Kristina Ferrara
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Biography
Kristina graduated from Rensselaer Polytechnic Institute with a B.S. in Biochemistry & Biophysics. After earning her bachelor's degree, she worked in the laboratory of Dr. Deborah Hung at Massachusetts General Hospital where she studied the pathogen Pseudomonas aeruginosa. She is currently a graduate student in the Pi Lab and is investigating the formation of ferrosomes in Clostridioides difficile.
Last Updated on March 24, 2024.
Departments & Organizations
Education & Training
- BS
- Rensselaer Polytechnic Institute, Biochemistry & Biophysics (2020)
Research
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Overview
Medical Research Interests
Bacterial Infections; Microbiology
ORCID
0009-0003-7039-3030
Research at a Glance
Yale Co-Authors
Frequent collaborators of Kristina Ferrara's published research.
Hualiang Pi, PhD
Kuldeepkumar Gupta
Former YSMYixuan Liu
Publications
2026
Ferrosome Organelles Spatially Insulate a Redox-Active Ferrous Phosphate Biomineral from Cytosolic ROS Chemistry.
Zhao K, Ferrara KM, Liu Y, Abernathy MJ, Sarangi R, Pi H. Ferrosome Organelles Spatially Insulate a Redox-Active Ferrous Phosphate Biomineral from Cytosolic ROS Chemistry. BioRxiv 2026 PMID: 42367999, DOI: 10.64898/2026.06.16.732667.Peer-Reviewed Original ResearchAn inducible CRISPRi system for phenotypic analysis of essential genes in Pseudomonas aeruginosa
Sullivan J, Ferrara K, Barrick R, Romano K, Warrier T, Hung D. An inducible CRISPRi system for phenotypic analysis of essential genes in Pseudomonas aeruginosa. MBio 2026, 17: e02767-25. PMID: 41670347, PMCID: PMC12977507, DOI: 10.1128/mbio.02767-25.Peer-Reviewed Original ResearchMeSH Keywords and ConceptsConceptsessential genesCRISPR interferenceCRISPRi systemgenetic perturbationsimpact of genetic perturbationsstable maintenanceanalysis of essential geneshigh-throughput functional genomicsstudy of essential genesphenotypic analysisrhamnose-inducible promoterconstruction of strainsantibiotic discovery effortsinducible CRISPRi systemsmall molecule mechanism of actionCRISPR interference systemresistance to current antibioticssusceptibility to antibioticscomparison of phenotypesGram-negative pathogensgenome-widemutant librarygenetic interactionsfunctional genomicsgene perturbations
2024
Discovery of a Pseudomonas aeruginosa-specific small molecule targeting outer membrane protein OprH-LPS interaction by a multiplexed screen
Poulsen B, Warrier T, Barkho S, Bagnall J, Romano K, White T, Yu X, Kawate T, Nguyen P, Raines K, Ferrara K, Golas A, FitzGerald M, Boeszoermenyi A, Kaushik V, Serrano-Wu M, Shoresh N, Hung D. Discovery of a Pseudomonas aeruginosa-specific small molecule targeting outer membrane protein OprH-LPS interaction by a multiplexed screen. Cell Chemical Biology 2024, 32: 307-324.e15. PMID: 39732052, PMCID: PMC12117999, DOI: 10.1016/j.chembiol.2024.12.001.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsP. aeruginosa mutantsouter membranearray of efflux pumpsasymmetric outer membranemultiplex screeningGram-negative pathogensresistant Gram-negative pathogensessential proteinspathogen biologyantibiotic discoveryefflux pumpsP. aeruginosaPseudomonas aeruginosasmall molecule probeschemical biology studiesantimicrobial resistancesmall moleculesOprHmutantschemical probesbiological studiespathogensmembrane fluiditymolecule probeswhole-cellBacterial Organelles in Iron Physiology
Ferrara K, Gupta K, Pi H. Bacterial Organelles in Iron Physiology. Molecular Microbiology 2024, 122: 914-928. PMID: 39545931, PMCID: PMC11659020, DOI: 10.1111/mmi.15330.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsCitationsAltmetricConceptsmembrane-bound organellesbacterial organellesferritin-like proteinseukaryotic organellesprotein-lipid monolayerseukaryotic cellsproteinaceous shellspecies-specificbacterial cellsorganellesprotecting cellslife formsbiochemical reactionsphysiological functionsdiverse arrayiron physiologyenvironmental conditionslipid bilayerbacteriaessential micronutrientcellsspecial structurebiogenesisgeneticsproteinPerturbation-specific transcriptional mapping for unbiased target elucidation of antibiotics
Romano K, Bagnall J, Warrier T, Sullivan J, Ferrara K, Orzechowski M, Nguyen P, Raines K, Livny J, Shoresh N, Hung D. Perturbation-specific transcriptional mapping for unbiased target elucidation of antibiotics. Proceedings Of The National Academy Of Sciences Of The United States Of America 2024, 121: e2409747121. PMID: 39467118, PMCID: PMC11551328, DOI: 10.1073/pnas.2409747121.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptstarget elucidationClustered regularly interspaced short palindromic repeats interferenceprofiling of small moleculesmechanism-of-actionchemical entitiestranscription mapexpression profilescellular responses to perturbationsprevalence of antibiotic resistanceexpression profiles of wild-typeantibiotic discovery effortssmall moleculesreference-based strategydiscovery effortssmall molecule inhibitiongenetic perturbationshypomorphic mutantstranscriptional responsepostgenomic eraantibiotic discoveryantimicrobial compoundsantibiotic resistancegenetic depletionresponse to perturbationsreference sets
2021
Genetic and Biochemical Characterization of the Na+/H+ Antiporters of Pseudomonas aeruginosa
Foreman S, Ferrara K, Hreha T, Duran-Pinedo A, Frias-Lopez J, Barquera B. Genetic and Biochemical Characterization of the Na+/H+ Antiporters of Pseudomonas aeruginosa. Journal Of Bacteriology 2021, 203: 10.1128/jb.00284-21. PMID: 34280000, PMCID: PMC8378476, DOI: 10.1128/jb.00284-21.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptswild-type straindeletion mutantsphysiology of P. aeruginosaquadruple deletion mutantquadruple deletion strainphysiological roletranscriptome sequencing analysiskinetic propertiesantiport activitynative membranespyocyanin synthesisdeletion strainNa+/H+ antiporterglycerol metabolismquadruple mutantbiochemical characterizationsequence analysisbiofilm formationpH valuesP. aeruginosaPseudomonas aeruginosamutantselectrogenic antiporterelectroneutral antiportantiporterThe three NADH dehydrogenases of Pseudomonas aeruginosa: Their roles in energy metabolism and links to virulence
Hreha T, Foreman S, Duran-Pinedo A, Morris A, Diaz-Rodriguez P, Jones J, Ferrara K, Bourges A, Rodriguez L, Koffas M, Hahn M, Hauser A, Barquera B. The three NADH dehydrogenases of Pseudomonas aeruginosa: Their roles in energy metabolism and links to virulence. PLOS ONE 2021, 16: e0244142. PMID: 33534802, PMCID: PMC7857637, DOI: 10.1371/journal.pone.0244142.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsNADH dehydrogenasepyocyanin productiondeletion mutantsdouble deletion mutantwild-type activitytranscription of genesmouse infection modelminimal mediumopportunistic pathogenbiofilm formationexponential phasemutantsrespiratory chainwild typeP. aeruginosaPseudomonas aeruginosaNADHinfection modelpyocyaninredox functionenergy metabolismenzymenuodehydrogenasestrain
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