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Lytic cell death induced by melittin bypasses pyroptosis but induces NLRP3 inflammasome activation and IL-1β release

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dc.contributor.authorMuñoz-García, María
dc.contributor.authorAndreu Martínez, David
dc.contributor.authorRivas, Luis
dc.contributor.authorMartín Sánchez, María Rosario Fátima
dc.contributor.authorMartínez Villanueva, Miriam
dc.contributor.authorNoguera Velasco, José Antonio
dc.contributor.authorPelegrín Vivancos, Pablo
dc.contributor.authorMartínez García, Juan José
dc.contributor.departmentFarmacología
dc.date.accessioned2026-02-12T12:54:17Z
dc.date.available2026-02-12T12:54:17Z
dc.date.issued2017-10-08
dc.description.abstractThe nucleotide-binding domain and leucine-rich repeat-containing receptor with a pyrin domain 3 (NLRP3) inflammasome is a sensor for different types of infections and alterations of homeostatic parameters, including abnormally high levels of the extracellular nucleotide ATP or crystallization of different metabolites. All NLRP3 activators trigger a similar intracellular pathway, where a decrease in intracellular K+ concentration and permeabilization of plasma membrane are key steps. Cationic amphipathic antimicrobial peptides and peptide toxins permeabilize the plasma membrane. In fact, some of them have been described to activate the NLRP3 inflammasome. Among them, the bee venom antimicrobial toxin peptide melittin is known to elicit an inflammatory reaction via the NLRP3 inflammasome in response to bee venom. Our study found that melittin induces canonical NLRP3 inflammasome activation by plasma membrane permeabilization and a reduction in the intracellular K+ concentration. Following melittin treatment, the apoptosis-associated speck-like protein, an adaptor protein with a caspase recruitment domain (ASC), was necessary to activate caspase-1 and induce IL-1β release. However, cell death induced by melittin prevented the formation of large ASC aggregates, amplification of caspase-1 activation, IL-18 release and execution of pyroptosis. Therefore, melittin-induced activation of the NLRP3 inflammasome results in an attenuated inflammasome response that does not result in caspase-1 dependent cell death.
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dc.identifier.citationMartín-Sánchez, F., Martínez-García, J., Muñoz-García, M. et al. Lytic cell death induced by melittin bypasses pyroptosis but induces NLRP3 inflammasome activation and IL-1β release. Cell Death Dis 8, e2984 (2017). https://doi.org/10.1038/cddis.2017.390
dc.identifier.doihttps://doi.org/10.1038/cddis.2017.390
dc.identifier.issn2041-4889
dc.identifier.urihttp://hdl.handle.net/10201/204541
dc.languagespa
dc.publisherSpringer Nature
dc.relationThis work was supported by SAF2015-65740-R and Subdirección General de Redes y Centros de Investigación Cooperativa-FEDER, RICET RD12/0018/0007 and RD16/0027/0010. This work was also supported by grants from the European Research Council (ERC-2013-CoG 614578 to PP) and the Instituto Salud Carlos III-Fondo Europeo de Desarrollo Regional (PI13/00174 to PP). FM-S was supported by the Sara Borrell postdoctoral grant from the Instituto Salud Carlos III (CD12/00523)
dc.relation.publisherversionhttps://www.nature.com/articles/cddis2017390
dc.rightsAttribution 4.0 International*
dc.rights.accessRightsinfo:eu-repo/semantics/openAccess
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.subject.odsObjetivo 3: Salud
dc.titleLytic cell death induced by melittin bypasses pyroptosis but induces NLRP3 inflammasome activation and IL-1β release
dc.typeinfo:eu-repo/semantics/article
dc.type.versioninfo:eu-repo/semantics/publishedVersion
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