2023
Clostridioides difficile ferrosome organelles combat nutritional immunity
Pi H, Sun R, McBride J, Kruse A, Gibson-Corley K, Krystofiak E, Nicholson M, Spraggins J, Zhou Q, Skaar E. Clostridioides difficile ferrosome organelles combat nutritional immunity. Nature 2023, 623: 1009-1016. PMID: 37968387, PMCID: PMC10822667, DOI: 10.1038/s41586-023-06719-9.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBacterial ProteinsCell MembraneClostridioides difficileClostridium InfectionsCryoelectron MicroscopyDisease Models, AnimalElectron Microscope TomographyFerric CompoundsHomeostasisHost Microbial InteractionsInflammationIntestinesIronLeukocyte L1 Antigen ComplexMiceMicrobial ViabilityOrganellesConceptsFerric uptake regulator FurCryo-electron tomographyRegulator FurGram-negative bacteriaMembrane proteinsNutritional immunityIron uptakeCellular membranesDetoxification strategiesIron homeostasisForms of lifeStore ironBacterial pathogensIron sequestrationBiomineralization processPhosphate biomineralsRecent studiesImportant roleBacterial colonizationOrganellesInflamed gutMouse modelProteinTransportersHomeostasis
2016
The Listeria monocytogenes Fur‐regulated virulence protein FrvA is an Fe(II) efflux P1B4‐type ATPase
Pi H, Patel S, Argüello J, Helmann J. The Listeria monocytogenes Fur‐regulated virulence protein FrvA is an Fe(II) efflux P1B4‐type ATPase. Molecular Microbiology 2016, 100: 1066-1079. PMID: 26946370, PMCID: PMC4914386, DOI: 10.1111/mmi.13368.Peer-Reviewed Original Research
2015
Structure–Activity Relationship for the Oxadiazole Class of Antibiotics
Spink E, Ding D, Peng Z, Boudreau M, Leemans E, Lastochkin E, Song W, Lichtenwalter K, O’Daniel P, Testero S, Pi H, Schroeder V, Wolter W, Antunes N, Suckow M, Vakulenko S, Chang M, Mobashery S. Structure–Activity Relationship for the Oxadiazole Class of Antibiotics. Journal Of Medicinal Chemistry 2015, 58: 1380-1389. PMID: 25590813, PMCID: PMC6863074, DOI: 10.1021/jm501661f.Peer-Reviewed Original ResearchConceptsMethicillin-resistant S. aureusStructure-activity relationshipsOxadiazole classClasses of antibioticsLinezolid-resistant S. aureusS. aureusMRSA infectionLead structuresCrystal structureMouse modelIndol-5Lower clearanceExhibit activityAntibioticsSilico dockingBacterium Staphylococcus aureusStaphylococcus aureusInfectionGram-positive bacterium Staphylococcus aureusCell wall biosynthesisPenicillin-binding proteinsGreat promiseAureus
2014
Discovery of a New Class of Non-β-lactam Inhibitors of Penicillin-Binding Proteins with Gram-Positive Antibacterial Activity
O’Daniel P, Peng Z, Pi H, Testero S, Ding D, Spink E, Leemans E, Boudreau M, Yamaguchi T, Schroeder V, Wolter W, Llarrull L, Song W, Lastochkin E, Kumarasiri M, Antunes N, Espahbodi M, Lichtenwalter K, Suckow M, Vakulenko S, Mobashery S, Chang M. Discovery of a New Class of Non-β-lactam Inhibitors of Penicillin-Binding Proteins with Gram-Positive Antibacterial Activity. Journal Of The American Chemical Society 2014, 136: 3664-3672. PMID: 24517363, PMCID: PMC3985699, DOI: 10.1021/ja500053x.Peer-Reviewed Original ResearchConceptsMethicillin-resistant Staphylococcus aureusPenicillin-binding protein 2aLinezolid-resistant methicillin-resistant Staphylococcus aureusNon-β-lactam antibioticsGlobal public health concernSerious global public health concernPublic health concernClasses of antibioticsMouse modelVivo efficacyOral bioavailabilityProtein 2ABactericidal activityGram-positive antibacterial activityStaphylococcus aureusNon-β-lactam inhibitorsInfectionPenicillin binding proteinsAntibioticsAntibacterial activityVancomycin