LPS binding caspase activation and recruitment domains (CARDs) are bipartite lipid binding modules

被引:0
作者
Cao, Anh B. [1 ]
Devant, Pascal [1 ]
Wang, Chengliang [2 ]
Sun, Mengyu [1 ]
Kennedy, Stephanie N. [1 ]
Ma, Weiyi [1 ]
Ruan, Jianbin [2 ]
Kagan, Jonathan C. [1 ]
机构
[1] Harvard Med Sch, Boston Childrens Hosp, Div Gastroenterol, 300 Longwood Ave, Boston, MA 02115 USA
[2] UConn Hlth Sch Med, Dept Immunol, 263 Farmington Ave, Farmington, CT 06030 USA
来源
SCIENCE ADVANCES | 2025年 / 11卷 / 10期
关键词
AIM2; INFLAMMASOME; PROTEIN; ASYMPTOTE; BACTERIA; TARGETS; DEATH; TREX1; CD14;
D O I
10.1126/sciadv.adt9027
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Caspase-11 is an innate immune pattern recognition receptor (PRR) that detects cytosolic bacterial lipopolysaccharides (LPS) through its caspase activation and recruitment domain (CARD). Caspase-11 also detects eukaryotic (i.e., self) lipids. This observation raises the question of whether common or distinct mechanisms govern caspase interactions with self- and nonself-lipids. In this study, using biochemical, computational, and cell-based assays, we report that the caspase-11 CARD functions as a bipartite lipid-binding module. Distinct regions within the CARD bind to phosphate groups and long acyl chains of self- and nonself-lipids. Self-lipid binding capability is conserved across numerous caspase-11 homologs and orthologs. The symmetry in self- and nonself-lipid detection mechanisms enabled us to engineer an LPS-binding domain de novo, using an ancestral CARD-like domain present in the fish Amphilophus citrinellus. These findings offer insights into the molecular basis of LPS recognition by caspase-11 and highlight the fundamental and likely inseparable relationship between self and nonself discrimination.
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页数:15
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