Gasdermins induce the release of mitochondrial DNA during pyroptosis and apoptosis

Gasdermins induce the release of mitochondrial DNA during pyroptosis and apoptosis | Research Square window.SnipcartSettings = { analytics: { enabled: false } }; (function() { var accessVector = localStorage.getItem('access_vector') || ''; window.dataLayer = window.dataLayer || []; if (accessVector) { window.dataLayer.push({ user: { profile: { profileInfo: { snid: accessVector } } } }); } })(); (function(w,d,s,l,i){w[l]=w[l]||[];w[l].push({'gtm.start':new Date().getTime(),event:'gtm.js'});var f=d.getElementsByTagName(s)[0],j=d.createElement(s),dl=l!='dataLayer'?'&l='+l:'';j.async=true;j.src='https://www.googletagmanager.com/gtm.js?id='+i+dl;f.parentNode.insertBefore(j,f);})(window,document,'script','dataLayer','GTM-K279D39R'); Browse Preprints In Review Journals COVID-19 Preprints AJE Video Bytes Research Tools Research Promotion AJE Professional Editing AJE Rubriq About Preprint Platform In Review Editorial Policies Our Team Advisory Board Help Center Sign In Submit a Preprint Cite Share Download PDF Article Gasdermins induce the release of mitochondrial DNA during pyroptosis and apoptosis Carlos de Torre-Minguela, Ana Gomez, Isabelle Couillin, Pablo Pelegrin This is a preprint; it has not been peer reviewed by a journal. https://doi.org/ 10.21203/rs.3.rs-106456/v1 This work is licensed under a CC BY 4.0 License Status: Posted Version 1 posted You are reading this latest preprint version Abstract Pyroptosis and intrinsic apoptosis are two forms of regulated cell death driven by active caspases where plasma membrane permeabilization is induced by gasdermin pores. Caspase-1 induces gasdermin D pore formation during pyroptosis meanwhile caspase-3 promotes gasdermin E pore formation during apoptosis. These two types of cell death are accompanied by mitochondrial outer membrane permeabilization due to BAK/BAX pore formation in the external membrane of mitochondria, and to some extent this complex also affects the inner mitochondrial membrane facilitating mitochondrial DNA relocalisation from the matrix to the cytosol. However, the detailed mechanism responsible for this process has not been investigated. Herein, we reported that gasdermin processing is required to induce mitochondrial DNA release from cells, despite mitochondrial outer membrane permeabilization, during pyroptosis and apoptosis. Gasdermin targeting the plasma membrane promotes a fast-mitochondrial collapse with the initial accumulation of mitochondrial DNA in the cytosol and then facilitate its release from the cell upon plasma membrane rupture. These findings demonstrate a critical role of gasdermin action on the plasma membrane facilitating the release of mitochondrial DNA as a damage-associated molecular pattern. Biological sciences/Immunology/Inflammation/Inflammasome Biological sciences/Cell biology Pyroptosis GSDMD GSDME mitochondrial DNA Macrophages Figures Figure 1 Figure 2 Figure 3 Figure 4 Figure 5 Figure 6 Full Text Additional Declarations There is no duality of interest Supplementary Files SupplementaryMaterial.pdf Supplementary Figures 1 to 13 Cite Share Download PDF Status: Posted Version 1 posted You are reading this latest preprint version Research Square lets you share your work early, gain feedback from the community, and start making changes to your manuscript prior to peer review in a journal. As a division of Research Square Company, we’re committed to making research communication faster, fairer, and more useful. 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Also discoverable on Platform About Our Team In Review Editorial Policies Advisory Board Help Center Resources Author Services Accessibility API Access RSS feed Manage Cookie Preferences © Research Square 2026 | ISSN 2693-5015 (online) Privacy Policy Terms of Service Do Not Sell My Personal Information {"props":{"pageProps":{"initialData":{"identity":"rs-106456","acceptedTermsAndConditions":true,"allowDirectSubmit":true,"archivedVersions":[],"articleType":"Article","associatedPublications":[],"authors":[{"id":405613081,"identity":"5c2f00f9-60e1-4674-b5c8-a463658f1963","order_by":0,"name":"Carlos de Torre-Minguela","email":"","orcid":"","institution":"Biomedical Research Institute of Murcia (IMIB-Arrixaca)","correspondingAuthor":false,"prefix":"","firstName":"Carlos","middleName":"","lastName":"de Torre-Minguela","suffix":""},{"id":405613082,"identity":"4908c436-0764-4dec-91e9-d86f044561ac","order_by":1,"name":"Ana Gomez","email":"","orcid":"","institution":"University Hospital Virgen Arrixaca","correspondingAuthor":false,"prefix":"","firstName":"Ana","middleName":"","lastName":"Gomez","suffix":""},{"id":405613083,"identity":"f59e6487-f1b7-4a99-a23d-e5cc682700ed","order_by":2,"name":"Isabelle Couillin","email":"","orcid":"","institution":"French National Centre for Scientific Research","correspondingAuthor":false,"prefix":"","firstName":"Isabelle","middleName":"","lastName":"Couillin","suffix":""},{"id":405613084,"identity":"4f495fb3-b0a3-4e8d-984c-f35851748376","order_by":3,"name":"Pablo Pelegrin","email":"data:image/png;base64,iVBORw0KGgoAAAANSUhEUgAAAZAAAAAyAQMAAABI0h/eAAAABlBMVEX///8AAABVwtN+AAAACXBIWXMAAA7EAAAOxAGVKw4bAAAA9UlEQVRIiWNgGAWjYFACHsYDIIoPRCQw2PAwMPMQ1MIA1sIG0ZJGqhYGhsNgEbzAnP3sgQMfGO7IsbG3X/vwcMd5Gd123gMMH/7g1mLZk5dwcAbDM2M2njPFMxLP3OYxO8yXwDizDbcWgwM5Bod5GA4ntknkJDMktoG08Bgw8zbg0XL+DVhLfZv8G5CWcxAtf/A4zOAGxJYENgn2w0AtByBaYKGB1S8z3gH9YvDMsI0nhxmoJRnsl4O9ePxizp978MGHijvy/OzHHzP+bLOzNzt/9uCDH/gcBg0EIMFjABc9gFsDTAtYDfsDfApHwSgYBaNgBAMAHwtTTsFvr48AAAAASUVORK5CYII=","orcid":"https://orcid.org/0000-0002-9688-1804","institution":"Biomedical Research Institute of Murcia (IMIB-Arrixaca)","correspondingAuthor":true,"prefix":"","firstName":"Pablo","middleName":"","lastName":"Pelegrin","suffix":""}],"badges":[],"createdAt":"2020-11-11 16:25:30","currentVersionCode":1,"declarations":"","doi":"10.21203/rs.3.rs-106456/v1","doiUrl":"https://doi.org/10.21203/rs.3.rs-106456/v1","draftVersion":[],"editorialEvents":[],"editorialNote":"","failedWorkflow":false,"files":[{"id":74508903,"identity":"b1249592-7f39-4e59-a178-bdc3c1c54732","added_by":"auto","created_at":"2025-01-23 03:21:01","extension":"png","order_by":1,"title":"Figure 1","display":"","copyAsset":false,"role":"figure","size":1080919,"visible":true,"origin":"","legend":"\u003cp\u003eNLRP3 inflammasome activation induces GSDMD-dependent mitochondrial network \u0026nbsp;fragmentation \u0026nbsp;A,B Different genotypes of mouse macrophages (as indicated) were primed for 4 h with LPS (10 \u0026nbsp;ng/ml) and then stimulated during 20 min with ATP (3 mM), nigericin (5 μM) or with antimycin A \u0026nbsp;(10 μM). Whole cell lysates (A), or cytosolic and organelle fractions (B) were analysed by \u0026nbsp;immunoblot for the indicated proteins. \u0026nbsp;C Maximum intensity projections of z-stack images of macrophages primed for 4 h with LPS (10 \u0026nbsp;ng/ml) and then stimulated during 10 min with nigericin (5 μM) and stained with TOMM20 \u0026nbsp;antibodies (green) and DAPI (blue). Scale bar represents 8 μm. \u0026nbsp;Data information: All immunoblots and microscopy images are representative of three independent \u0026nbsp;experiments.\u003c/p\u003e","description":"","filename":"1.png","url":"https://assets-eu.researchsquare.com/files/rs-106456/v1/87323c97de215095d1e2bcc4.png"},{"id":74509720,"identity":"701a8cf7-bd09-44ab-bc2b-652011f68153","added_by":"auto","created_at":"2025-01-23 03:29:01","extension":"png","order_by":2,"title":"Figure 2","display":"","copyAsset":false,"role":"figure","size":355164,"visible":true,"origin":"","legend":"\u003cp\u003eGSDMD induces mitochondrial DNA release after NLRP3 inflammasome activation \u0026nbsp;A Kinetic of MitoSOX fluorescence from macrophages of different genotypes (as indicated) primed \u0026nbsp;for 4 h with LPS (10 ng/ml) and then fluorescence was monitored during 50 min of stimulation \u0026nbsp;with ATP (3 mM), nigericin (5 μM) or antimycin A (10 μM). \u0026nbsp;B Quantification of mitochondrial DNA presence in the cytosolic fraction from macrophages of \u0026nbsp;different genotypes (as indicated) primed as in A and stimulated during 20 min with nigericin \u0026nbsp;(10μM). \u0026nbsp;C Maximum intensity projections of z-stack images of macrophages primed as in A stimulated or \u0026nbsp;not during 10 min with nigericin (5 μM) and then stained with anti-DNA antibodies (red), TOMM20 \u0026nbsp;antibodies (green) and DAPI (blue). Scale bar represents 5 μm. \u0026nbsp;D Quantification of mitochondrial DNA release in macrophage supernatant (SPN) of different \u0026nbsp;genotypes (as indicated) primed as in A and stimulated during 20 min with nigericin (10 μM).\u003c/p\u003e\n\u003cp\u003eData information: Data from A are means ± SEM of three independent experiments and were \u0026nbsp;normalized considering 100% the average of fluorescence of antimycin A at 45 min. Data from B and \u0026nbsp;D are means ± SEM of four-five independent experiments. Statistical analyses were performed using \u0026nbsp;non-parametric Mann–Whitney t-test. Data were considered significant when * P \u0026lt; 0.05. Microscopy \u0026nbsp;images of panel C are representative of three independent experiments.\u003c/p\u003e","description":"","filename":"2.png","url":"https://assets-eu.researchsquare.com/files/rs-106456/v1/fe4c40b58b2318c222da7b3f.png"},{"id":74508905,"identity":"36340328-9d3e-4064-8982-65448f05ad4c","added_by":"auto","created_at":"2025-01-23 03:21:01","extension":"png","order_by":3,"title":"Figure 3","display":"","copyAsset":false,"role":"figure","size":469441,"visible":true,"origin":"","legend":"\u003cp\u003ePyrin inflammasome activation and GSDMDNT induce mitochondrial DNA release \u0026nbsp;A Different genotype of macrophages (as indicated) were primed for 4 h with LPS (10 ng/ml) and \u0026nbsp;them stimulated at indicated times with nigericin (5 μM) or with the toxin B from Clostridium \u0026nbsp;difficile (TcdB) (1 μg/ml). Cells extract were analysed by immunoblot for the indicated proteins. \u0026nbsp;B IL-1b and LDH release detected in cell-free supernatants from Nlrp3−/− macrophages primed and \u0026nbsp;stimulated with TcdB as indicated in A. \u0026nbsp;C Maximum intensity projections of z-stack images of Nlrp3−/− and Casp1/11−/− macrophages \u0026nbsp;primed and stimulated with TcdB as indicated in A and stained with TOMM20 antibodies (green) \u0026nbsp;and DAPI (blue). Scale bar represents 8 μm. \u0026nbsp;D Mitochondrial DNA release detected in cell-free supernatants from Nlrp3−/− macrophages primed \u0026nbsp;and stimulated with TcdB as indicated in A. \u0026nbsp;E Maximum intensity projections of z-stack images of HEK293T after 16 h transfected with \u0026nbsp;plasmids encoding for human full-length GSDMD or GSDMDNT (1-275) and stained with \u0026nbsp;TOMM20 antibodies (green) and DAPI (blue). Scale bar represents 10 μm. \u0026nbsp;F Quantification of HMGB1 and mitochondrial DNA released in cell free supernatant obtained from \u0026nbsp;HEK293T transfected as in E.\u003c/p\u003e\n\u003cp\u003eData information: Data for panels B, D and F are means ± SEM from four-five independent \u0026nbsp;experiments. Statistical analyses were performed using non-parametric Mann–Whitney t-tests. Data \u0026nbsp;were considered significant when *P \u0026lt; 0.05, **P \u0026lt; 0.01. Immunoblots of panel A and microscopy \u0026nbsp;images of panels C and E are representative of three independent experiments.\u003c/p\u003e","description":"","filename":"3.png","url":"https://assets-eu.researchsquare.com/files/rs-106456/v1/15e7ece2c6031f4fa46bd62d.png"},{"id":74508906,"identity":"19846b86-abb0-4cd6-9b9d-cec3d26bc078","added_by":"auto","created_at":"2025-01-23 03:21:01","extension":"png","order_by":4,"title":"Figure 4","display":"","copyAsset":false,"role":"figure","size":551105,"visible":true,"origin":"","legend":"\u003cp\u003eMitochondrial DNA release is also promoted by GSDME \u0026nbsp;A Wild type macrophage were primed for 4 h with LPS (10 ng/ml) and then stimulated with nigericin \u0026nbsp;(10μM), Casp1/11−/− macrophages were treated with DMSO or staurosporin (1 μM) during the \u0026nbsp;indicated times. Cell lysates were analysed by immunoblot for the indicated proteins. \u0026nbsp;B Macrophages of different genotypes (as indicated) were primed and stimulated as in A. LDH and \u0026nbsp;HMGB1 release was determined in cell-free supernatant. \u0026nbsp;C Maximum intensity projections of z-stack images of Casp1/11−/− macrophages treated for 4 h \u0026nbsp;with DMSO or staurosporin (1 μM) and stained with TOMM20 antibodies (green) and DAPI \u0026nbsp;(blue). Scale bar represents 10 μm. \u0026nbsp;D Quantification of mitochondrial DNA released in cell free supernatant obtained from \u0026nbsp;macrophages stimulated as in A. \u0026nbsp;E Quantification of HMGB1 released in cell free supernatant obtained from HEK293T expressing \u0026nbsp;human GSDMENT (1-270) during 16 h. \u0026nbsp;F Maximum intensity projection of z-stack image of HEK293T expressing human GSDMENT as in \u0026nbsp;E and stained with TOMM20 antibodies (green) and DAPI (blue). Scale bar represents 10 μm. \u0026nbsp;G Quantification of mitochondrial DNA released in cell free supernatant obtained from expressing \u0026nbsp;human GSDMENT as in E. \u0026nbsp;Data information: Immunoblots of panel A and microscopic images of panels C and F are \u0026nbsp;representative of three independent experiments. For panels B, D, E and G data are means ± SEM \u0026nbsp;from at least four independent experiments. Statistical analyses were performed using non parametric Mann–Whitney t-tests. Data were considered significant when *P \u0026lt; 0.05, **P \u0026lt; 0.01, or \u0026nbsp;***P \u0026lt; 0.001.\u003c/p\u003e","description":"","filename":"4.png","url":"https://assets-eu.researchsquare.com/files/rs-106456/v1/f19a35bac1034fc0871dd8cb.png"},{"id":74508907,"identity":"2e02eba6-318b-4368-ae85-68da93582f8d","added_by":"auto","created_at":"2025-01-23 03:21:01","extension":"png","order_by":5,"title":"Figure 5","display":"","copyAsset":false,"role":"figure","size":420112,"visible":true,"origin":"","legend":"\u003cp\u003eGSDMD promotes mitochondrial DNA relocalisation to the cytosol in the absence of \u0026nbsp;cell lysis \u0026nbsp;A Kinetic of YoPro-1 uptake and MitoSOX fluorescence in wild type macrophages primed for 4 h \u0026nbsp;with LPS (10 ng/ml) and then stimulated with nigericin (5 μM, as shown by the arrow) in the \u0026nbsp;presence or not of glycine (5 mM). Glycine was added 15 min before and during stimulation. \u0026nbsp;B IL-1b and LDH was determined in cell-free supernatant of macrophages stimulated as in A but \u0026nbsp;after 20 or 40 min of nigericin as indicated. \u0026nbsp;C Cytosolic and organelle fraction of macrophages stimulated as in B were analysed by \u0026nbsp;immunoblot for the indicated proteins. \u0026nbsp;D Maximum intensity projections of z-stack images of wild type macrophages primed with LPS as \u0026nbsp;in A and then stimulated for 20 or 40 min with nigericin (5 μM) in presence or not of glycine (5 \u0026nbsp;mM), and stained with TOMM20 antibodies (green) and DAPI (blue). Scale bar represents 10 \u0026nbsp;μm. \u0026nbsp;E Quantification of mitochondrial DNA in supernatants and cytosol of macrophages primed and \u0026nbsp;stimulated as in B. \u0026nbsp;Data information: Data of panel A are means ± SEM from three independent experiments. Data of \u0026nbsp;panels B and E are means ± SEM from three-six independent experiments. Statistical analyses were \u0026nbsp;performed using non-parametric Mann–Whitney t-tests. Data were considered significant when *P \u0026lt; \u0026nbsp;0.05, **P \u0026lt; 0.01. Immunoblots of panel C and microscopy images of panel D are representative of \u0026nbsp;three independent experiments.\u003c/p\u003e","description":"","filename":"5.png","url":"https://assets-eu.researchsquare.com/files/rs-106456/v1/a26264ab2e7a7245bc4773ca.png"},{"id":74509721,"identity":"c95a4303-92be-42c8-a30f-aae1fa9c7f45","added_by":"auto","created_at":"2025-01-23 03:29:01","extension":"png","order_by":6,"title":"Figure 6","display":"","copyAsset":false,"role":"figure","size":559222,"visible":true,"origin":"","legend":"\u003cp\u003eGSDMDNT plasma membrane pore activity is required for mitochondrial damage \u0026nbsp;A Wild type macrophage were primed for 4 h with LPS (10 ng/ml) and then stimulated for 20 min \u0026nbsp;with nigericin (5 μM) in presence or not of punicalagin (50 μM). Punicalagin was added 10 min \u0026nbsp;before and during nigericin stimulation. Cell lysates were analysed by immunoblot for the \u0026nbsp;indicated proteins. \u0026nbsp;B Kinetic of YoPro-1 uptake in macrophages primed and stimulated as in A.Nigericin was added \u0026nbsp;as shown by the arrow. \u0026nbsp;C LDH and mitochondrial DNA presence in cell-free supernatants from macrophages primed and \u0026nbsp;stimulated as in A. \u0026nbsp;D Maximum intensity projections of z-stack images of wild type macrophages primed and \u0026nbsp;stimulated as in A, but 25 μM of punicalagin was used. In the indicated images, nigericin and \u0026nbsp;punicalagin were removed from the cell culture after 15 min of stimulation and cells were fixed \u0026nbsp;after 10 min washout. Cells were stained with DNA antibodies (red), TOMM20 antibodies (green) \u0026nbsp;and DAPI (blue). Scale bar represents 10 μm. \u0026nbsp;E Kinetic of MitoSOX fluorescence in macrophages primed and stimulated as in A. Nigericin was \u0026nbsp;added as shown by the arrow. \u0026nbsp;Data information: Immunoblots of panel A and microscopy images of panel D are representative of \u0026nbsp;three independent experiments. Data from panels B and E are means ± SEM from three independent \u0026nbsp;experiments. Data from panel C represent means ± SEM from three-five independent experiments. \u0026nbsp;Statistical analyses were performed using non-parametric Mann–Whitney t-tests. Data were \u0026nbsp;considered significant when *P \u0026lt; 0.05, **P \u0026lt; 0.01.\u003c/p\u003e","description":"","filename":"6.png","url":"https://assets-eu.researchsquare.com/files/rs-106456/v1/ccd1fc1d85833b08c8989781.png"},{"id":74510076,"identity":"f58a6c49-ae0d-4fc2-b40f-1e4587bc9a6e","added_by":"auto","created_at":"2025-01-23 03:37:07","extension":"pdf","order_by":1,"title":"","display":"","copyAsset":false,"role":"manuscript-pdf","size":1790566,"visible":true,"origin":"","legend":"Article File","description":"","filename":"ManuscriptGasderminsmtDNA2020v8.pdf","url":"https://assets-eu.researchsquare.com/files/rs-106456/v1_covered_9cdc2561-6897-45d9-8981-712e10dfac1b.pdf"},{"id":74508909,"identity":"b89f070d-2c99-4e11-91ec-89f37d2185e2","added_by":"auto","created_at":"2025-01-23 03:21:01","extension":"pdf","order_by":1,"title":"","display":"","copyAsset":false,"role":"supplement","size":3434865,"visible":true,"origin":"","legend":"Supplementary Figures 1 to 13","description":"","filename":"SupplementaryMaterial.pdf","url":"https://assets-eu.researchsquare.com/files/rs-106456/v1/90aa5f00edecb6f965de64f2.pdf"}],"financialInterests":"There is no duality of interest","formattedTitle":"Gasdermins induce the release of mitochondrial DNA during pyroptosis and apoptosis","fulltext":[],"fulltextSource":"","fullText":"","funders":[],"hasAdminPriorityOnWorkflow":false,"hasManuscriptDocX":false,"hasOptedInToPreprint":true,"hasPassedJournalQc":"","hasAnyPriority":true,"hideJournal":true,"highlight":"","institution":"","isAcceptedByJournal":false,"isAuthorSuppliedPdf":true,"isDeskRejected":"","isHiddenFromSearch":false,"isInQc":false,"isInWorkflow":false,"isPdf":true,"isPdfUpToDate":true,"isWithdrawnOrRetracted":false,"journal":{"display":true,"email":"[email protected]","identity":"researchsquare","isNatureJournal":false,"hasQc":true,"allowDirectSubmit":true,"externalIdentity":"","sideBox":"","snPcode":"","submissionUrl":"/submission","title":"Research Square","twitterHandle":"researchsquare","acdcEnabled":true,"dfaEnabled":false,"editorialSystem":"","reportingPortfolio":"","inReviewEnabled":false,"inReviewRevisionsEnabled":true},"keywords":"Pyroptosis, GSDMD, GSDME, mitochondrial DNA, Macrophages","lastPublishedDoi":"10.21203/rs.3.rs-106456/v1","lastPublishedDoiUrl":"https://doi.org/10.21203/rs.3.rs-106456/v1","license":{"name":"CC BY 4.0","url":"https://creativecommons.org/licenses/by/4.0/"},"manuscriptAbstract":"Pyroptosis and intrinsic apoptosis are two forms of regulated cell death driven by active caspases where plasma membrane permeabilization is induced by gasdermin pores. Caspase-1 induces gasdermin D pore formation during pyroptosis meanwhile caspase-3 promotes gasdermin E pore formation during apoptosis. These two types of cell death are accompanied by mitochondrial outer membrane permeabilization due to BAK/BAX pore formation in the external membrane of mitochondria, and to some extent this complex also affects the inner mitochondrial membrane facilitating mitochondrial DNA relocalisation from the matrix to the cytosol. However, the detailed mechanism responsible for this process has not been investigated. Herein, we reported that gasdermin processing is required to induce mitochondrial DNA release from cells, despite mitochondrial outer membrane permeabilization, during pyroptosis and apoptosis. Gasdermin targeting the plasma membrane promotes a fast-mitochondrial collapse with the initial accumulation of mitochondrial DNA in the cytosol and then facilitate its release from the cell upon plasma membrane rupture. These findings demonstrate a critical role of gasdermin action on the plasma membrane facilitating the release of mitochondrial DNA as a damage-associated molecular pattern.","manuscriptTitle":"Gasdermins induce the release of mitochondrial DNA during pyroptosis and apoptosis","msid":"","msnumber":"","nonDraftVersions":[{"code":1,"date":"2025-01-23 03:20:57","doi":"10.21203/rs.3.rs-106456/v1","editorialEvents":[{"type":"communityComments","content":0}],"status":"published","journal":{"display":true,"email":"[email protected]","identity":"researchsquare","isNatureJournal":false,"hasQc":true,"allowDirectSubmit":true,"externalIdentity":"","sideBox":"","snPcode":"","submissionUrl":"/submission","title":"Research Square","twitterHandle":"researchsquare","acdcEnabled":true,"dfaEnabled":false,"editorialSystem":"","reportingPortfolio":"","inReviewEnabled":false,"inReviewRevisionsEnabled":true}}],"origin":"","ownerIdentity":"d0e76b3a-762a-4e21-94fb-f8a50a1bd5f4","owner":[],"postedDate":"January 23rd, 2025","published":true,"recentEditorialEvents":[],"rejectedJournal":[],"revision":"","amendment":"","status":"posted","subjectAreas":[{"id":43249083,"name":"Biological sciences/Immunology/Inflammation/Inflammasome"},{"id":43249084,"name":"Biological sciences/Cell biology"}],"tags":[],"updatedAt":"2025-01-23T03:20:57+00:00","versionOfRecord":[],"versionCreatedAt":"2025-01-23 03:20:57","video":"","vorDoi":"","vorDoiUrl":"","workflowStages":[]},"version":"v1","identity":"rs-106456","journalConfig":"researchsquare"},"__N_SSP":true},"page":"/article/[identity]/[[...version]]","query":{"redirect":"/article/rs-106456","identity":"rs-106456","version":["v1"]},"buildId":"8U1c8b4HqxoKbykW_rLl7","isFallback":false,"isExperimentalCompile":false,"dynamicIds":[84888],"gssp":true,"scriptLoader":[]}