The N-terminal domain of gasdermin D (GSDMD(1-275), also known as GSDMD-NT) binds to cardiolipin, a lipid found on the bacterial cell membrane, and oligomerizes to form pores on the bacterial cell membrane (Ding J et al. 2016; Liu X et al. 2016). GSDMD(1-275) was reported to damage and lyse Gram-positive and Gram-negative bacteria directly, including Escherichia coli, Staphylococcus aureus and Bacillus megaterium protoplasts (Ding J et al. 2016; Liu X et al. 2016). GSDMD(1-275) also interacts with cardiolipin present in the inner leaflet of the host mitochondrial membrane (Rogers C et al. 2019). However, it is not known how GSDMD can pass the outer membrane to access the inner member if it can disrupt the bacterial and mitochondrial membrane under physiological conditions.
Wang, DC, Ding, J, Liu, W, Shi, J, Shao, F, Wang, K, Sun, Q, Sun, H, She, Y
Lieberman, J, Wu, H, Zhang, Z, Magupalli, VG, Ruan, J, Pan, Y, Liu, X
© 2022 Reactome
