Caspase-11
Caspase-11 is the murine inflammatory caspase that defines the noncanonical inflammasome pathway, functioning as the rodent counterpart of the human Caspase-4/Caspase-5 pair. Unlike most pattern recognition receptors, the CARD domain of Caspase-11 binds lipopolysaccharide directly, enabling cytosolic sensing of Gram-negative bacteria independently of Toll-like receptor 4. Activated Caspase-11 cleaves gasdermin D, and the resulting pyroptotic lysis releases IL-1β and IL-18 through secondary caspase-1 activation, a sequence demonstrated in landmark studies of endotoxemic shock in mice. Mice lacking Caspase-11 are protected from lethal endotoxemia, which established this caspase as a pivotal mediator of sepsis pathology and a target for anti-inflammatory intervention.
