2024
Antagonistic nanobodies implicate mechanism of GSDMD pore formation and potential therapeutic application
Schiffelers L, Tesfamariam Y, Jenster L, Diehl S, Binder S, Normann S, Mayr J, Pritzl S, Hagelauer E, Kopp A, Alon A, Geyer M, Ploegh H, Schmidt F. Antagonistic nanobodies implicate mechanism of GSDMD pore formation and potential therapeutic application. Nature Communications 2024, 15: 8266. PMID: 39327452, PMCID: PMC11427689, DOI: 10.1038/s41467-024-52110-1.Peer-Reviewed Original ResearchConceptsMembrane insertionGasdermin DN-terminal domainCleavage of gasdermin DPore formationPro-inflammatory caspasesPyroptosis to apoptosisActivated caspase-3Caspase-1 activationTarget membraneCaspase-3Assembled poresPlasma membraneCytosolic expressionLiving cellsConformational changesEnhanced caspase-1 activityOligomerizationPotential therapeutic applicationsInflammasome activationNanobodiesPyroptosisStudy pore formationMembraneTherapeutic applicationsNative architecture of a human GBP1 defense complex for cell-autonomous immunity to infection
Zhu S, Bradfield C, Maminska A, Park E, Kim B, Kumar P, Huang S, Kim M, Zhang Y, Bewersdorf J, MacMicking J. Native architecture of a human GBP1 defense complex for cell-autonomous immunity to infection. Science 2024, 383: eabm9903. PMID: 38422126, DOI: 10.1126/science.abm9903.Peer-Reviewed Original ResearchConceptsGuanylate-binding proteinsCaspase-4Surface of Gram-negative bacteriaGuanosine triphosphate hydrolysisImmunity to infectionInnate immunity to infectionCryo-electron tomographyGram-negative bacteriaImmunity proteinSignaling platformsMembrane insertionHuman cellsNative structureCombat infectionsLipopolysaccharide releaseGasdermin DExtended conformationLiving organismsProteinDefense complexCellsNative architectureGBP1BacteriaInfection
2023
Pyroptosis in cardiovascular diseases: Pumping gasdermin on the fire
Yarovinsky T, Su M, Chen C, Xiang Y, Tang W, Hwa J. Pyroptosis in cardiovascular diseases: Pumping gasdermin on the fire. Seminars In Immunology 2023, 69: 101809. PMID: 37478801, PMCID: PMC10528349, DOI: 10.1016/j.smim.2023.101809.Peer-Reviewed Original ResearchConceptsPost-translational modificationsAcute cardiovascular eventsChronic cardiovascular diseaseCardiovascular diseaseSmall molecule inhibitorsPyroptosis resultsGenetic toolsGasdermin proteinsWhole organismInflammatory caspasesCardiovascular eventsCell deathMolecule inhibitorsCell typesProteolytic cleavageCellular mechanismsActivation of inflammasomesCardiovascular systemKnockout animalsAmplification of inflammationRole of pyroptosisPro-inflammatory processesDifferent cellsNovel therapeutic approachesPyroptosisGasdermin D licenses MHCII induction to maintain food tolerance in small intestine
He K, Wan T, Wang D, Hu J, Zhou T, Tao W, Wei Z, Lu Q, Zhou R, Tian Z, Flavell R, Zhu S. Gasdermin D licenses MHCII induction to maintain food tolerance in small intestine. Cell 2023, 186: 3033-3048.e20. PMID: 37327784, DOI: 10.1016/j.cell.2023.05.027.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCaspase 3GasderminsImmune ToleranceIntestine, SmallMiceNeoplasm ProteinsPyroptosisConceptsIntestinal epithelial cellsCleavage fragmentsSmall intestineCaspase-3/7 inhibitorRegulatory hubTolerance phenotypeN-terminal fragmentHost cellsDifferential cleavageCaspase-3/7Upper small intestineTranscription of CIITAGasdermin DEpithelial cellsMHCII deficiencyMHCII inductionDietary antigensTr1 cellsImmune toleranceProtective immunityFood toleranceForeign antigensMHCII moleculesMiceCells
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