ArticleScience advances2025
LPS binding caspase activation and recruitment domains (CARDs) are bipartite lipid binding modules.
Article in Science advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Structural insights into human caspase-9 CARD assembly modes driven by conserved arginine hotspots.Journal of structural biology: X · 2026Article
- When folding CARDs wins the game: molecular snapshots of lipopolysaccharide sensing by the non-canonical inflammasome.Biochemical Society transactions · 2026Review
- Macrophage Proteomic Profiling Reveals Divergent TLR4-Dependent and -Independent Responses to KdoLife (Basel, Switzerland) · 2026Article
- LPS-induced structural reorganization and polymerization drive noncanonical inflammasome activation.Science advances · 2026Article
- Cardiolipin inhibits the non-canonical inflammasome by preventing LPS binding to caspase-4/11.The EMBO journal · 2025Article
- Recognition ofJournal of oral microbiology · 2025Article
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8 authors.
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Abstract
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
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