GSDMD (1-275) binds bacterial cardiolipin

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.

气囊素D（GSDMD(1-275)，亦称GSDMD-NT）的N端结构域与细菌细胞膜上的心磷脂结合，并发生寡聚化，从而在细菌细胞膜上形成孔洞（Ding J 等人，2016；Liu X 等人，2016）。研究表明，GSDMD(1-275)可直接损伤并裂解革兰氏阳性菌和革兰氏阴性菌，包括大肠杆菌、金黄色葡萄球菌和巨大芽孢杆菌的原生质体（Ding J 等人，2016；Liu X 等人，2016）。此外，GSDMD(1-275)还与存在于宿主线粒体内膜内叶的心磷脂相互作用（Rogers C 等人，2019）。然而，GSDMD在生理条件下若能破坏细菌和线粒体膜，其如何穿过外膜以进入内层结构，目前尚不明确。