2024
Durlobactam, a Diazabicyclooctane β‑Lactamase Inhibitor, Inhibits BlaC and Peptidoglycan Transpeptidases of Mycobacterium tuberculosis
Nantongo M, Nguyen D, Bethel C, Taracila M, Li Q, Dousa K, Shin E, Kurz S, Nguyen L, Kreiswirth B, Boom W, Plummer M, Bonomo R. Durlobactam, a Diazabicyclooctane β‑Lactamase Inhibitor, Inhibits BlaC and Peptidoglycan Transpeptidases of Mycobacterium tuberculosis. ACS Infectious Diseases 2024, 10: 1767-1779. PMID: 38619138, DOI: 10.1021/acsinfecdis.4c00119.Peer-Reviewed Original ResearchConceptsESI-MSElectrospray ionization mass spectrometryIonization mass spectrometryB-lactamase inhibitorsAcyl-enzyme complexMycobacterial cell wall synthesisMolecular dockingMass spectrometryActive siteInhibit BlaCPeptidoglycan transpeptidaseDiazabicyclooctaneSynthesisAntibiotic susceptibility testingCell wall synthesisInhibition kineticsDrug targetsB-lactamaseDurlobactamSusceptibility testingComplexDockingSpectrometryWall synthesisPeptidoglycan synthesis
2020
Drug-Resistant Tuberculosis A Glance at Progress and Global Challenges
Dousa K, Kurz S, Bark C, Bonomo R, Furin J. Drug-Resistant Tuberculosis A Glance at Progress and Global Challenges. Infectious Disease Clinics Of North America 2020, 34: 863-886. PMID: 33011048, DOI: 10.1016/j.idc.2020.06.001.Peer-Reviewed Original ResearchConceptsSecond-line medicationsMultidrug-resistant Mycobacterium tuberculosisDrug susceptibility predictionOral formulationMultinational trialDrug resistancePublic health threatEconomic burdenDiagnostic techniquesTuberculosisAdequate clinical resourcesClinical resourcesHealth threatLaboratory services
2016
Drug-Resistant Tuberculosis Challenges and Progress
Kurz S, Furin J, Bark C. Drug-Resistant Tuberculosis Challenges and Progress. Infectious Disease Clinics Of North America 2016, 30: 509-522. PMID: 27208770, PMCID: PMC4876017, DOI: 10.1016/j.idc.2016.02.010.Peer-Reviewed Original ResearchMeSH KeywordsAntitubercular AgentsDrug Resistance, Multiple, BacterialHumansMycobacterium tuberculosisTuberculosis, Multidrug-ResistantConceptsEmergence of drug-resistant tuberculosisCombination drug regimensEmergence of drug-resistant strainsDrug-resistant tuberculosisDrug-resistant strainsSpontaneous chromosomal mutationsCase of Mycobacterium tuberculosisDrug regimensClinical developmentAntimicrobial resistanceSupervised therapyChromosomal mutationsTB controlResistance mechanismsRegimensTherapy
2015
Kinetic and Structural Characterization of the Interaction of 6‑Methylidene Penem 2 with the β‑Lactamase from Mycobacterium tuberculosis
Hazra S, Kurz S, Wolff K, Nguyen L, Bonomo R, Blanchard J. Kinetic and Structural Characterization of the Interaction of 6‑Methylidene Penem 2 with the β‑Lactamase from Mycobacterium tuberculosis. Biochemistry 2015, 54: 5657-5664. PMID: 26237118, PMCID: PMC4795174, DOI: 10.1021/acs.biochem.5b00698.Peer-Reviewed Original ResearchConceptsB-lactamaseB-lactamPenem 2Inhibit BlaCActive site residuesB-lactam antibioticsMycobacterium tuberculosisCultures of M. tuberculosisRing openingSite residuesBoronic acidsConstitutive expressionSignificant growth inhibitionStructural characterizationMass spectrometryCompound formsCovalent complexM. tuberculosisGrowth inhibitionBinding inhibitorAcylated formEnzymeRingCompounds
2013
Can Inhibitor-Resistant Substitutions in the Mycobacterium tuberculosis β-Lactamase BlaC Lead to Clavulanate Resistance?: a Biochemical Rationale for the Use of β-Lactam–β-Lactamase Inhibitor Combinations
Kurz S, Wolff K, Hazra S, Bethel C, Hujer A, Smith K, Xu Y, Tremblay L, Blanchard J, Nguyen L, Bonomo R. Can Inhibitor-Resistant Substitutions in the Mycobacterium tuberculosis β-Lactamase BlaC Lead to Clavulanate Resistance?: a Biochemical Rationale for the Use of β-Lactam–β-Lactamase Inhibitor Combinations. Antimicrobial Agents And Chemotherapy 2013, 57: 6085-6096. PMID: 24060876, PMCID: PMC3837893, DOI: 10.1128/aac.01253-13.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SubstitutionAntitubercular Agentsbeta-Lactamase Inhibitorsbeta-LactamasesClavulanic AcidDrug Therapy, CombinationEscherichia coliExtensively Drug-Resistant TuberculosisGene ExpressionHumansMeropenemMicrobial Sensitivity TestsMutagenesis, Site-DirectedMycobacterium tuberculosisProtein EngineeringRecombinant ProteinsThienamycinsConceptsInhibitor combinationsResistance to clavulanic acidMultidrug resistanceDrug resistanceClavulanic acidExtensively drug-resistant M. tuberculosis strainsEmergence of multidrug resistanceCombination of meropenemDrug-resistant M. tuberculosis strainsPresence of ampicillinAmino acid residuesExtensively drug-resistantM. tuberculosis strainsNovel treatment strategiesInhibition of growthPotential therapeutic targetTreatment regimensTherapeutic modalitiesTreatment strategiesInhibitor resistanceM. tuberculosisEnzymatic assayImpaired inhibitionTherapeutic targetAcid resistance
2012
Reappraising the use of β-lactams to treat tuberculosis
Kurz S, Bonomo R. Reappraising the use of β-lactams to treat tuberculosis. Expert Review Of Anti-infective Therapy 2012, 10: 999-1006. PMID: 23106275, PMCID: PMC3728824, DOI: 10.1586/eri.12.96.Peer-Reviewed Original Research
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