06739.x.Peer-Reviewed Original ResearchMeSH KeywordsAdhesins, BacterialAnti-Bacterial Agentsbeta-GlucansBiofilmsCyclic GMPEscherichia coliEscherichia coli ProteinsGene Expression Regulation, BacterialGuanosine TetraphosphatePhosphorus-Oxygen LyasesProtein BiosynthesisPyrophosphatasesRibosomesRNA Processing, Post-TranscriptionalSecond Messenger SystemsConceptsBiofilm inductionRibosome-targeting antibioticsNovel regulatory mechanismSecond messenger signalingSpecific derepressionBiosynthesis machineryRibosomal stressTranslational stressTranslation inhibitorsPpGpp levelsExposure of bacteriaMicrobial cellsRegulatory mechanismsAdhesin productionPolysaccharide adhesinBiofilm formationPpGppImportant synergistic roleMaximal inductionBiofilm controlMachineryBiofilm modelInductionGMPSubinhibitory concentrations
1992
Adipose Tissue Distribution and Chemical Structure of Basic Lipophilic Drugs: Desipramine, N‐Acetyl Desipramine, and Haloperidol
Moor M, Steiner S, Jachertz G, Bickel M. Adipose Tissue Distribution and Chemical Structure of Basic Lipophilic Drugs: Desipramine, N‐Acetyl Desipramine, and Haloperidol. Basic & Clinical Pharmacology & Toxicology 1992, 70: 121-124. PMID: 1508837, DOI: 10.1111/j.1600-0773.1992.tb00440.x.Peer-Reviewed Original Research
Academic Achievements & Community Involvement
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Yale School of Medicine
Boyer Center for Molecular Medicine, rm 347, 295 Congress Avenue
New Haven, CT 06536-0812
United States