Article Publish Status: FREE
Abstract Title:

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

Abstract Source:

Cell Death Dis. 2017 08 10 ;8(8):e2984. Epub 2017 Aug 10. PMID: 28796264

Abstract Author(s):

Fátima Martín-Sánchez, Juan José Martínez-García, María Muñoz-García, Miriam Martínez-Villanueva, José A Noguera-Velasco, David Andreu, Luís Rivas, Pablo Pelegrín

Article Affiliation:

Fátima Martín-Sánchez


The 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 Kconcentration 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 Kconcentration. 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 thatdoes not result in caspase-1 dependent cell death.

Study Type : In Vitro Study

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