Fig. 1

Structure of NLRP family, NLRC4/IPAF-NAIP family, PYHIN family, and pyrin inflammasomes. These cytosolic sensors contain various domains such as NACHT, LRR, PYD that interact with ASC to recruit and cleave pro-caspase-1 by CARD domain. Activated pro-caspase-1 cleaves inactivated pro-IL1β and pro-IL18 to release activated IL-1β and IL-18. NLRP1b can be activated by T. gondii and lethal factor of Bacillus anthracis. NLRP3 can be activated by pore-forming toxins, Klebsiella, Enterobacter, K. aerogenes, E. coli, C. rodentium, V. cholerae, P. mirabilis, C. pneumoniae, and S. aureus. NLRC4/IPAF-NAIP family inflammasome can be triggered by S. typhimurium, L. pneumophila, Sh. flexneri, P. aeruginosa, Flagellin, T3SS needle subunit (human), and T3S Rod Protein (mouse). AIM2 inflammasome is activated by Murine CMV, vaccinia virus, F. tularensis, and L. monocytogenes. IFI16 is specifically activated by Kaposi’s sarcoma-associated herpes virus (KSHV). Pyrin inflammasome is activated by Yersinia outer protein M (YopM). Abbreviations: Baculovirus inhibitor of apoptosis repeat domain (BIR); Caspase recruitment domain (CARD); function-to-find domain (FIIND); Leucine-rich repeat (LRR); Nucleotide-binding and oligomerization domain (NACHT); Pyrin domain (PYD)