Pyroptosis in defense against intracellular bacteria
Tài liệu tham khảo
Girardin, 2002, Intracellular vs extracellular recognition of pathogens – common concepts in mammals and flies, Trends Microbiol, 10, 193, 10.1016/S0966-842X(02)02334-X
Petit, 2022, Adaptations of intracellular bacteria to vacuolar or cytosolic niches, Trends Microbiol, 30, 736, 10.1016/j.tim.2022.01.015
Anand, 2020, The vacuole guard hypothesis: how intravacuolar pathogens fight to maintain the integrity of their beloved home, Curr. Opin. Microbiol, 54, 51, 10.1016/j.mib.2020.01.008
Gutierrez, 2022, Intracellular niche switching as host subversion strategy of bacterial pathogens, Curr. Opin. Cell Biol., 76, 10.1016/j.ceb.2022.102081
Sironi, 2015, Evolutionary insights into host–pathogen interactions from mammalian sequence data, Nat. Rev. Genet, 16, 224, 10.1038/nrg3905
Aleru, 2020, Battlefronts of evolutionary conflict between bacteria and animal hosts, Plos Pathog., 16, 10.1371/journal.ppat.1008797
Solé, R. Revisiting Leigh Van Valen’s “A New Evolutionary Law” , 1973. Biological Theory 17, 120–125 (2022).
Maltez, 2016, Reassessing the evolutionary Importance of Inflammasomes, J. Immunol., 196, 956, 10.4049/jimmunol.1502060
Jorgensen, 2017, Programmed cell death as a defence against infection, Nat. Rev. Immunol., 17, 151, 10.1038/nri.2016.147
Nozaki, 2022, Innate sensors trigger regulated cell death to combat intracellular infection, Annu Rev. Immunol., 40, 469, 10.1146/annurev-immunol-101320-011235
Shi, 2015, Cleavage of GSDMD by inflammatory caspases determines pyroptotic cell death, Nature, 526, 660, 10.1038/nature15514
Kayagaki, 2015, Caspase-11 cleaves gasdermin D for non-canonical inflammasome signalling, Nature, 526, 666, 10.1038/nature15541
Ding, 2016, Pore-forming activity and structural autoinhibition of the gasdermin family, Nature, 535, 111, 10.1038/nature18590
Liu, 2016, Inflammasome-activated gasdermin D causes pyroptosis by forming membrane pores, Nature, 535, 153, 10.1038/nature18629
Davis, 2011, The inflammasome NLRs in immunity, inflammation, and associated diseases, Annu Rev. Immunol., 29, 707, 10.1146/annurev-immunol-031210-101405
Vance, 2009, Patterns of pathogenesis: discrimination of pathogenic and nonpathogenic microbes by the innate immune system, Cell Host Microbe, 6, 10, 10.1016/j.chom.2009.06.007
Green, 2019, The coming decade of cell death research: five riddles, Cell, 177, 1094, 10.1016/j.cell.2019.04.024
Galluzzi, 2018, Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018, Cell Death Differ., 25, 486, 10.1038/s41418-017-0012-4
Elmore, 2007, Apoptosis: a review of programmed cell death, Toxicol. Pathol., 35, 495, 10.1080/01926230701320337
Doerflinger, 2020, Flexible usage and interconnectivity of diverse cell death pathways protect against intracellular infection, Immunity, 53
Abele, T.J. et al. Apoptotic signaling clears engineered Salmonella in an organ-specific manner. (2023) doi:10.1101/2023.05.06.539681.
Kovacs, 2017, Gasdermins: effectors of pyroptosis, Trends Cell Biol., 27, 673, 10.1016/j.tcb.2017.05.005
Ruan, 2018, Cryo-EM structure of the gasdermin A3 membrane pore, Nature, 557, 62, 10.1038/s41586-018-0058-6
Xia, 2021, Gasdermin D pore structure reveals preferential release of mature interleukin-1, Nature, 593, 607, 10.1038/s41586-021-03478-3
He, 2015, Gasdermin D is an executor of pyroptosis and required for interleukin-1β secretion, Cell Res, 25, 1285, 10.1038/cr.2015.139
Schneider, 2017, The inflammasome drives GSDMD-independent secondary pyroptosis and IL-1 release in the absence of caspase-1 protease activity, Cell Rep., 21, 3846, 10.1016/j.celrep.2017.12.018
Saeki, 2020, Gasdermin D‐independent release of interleukin‐1β by living macrophages in response to mycoplasmal lipoproteins and lipopeptides, Immunology, 161, 114, 10.1111/imm.13230
Kayagaki, 2021, NINJ1 mediates plasma membrane rupture during lytic cell death, Nature, 591, 131, 10.1038/s41586-021-03218-7
Loomis, 2019, Diverse small molecules prevent macrophage lysis during pyroptosis, Cell Death Dis., 10, 326, 10.1038/s41419-019-1559-4
Borges, 2022, Glycine inhibits NINJ1 membrane clustering to suppress plasma membrane rupture in cell death, Elife, 11, 10.7554/eLife.78609
Hansen, 1994, Extra- and intracellular amino acid concentrations in continuous Chinese hamster ovary cell culture, Appl. Microbiol Biotechnol., 41, 560, 10.1007/BF00178489
Jorgensen, 2016, Pyroptosis triggers pore-induced intracellular traps (PITs) that capture bacteria and lead to their clearance by efferocytosis, J. Exp. Med., 213, 2113, 10.1084/jem.20151613
Wright, 2016, The killer protein Gasdermin D, Cell Death Differ., 23, 1897, 10.1038/cdd.2016.100
Estfanous, 2021, Gasdermin D restricts Burkholderia cenocepacia infection in vitro and in vivo, Sci. Rep. -uk, 11, 855, 10.1038/s41598-020-79201-5
Torre‐Minguela, 2021, Gasdermins mediate cellular release of mitochondrial DNA during pyroptosis and apoptosis, Faseb J., 35, 10.1096/fj.202100085R
Du, G. et al. ROS-dependent palmitoylation is an obligate licensing modification for GSDMD pore formation. Biorxiv 2023.03.07.531538 (2023) doi:10.1101/2023.03.07.531538.
López-Pérez, 2021, TAK1 inhibition elicits mitochondrial ROS to block intracellular bacterial colonization, Proc. Natl. Acad. Sci., 118, 10.1073/pnas.2023647118
Bjanes, 2021, Genetic targeting of Card19 is linked to disrupted NINJ1 expression, impaired cell lysis, and increased susceptibility to Yersinia infection, Plos Pathog., 17, 10.1371/journal.ppat.1009967
Chen, 2014, The neutrophil NLRC4 inflammasome selectively promotes IL-1β maturation without pyroptosis during acute salmonella challenge, CellReports, 8, 570
Bakele, 2014, Localization and functionality of the inflammasome in neutrophils*, J. Biol. Chem., 289, 5320, 10.1074/jbc.M113.505636
Karmakar, 2016, Neutrophil P2×7 receptors mediate NLRP3 inflammasome-dependent IL-1β secretion in response to ATP, Nat. Commun., 7, 10555, 10.1038/ncomms10555
Goldberg, 2017, β-Hydroxybutyrate deactivates neutrophil NLRP3 inflammasome to relieve gout flares, Cell Rep., 18, 2077, 10.1016/j.celrep.2017.02.004
Heilig, 2018, The Gasdermin‐D pore acts as a conduit for IL‐1β secretion in mice, Eur. J. Immunol., 48, 584, 10.1002/eji.201747404
Kovacs, 2020, Neutrophil caspase-11 is essential to defend against a cytosol-invasive bacterium, Cell Rep., 32, 10.1016/j.celrep.2020.107967
Karmakar, 2020, N-GSDMD trafficking to neutrophil organelles facilitates IL-1β release independently of plasma membrane pores and pyroptosis, Nat. Commun., 11, 2212, 10.1038/s41467-020-16043-9
Santoni, 2022, Caspase-1-driven neutrophil pyroptosis and its role in host susceptibility to Pseudomonas aeruginosa, Plos Pathog., 18, 10.1371/journal.ppat.1010305
Oh, 2022, Neutrophil inflammasomes sense the subcellular delivery route of translocated bacterial effectors and toxins, Cell Rep., 41, 10.1016/j.celrep.2022.111688
Chen, 2018, Noncanonical inflammasome signaling elicits gasdermin D-dependent neutrophil extracellular traps, Sci. Immunol. 3, eaar6676, 10.1126/sciimmunol.aar6676
Sollberger, 2018, Gasdermin D plays a vital role in the generation of neutrophil extracellular traps, Sci. Immunol. 3, eaar6689, 10.1126/sciimmunol.aar6689
Aachoui, 2013, Caspase-11 protects against bacteria that escape the vacuole, Science, 339, 1230751, 10.1126/science.1230751
Churchill, 2022, Epithelial pyroptosis in host defense, J. Mol. Biol., 434, 10.1016/j.jmb.2021.167278
Knodler, 2010, Dissemination of invasive Salmonella via bacterial-induced extrusion of mucosal epithelia, Proc. Natl. Acad. Sci., 107, 17733, 10.1073/pnas.1006098107
Sellin, 2014, Epithelium-Intrinsic NAIP/NLRC4 inflammasome drives infected enterocyte expulsion to restrict salmonella replication in the intestinal mucosa, Cell Host Microbe, 16, 237, 10.1016/j.chom.2014.07.001
Rauch, 2017, NAIP-NLRC4 inflammasomes coordinate intestinal epithelial cell expulsion with eicosanoid and IL-18 release via activation of caspase-1 and -8, Immunity, 46, 649, 10.1016/j.immuni.2017.03.016
Sellin, 2018, Consequences of epithelial inflammasome activation by bacterial pathogens, J. Mol. Biol., 430, 193, 10.1016/j.jmb.2017.03.031
Hausmann, 2020, Intestinal epithelial NAIP/NLRC4 restricts systemic dissemination of the adapted pathogen Salmonella Typhimurium due to site-specific bacterial PAMP expression, Mucosal Immunol., 13, 530, 10.1038/s41385-019-0247-0
Nozaki, 2022, Caspase-7 activates ASM to repair gasdermin and perforin pores, Nature, 606, 960, 10.1038/s41586-022-04825-8
Nozaki, 2023, Bucket lists must be completed during cell death, Trends Cell Biol., 10.1016/j.tcb.2023.02.008
Winter, 2010, Gut inflammation provides a respiratory electron acceptor for Salmonella, Nature, 467, 426, 10.1038/nature09415
Brokatzky, 2022, Pyroptosis in host defence against bacterial infection, Dis. Model Mech., 15, 10.1242/dmm.049414
Wanford, 2022, Reprogramming of cell death pathways by bacterial effectors as a widespread virulence strategy, Infect. Immun., 90, e00614, 10.1128/iai.00614-21
Hagar, 2013, Cytoplasmic LPS activates caspase-11: implications in TLR4-independent endotoxic shock, Science, 341, 1250, 10.1126/science.1240988
Kayagaki, 2013, Noncanonical inflammasome activation by intracellular LPS independent of TLR4, Science, 341, 1246, 10.1126/science.1240248
Lagrange, 2018, Human caspase-4 detects tetra-acylated LPS and cytosolic Francisella and functions differently from murine caspase-11, Nat. Commun., 9, 242, 10.1038/s41467-017-02682-y
Kobayashi, 2013, The shigella OspC3 effector inhibits caspase-4, antagonizes inflammatory cell death, and promotes epithelial infection, Cell Host Microbe, 13, 570, 10.1016/j.chom.2013.04.012
Oh, 2021, Shigella OspC3 suppresses murine cytosolic LPS sensing, Iscience, 24, 10.1016/j.isci.2021.102910
Li, 2021, Shigella evades pyroptosis by arginine ADP-riboxanation of caspase-11, Nature, 599, 290, 10.1038/s41586-021-04020-1
Luchetti, 2021, Shigella ubiquitin ligase IpaH7.8 targets gasdermin D for degradation to prevent pyroptosis and enable infection, Cell Host Microbe, 29
Yin, 2023, Insights into the GSDMB-mediated cellular lysis and its targeting by IpaH7.8, Nat. Commun., 14, 61, 10.1038/s41467-022-35725-0
Zhong, 2023, Structural mechanisms for regulation of GSDMB pore-forming activity, Nature, 616, 598, 10.1038/s41586-023-05872-5
Wang, 2023, Structural basis for GSDMB pore formation and its targeting by IpaH7.8, Nature, 616, 590, 10.1038/s41586-023-05832-z
Hansen, 2021, Pathogenic ubiquitination of GSDMB inhibits NK cell bactericidal functions, Cell, 184
Rastogi, 2022, Interaction of mycobacteria with host cell inflammasomes, Front Immunol., 13, 10.3389/fimmu.2022.791136
Chen, 2016, Pyroptosis is driven by non-selective gasdermin-D pore and its morphology is different from MLKL channel-mediated necroptosis, Cell Res, 26, 1007, 10.1038/cr.2016.100
Chai, Q. et al. A bacterial phospholipid phosphatase inhibits host pyroptosis by hijacking ubiquitin. Science 378, eabq0132 (2022).
Rastogi, 2021, Mycobacterium tuberculosis inhibits the NLRP3 inflammasome activation via its phosphokinase PknF, Plos Pathog., 17, 10.1371/journal.ppat.1009712
Lara-Tejero, 2006, Role of the caspase-1 inflammasome in Salmonella typhimuriumpathogenesis, J. Exp. Med., 203, 1407, 10.1084/jem.20060206
Raupach, 2006, Caspase-1-mediated activation of interleukin-1 (IL-1) and IL-18 contributes to innate immune defenses against salmonella enterica serovar typhimurium infection, Infect. Immun., 74, 4922, 10.1128/IAI.00417-06
Broz, 2010, Redundant roles for inflammasome receptors NLRP3 and NLRC4 in host defense against Salmonella, J. Exp. Med., 207, 1745, 10.1084/jem.20100257
Franchi, 2012, NLRC4-driven interleukin-1β production discriminates between pathogenic and commensal bacteria and promotes host intestinal defense, Nat. Immunol., 13, 449, 10.1038/ni.2263
Broz, 2012, Caspase-11 increases susceptibility to Salmonella infection in the absence of caspase-1, Nature, 490, 288, 10.1038/nature11419
Knodler, 2014, Noncanonical inflammasome activation of caspase-4/caspase-11 mediates epithelial defenses against enteric bacterial pathogens, Cell Host Microbe, 16, 249, 10.1016/j.chom.2014.07.002
Miao, 2010, Caspase-1-induced pyroptosis is an innate immune effector mechanism against intracellular bacteria, Nat. Immunol., 11, 1136, 10.1038/ni.1960
Miao, 2010, Innate immune detection of the type III secretion apparatus through the NLRC4 inflammasome, Proc. Natl. Acad. Sci., 107, 3076, 10.1073/pnas.0913087107
Aachoui, 2015, Canonical inflammasomes drive IFN-γ to prime caspase-11 in defense against a cytosol-invasive bacterium, Cell Host Microbe, 18, 320, 10.1016/j.chom.2015.07.016
Wang, 2019, Gasdermin D protects from melioidosis through pyroptosis and direct killing of bacteria, J. Immunol., 202, 3468, 10.4049/jimmunol.1900045
Durán, 2001, Chromobacterium violaceum: a review of pharmacological and industiral perspectives, Crit. Rev. Microbiol, 27, 201, 10.1080/20014091096747
Macher, 1982, Chronic granulomatous disease of childhood and chromobacterium violaceum infections in the Southeastern United States, Ann. Intern Med, 97, 51, 10.7326/0003-4819-97-1-51
Yang, 2011, Chromobacterium violaceum infection: a clinical review of an important but neglected infection, J. Chin. Med. Assoc. Jcma, 74, 435, 10.1016/j.jcma.2011.08.013
Miki, 2010, Chromobacterium pathogenicity island 1 type III secretion system is a major virulence determinant for Chromobacterium violaceum‐induced cell death in hepatocytes, Mol. Microbiol, 77, 855, 10.1111/j.1365-2958.2010.07248.x
Maltez, 2015, Inflammasomes coordinate pyroptosis and natural killer cell cytotoxicity to clear infection by a ubiquitous environmental bacterium, Immunity, 43, 987, 10.1016/j.immuni.2015.10.010
Franchi, 2009, Function of Nod‐like receptors in microbial recognition and host defense, Immunol. Rev., 227, 106, 10.1111/j.1600-065X.2008.00734.x
Martin, 2007, Toxicity ofChromobacterium subtsugae to Southern Green Stink Bug (Heteroptera: Pentatomidae) and Corn Rootworm (Coleoptera: Chrysomelidae), J. Econ. Èntomol., 107, 680, 10.1603/0022-0493(2007)100[680:TOCSTS]2.0.CO;2
Martin, 2007, Chromobacterium subtsugae sp. nov., a betaproteobacterium toxic to Colorado potato beetle and other insect pests, Int. J. Syst. Evol. Microbiol, 57, 993, 10.1099/ijs.0.64611-0
Brinkworth, 2020, Cell-autonomous immunity and the pathogen-mediated evolution of humans: or how our prokaryotic and single-celled origins affect the human evolutionary story, Q Rev. Biol., 95, 215, 10.1086/710389
Cadwell, 2016, Crosstalk between autophagy and inflammatory signalling pathways: balancing defence and homeostasis, Nat. Rev. Immunol., 16, 661, 10.1038/nri.2016.100
Deretic, 2018, Autophagy Balances Inflamm. innate Immun. Autophagy, 14, 243
Guo, R., Wang, H. & Cui, N. Autophagy Regulation on Pyroptosis: Mechanism and Medical Implication in Sepsis. Mediat Inflamm 2021, 9925059 (2021).
Pant, 2022, Interactions of autophagy and the immune system in health and diseases, Autophagy Rep., 1, 438, 10.1080/27694127.2022.2119743
Saitoh, 2008, Loss of the autophagy protein Atg16L1 enhances endotoxin-induced IL-1β production, Nature, 456, 264, 10.1038/nature07383
Shi, 2012, Activation of autophagy by inflammatory signals limits IL-1β production by targeting ubiquitinated inflammasomes for destruction, Nat. Immunol., 13, 255, 10.1038/ni.2215
Nakahira, 2011, Autophagy proteins regulate innate immune responses by inhibiting the release of mitochondrial DNA mediated by the NALP3 inflammasome, Nat. Immunol., 12, 222, 10.1038/ni.1980
Zhong, 2016, NF-κB restricts inflammasome activation via elimination of damaged mitochondria, Cell, 164, 896, 10.1016/j.cell.2015.12.057
Sumpter, 2016, Fanconi anemia proteins function in mitophagy and immunity, Cell, 165, 867, 10.1016/j.cell.2016.04.006
Suzuki, 2007, Differential regulation of caspase-1 activation, pyroptosis, and autophagy via Ipaf and ASC in Shigella-infected macrophages, PLoS Pathog., 3, 10.1371/journal.ppat.0030111
Meunier, 2014, Caspase-11 activation requires lysis of pathogen-containing vacuoles by IFN-induced GTPases, Nature, 509, 366, 10.1038/nature13157
Kimura, 2015, TRIM-mediated precision autophagy targets cytoplasmic regulators of innate immunity, J. Cell Biol., 210, 973, 10.1083/jcb.201503023
Liu, 2016, TRIM11 suppresses AIM2 inflammasome by degrading AIM2 via p62-dependent selective autophagy, Cell Rep., 16, 1988, 10.1016/j.celrep.2016.07.019
Mahenthiralingam, 2008, Burkholderia cepacia complex bacteria: opportunistic pathogens with important natural biology, J. Appl. Microbiol, 104, 1539, 10.1111/j.1365-2672.2007.03706.x
Krause, 2018, CASP4/caspase-11 promotes autophagosome formation in response to bacterial infection, Autophagy, 14, 1928, 10.1080/15548627.2018.1491494
Harvest, 2022, Autophagy may allow a cell to forbear pyroptosis when confronted with cytosol-invasive bacteria, Front Immunol., 13, 10.3389/fimmu.2022.871190
Pilla-Moffett, 2016, Interferon-inducible GTPases in host resistance, inflammation and disease, J. Mol. Biol., 428, 3495, 10.1016/j.jmb.2016.04.032
Rafeld, 2021, Interferon-induced GTPases orchestrate host cell-autonomous defence against bacterial pathogens, Biochem Soc. T, 49, 1287, 10.1042/BST20200900
Kim, 2012, IFN-Inducible GTPases in Host Cell Defense, Cell Host Microbe, 12, 432, 10.1016/j.chom.2012.09.007
Pilla, 2014, Guanylate binding proteins promote caspase-11–dependent pyroptosis in response to cytoplasmic LPS, Proc. Natl. Acad. Sci., 111, 6046, 10.1073/pnas.1321700111
Cerqueira, 2018, Guanylate-binding protein 5 licenses caspase-11 for Gasdermin-D mediated host resistance to Brucella abortus infection, Plos Pathog., 14, 10.1371/journal.ppat.1007519
Santos, 2018, LPS targets host guanylate‐binding proteins to the bacterial outer membrane for non‐canonical inflammasome activation, Embo J., 37, 10.15252/embj.201798089
Santos, 2020, Human GBP1 binds LPS to initiate assembly of a caspase-4 activating platform on cytosolic bacteria, Nat. Commun., 11, 3276, 10.1038/s41467-020-16889-z
Wandel, 2020, Guanylate-binding proteins convert cytosolic bacteria into caspase-4 signaling platforms, Nat. Immunol., 282
Park, E.-S. et al. A hierarchical GBP network promotes cytosolic LPS recognition and sepsis. Biorxiv 2021.08.25.457662 (2021) doi:10.1101/2021.08.25.457662.
Fisch, 2019, Human GBP1 is a microbe‐specific gatekeeper of macrophage apoptosis and pyroptosis, Embo J., 38, 10.15252/embj.2018100926
Fisch, 2020, Human GBP1 Differentially Targets Salmonella and Toxoplasma to License Recognition of Microbial Ligands and Caspase-Mediated Death, Cell Rep., 32, 10.1016/j.celrep.2020.108008
Dickinson, 2023, LPS-aggregating proteins GBP1 and GBP2 are each sufficient to enhance caspase-4 activation both in cellulo and in vitro, Proc. Natl. Acad. Sci., 120, 10.1073/pnas.2216028120
Kutsch, 2020, Direct binding of polymeric GBP1 to LPS disrupts bacterial cell envelope functions, Embo J., 39, 10.15252/embj.2020104926
Finethy, 2017, Inflammasome activation by bacterial outer membrane vesicles requires guanylate binding proteins, Mbio, 8, e01188, 10.1128/mBio.01188-17
Zhu, S. et al. Cryo-ET of a human GBP coatomer governing cell-autonomous innate immunity to infection. Biorxiv 2021.08.26.457804 (2021) doi:10.1101/2021.08.26.457804.
Kuhm, T. et al. Structural basis of membrane targeting and coatomer assembly by human GBP1. bioRxiv 2023.03.28.534355 (2023) doi:10.1101/2023.03.28.534355.
Goers, 2023, Shigella IpaH9.8 limits GBP1-dependent LPS release from intracytosolic bacteria to suppress caspase-4 activation, Proc. Natl. Acad. Sci., 120, 10.1073/pnas.2218469120
Man, 2015, The transcription factor IRF1 and guanylate-binding proteins target activation of the AIM2 inflammasome by Francisella infection, Nat. Immunol., 16, 467, 10.1038/ni.3118
Meunier, 2015, Guanylate-binding proteins promote activation of the AIM2 inflammasome during infection with Francisella novicida, Nat. Immunol., 16, 476, 10.1038/ni.3119
Wallet, 2017, IFN-γ extends the immune functions of Guanylate Binding Proteins to inflammasome-independent antibacterial activities during Francisella novicida infection, Plos Pathog., 13, 10.1371/journal.ppat.1006630
Man, 2016, IRGB10 liberates bacterial ligands for sensing by the AIM2 and caspase-11-NLRP3 inflammasomes, Cell, 167
Liu, 2018, Constitutive interferon maintains GBP expression required for release of bacterial components upstream of pyroptosis and anti-DNA responses, Cell Rep., 24
Xavier, 2020, hGBP1 coordinates chlamydia restriction and inflammasome activation through sequential GTP hydrolysis, Cell Rep., 31, 10.1016/j.celrep.2020.107667
Mariathasan, 2006, Cryopyrin activates the inflammasome in response to toxins and ATP, Nature, 440, 228, 10.1038/nature04515
Eren, 2020, Irgm2 and Gate‐16 cooperatively dampen Gram‐negative bacteria‐induced caspase‐11 response, Embo Rep., 21, 10.15252/embr.202050829
Finethy, 2020, Dynamin‐related Irgm proteins modulate LPS‐induced caspase‐11 activation and septic shock, Embo Rep., 21, 10.15252/embr.202050830
Zhou, 2020, Granzyme A from cytotoxic lymphocytes cleaves GSDMB to trigger pyroptosis in target cells, Science, 368, 10.1126/science.aaz7548
Rogers, 2017, Cleavage of DFNA5 by caspase-3 during apoptosis mediates progression to secondary necrotic/pyroptotic cell death, Nat. Commun., 8, 14128, 10.1038/ncomms14128
Wang, 2017, Chemotherapy drugs induce pyroptosis through caspase-3 cleavage of a gasdermin, Nature, 547, 99, 10.1038/nature22393
Lord, 2003, Granzyme B: a natural born killer, Immunol. Rev., 193, 31, 10.1034/j.1600-065X.2003.00044.x
Zhang, 2020, Gasdermin E suppresses tumour growth by activating anti-tumour immunity, Nature, 579, 415, 10.1038/s41586-020-2071-9
Orning, 2018, Pathogen blockade of TAK1 triggers caspase-8–dependent cleavage of gasdermin D and cell death, Sci. 30, eaau2818-, 12
Sarhan, J. et al. Caspase-8 induces cleavage of gasdermin D to elicit pyroptosis during Yersiniainfection. Proceedings of the National Academy of Sciences 67, 201809548–10 (2018).
Chen, 2019, Extrinsic and intrinsic apoptosis activate pannexin‐1 to drive NLRP3 inflammasome assembly, Embo J., 38, 10.15252/embj.2019101638
Hou, 2020, PD-L1-mediated gasdermin C expression switches apoptosis to pyroptosis in cancer cells and facilitates tumour necrosis, Nat. Cell Biol., 22, 1264, 10.1038/s41556-020-0575-z
Zhang, 2021, The metabolite α-KG induces GSDMC-dependent pyroptosis through death receptor 6-activated caspase-8, Cell Res, 31, 980, 10.1038/s41422-021-00506-9
Deng, 2022, Streptococcal pyrogenic exotoxin B cleaves GSDMA and triggers pyroptosis, Nature, 602, 496, 10.1038/s41586-021-04384-4
LaRock, 2022, Group A Streptococcus induces GSDMA-dependent pyroptosis in keratinocytes, Nature, 605, 527, 10.1038/s41586-022-04717-x
Panganiban, 2023, Direct cleavage and activation of gasdermin B by allergens, Allergy, 10.1111/all.15763
Tamura, 2007, Members of a novel gene family, Gsdm, are expressed exclusively in the epithelium of the skin and gastrointestinal tract in a highly tissue-specific manner, Genomics, 89, 618, 10.1016/j.ygeno.2007.01.003
Li, 2022, Role of caspases and gasdermin a during HSV-1 infection in mice, Viruses, 14, 2034, 10.3390/v14092034
Harvest, 2023, An innate granuloma eradicates an environmental pathogen using Gsdmd and Nos2, Biorxiv 2023. 03. 07. 531568
Tsuji, 2004, Roles of caspase-1 in Listeria infection in mice, Int. Immunol., 16, 335, 10.1093/intimm/dxh041
Ceballos-Olvera, 2011, Inflammasome-dependent pyroptosis and IL-18 protect against burkholderia pseudomallei lung infection while IL-1β is deleterious, PLoS Pathog., 7, 10.1371/journal.ppat.1002452
Exconde, P.M. et al. The tetrapeptide sequence of IL-1β regulates its recruitment and activation by inflammatory caspases. Biorxiv 2023.02.16.528859 (2023) doi:10.1101/2023.02.16.528859.
