MOESM2 of Secreting-lux/pT-ClyA engineered bacteria suppresses tumor growth via interleukin-1β in two pathways

Additional file 2: Figure S2. NLRP3 signaling pathway. NLRP3 activation of the N-terminal thermoprotein domain causes NLRP3 self-oligomerization, which in turn binds to apoptosis-associated microparticle proteins and recruits Pro-caspase1 to form the NLRP3 inflammatory complex. Upon activation of the inflammatory complex, Pro-caspase 1 is cleaved to form caspase 1, which then promotes IL-1β release to the extracellular environment. K+ efflux is a necessary signal for NLRP3 activation, and Cytolysin A forms a channel on the cell membrane that causes a large and sustained K+ outflow, activating the NLRP3 pathway and promoting sustained IL-1β release.