2021
“One-Two Punch”: Synergistic ß-Lactam Combinations for Mycobacterium abscessus and Target Redundancy in the Inhibition of Peptidoglycan Synthesis Enzymes
Nguyen D, Dousa K, Kurz S, Brown S, Drusano G, Holland S, Kreiswirth B, Boom W, Daley C, Bonomo R. “One-Two Punch”: Synergistic ß-Lactam Combinations for Mycobacterium abscessus and Target Redundancy in the Inhibition of Peptidoglycan Synthesis Enzymes. Clinical Infectious Diseases 2021, 73: 1532-1536. PMID: 34113990, PMCID: PMC8677594, DOI: 10.1093/cid/ciab535.Peer-Reviewed Original ResearchConceptsPeptidoglycan synthesis enzymesMinimum inhibitory concentration of clinical isolatesB-lactamCombination of imipenemSynthesis enzymesSynergistic in vitroClinical isolatesMinimum inhibitory concentrationMycobacterium abscessusClinical trialsMycobacterial infectionAbscessusEnzymeCeftarolineImipenem
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
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