The gasdermin family of cell death executor proteins are activated by different proteases under different physiological conditions. A recent study by Deng et al. in Nature revealed that the cysteine protease Streptococcal pyrogenic exotoxin B (SpeB) from the human pathogen Streptococcus pyogenes directly cleaves and activates Gasdermin A (GSDMA) to induce pyroptosis in skin cells
Gasdermin proteins are in fungi and bacteria and are activated through proteolytic cleavage into pore-forming effectors. It shows a common cell death mechanism.
Infected E. coli cells that express this system have been observed to experience early cell death after phage infection. This occurs through the cleavage of gasdermin into its active form, which in turn prevents the release of virions and helps protect neighboring cells. The bacterium Lysobacter enzymogenes possesses a defense system that includes most elements of the pyroptotic pathway. This system comprises an NLR-like protein, CARD domains, a protease, and a gasdermin.
see also:
Cell Death & Gasdermins