GSDMD (1-275) binds bacterial cardiolipin

Stable Identifier
R-HSA-9647643
Type
Reaction [binding]
Species
Homo sapiens
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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).

Literature References
PubMed ID Title Journal Year
27383986 Inflammasome-activated gasdermin D causes pyroptosis by forming membrane pores

Liu, X, Zhang, Z, Ruan, J, Pan, Y, Magupalli, VG, Wu, H, Lieberman, J

Nature 2016
27281216 Pore-forming activity and structural autoinhibition of the gasdermin family

Ding, J, Wang, K, Liu, W, She, Y, Sun, Q, Shi, J, Sun, H, Wang, DC, Shao, F

Nature 2016
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