Bacterial gasdermins reveal an ancient mechanism of cell death
Author(s) -
Alex G. Johnson,
Tanita Wein,
Megan L. Mayer,
B. Lowey,
Erez Yirmiya,
Yaara OppenheimerShaanan,
Gil Amitai,
Rotem Sorek,
Philip J. Kranzusch
Publication year - 2022
Publication title -
science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 12.556
H-Index - 1186
eISSN - 1095-9203
pISSN - 0036-8075
DOI - 10.1126/science.abj8432
Subject(s) - pyroptosis , programmed cell death , microbiology and biotechnology , proteases , inflammasome , lytic cycle , cleavage (geology) , cell , caspase , bacterial cell structure , chemistry , bacteria , apoptosis , biology , biochemistry , receptor , enzyme , genetics , paleontology , virus , virology , fracture (geology)
Ancient origin of cell death Gasdermins are cell death proteins in mammals that form membrane pores in response to pathogen infection. Johnsonet al . report that diverse bacteria encode structural and functional homologs of mammalian gasdermins. Like their mammalian counterparts, bacterial gasdermins are activated by caspase-like proteases, oligomerize into large membrane pores, and defend against pathogen—in this case, bacteriophage—infection. Proteolytic activation occurs through the release of a short inhibitory peptide, and many bacterial gasdermins are lipidated to facilitate membrane pore formation. Pyroptotic cell death, a central component of mammalian innate immunity, thus has a shared origin with an ancient antibacteriophage defense system. —SMH
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