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
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
2013
A Chemical Biological Strategy to Facilitate Diabetic Wound Healing
Gooyit M, Peng Z, Wolter W, Pi H, Ding D, Hesek D, Lee M, Boggess B, Champion M, Suckow M, Mobashery S, Chang M. A Chemical Biological Strategy to Facilitate Diabetic Wound Healing. ACS Chemical Biology 2013, 9: 105-110. PMID: 24053680, PMCID: PMC3947039, DOI: 10.1021/cb4005468.Peer-Reviewed Original Research
2012
Role of Catecholate Siderophores in Gram-Negative Bacterial Colonization of the Mouse Gut
Pi H, Jones S, Mercer L, Meador J, Caughron J, Jordan L, Newton S, Conway T, Klebba P. Role of Catecholate Siderophores in Gram-Negative Bacterial Colonization of the Mouse Gut. PLOS ONE 2012, 7: e50020. PMID: 23209633, PMCID: PMC3510177, DOI: 10.1371/journal.pone.0050020.Peer-Reviewed Original ResearchA Putative P-Type ATPase Required for Virulence and Resistance to Haem Toxicity in Listeria monocytogenes
McLaughlin H, Xiao Q, Rea R, Pi H, Casey P, Darby T, Charbit A, Sleator R, Joyce S, Cowart R, Hill C, Klebba P, Gahan C. A Putative P-Type ATPase Required for Virulence and Resistance to Haem Toxicity in Listeria monocytogenes. PLOS ONE 2012, 7: e30928. PMID: 22363518, PMCID: PMC3283593, DOI: 10.1371/journal.pone.0030928.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesAnimalsBacterial ProteinsBase SequenceBiological AssayComputational BiologyDrug Resistance, BacterialGene Expression Regulation, BacterialGenes, BacterialGenetic LociHemeHomeostasisIronListeria monocytogenesListeriosisMiceMolecular Sequence DataMothsMutagenesis, InsertionalMutationPlasmidsReal-Time Polymerase Chain ReactionRepressor ProteinsVirulenceConceptsPutative P-type ATPaseFerric uptake regulatorUptake of haemIntracellular pathogen Listeria monocytogenesWax moth Galleria mellonellaP-type ATPaseAcquisition of ironPathogen Listeria monocytogenesMoth Galleria mellonellaIron-deficient mediumMembrane proteinsMutantsHaem toxicityFree haemAlternative infection modelGalleria mellonellaIron homeostasisInhibition of growthFrvAVirulenceListeria monocytogenesHaemVirulence potentialFurDeficient medium
2011
Sortase independent and dependent systems for acquisition of haem and haemoglobin in Listeria monocytogenes
Xiao Q, Jiang X, Moore K, Shao Y, Pi H, Dubail I, Charbit A, Newton S, Klebba P. Sortase independent and dependent systems for acquisition of haem and haemoglobin in Listeria monocytogenes. Molecular Microbiology 2011, 80: 1581-1597. PMID: 21545655, PMCID: PMC3115469, DOI: 10.1111/j.1365-2958.2011.07667.x.Peer-Reviewed Original Research