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Details on Person Muramyl dipeptide (MDP; N-acetylmuramyl-L-alanyl-D-isoglutam...

Class:IdSummation:9989206
_displayNameMuramyl dipeptide (MDP; N-acetylmuramyl-L-alanyl-D-isoglutam...
_timestamp2026-05-19 13:17:07
created[InstanceEdit:9989214] Shamovsky, Veronica, 2026-05-19
literatureReference[LiteratureReference:844454] Reconstituted NALP1 inflammasome reveals two-step mechanism of caspase-1 activation
[LiteratureReference:9989205] A NOD2-NALP1 complex mediates caspase-1-dependent IL-1beta secretion in response to Bacillus anthracis infection and muramyl dipeptide
[LiteratureReference:9989210] NLRP1 and NLRP3 inflammasomes are essential for distinct outcomes of decreased cytokines but enhanced bacterial killing upon chronic Nod2 stimulation
textMuramyl dipeptide (MDP; N-acetylmuramyl-L-alanyl-D-isoglutamine), a peptidoglycan fragment common to both Gram-positive and Gram-negative bacteria, activates the NLRP1 inflammasome indirectly via the nucleotide-binding oligomerisation domain-containing protein 2 (NOD2) (Hsu LC et al., 2008; Hedl M et al., 2013). MDP binds the leucine-rich repeat (LRR) domain of NOD2, promoting NOD2 conformational change and CARD-domain exposure. Activated NOD2 then recruits NLRP1 through a homotypic CARD-CARD interaction forming the MDP:NOD2:NLRP1 complex (Hsu LC et al., 2008). In vitro studies suggest that MDP induces a conformational change in NLRP1 that allows ATP binding at the central NACHT domain and self-oligomerization of NLRP1, creating a binding platform for pro-caspase-1 (Faustin B et al. 2007). However, the mechanism by which the MDP:NOD2:NLRP1 complex promotes NLRP1 inflammasome assembly remains unclear. Whether NLRP1 mediates ATP hydrolysis is controversial, and neither release of the C-terminal UPA–CARD fragment nor proteasomal degradation of the N-terminal fragment of NLRP1 has been demonstrated during MDP:NOD2-mediated activation.
(summation)[BlackBoxEvent:9988918] MDP:NOD2 complex recruits NLRP1 (to replace 844447) [Homo sapiens]
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