The NLRP1 inflammasome: new mechanistic insights and unresolved mysteries

Patrick S. Mitchell, Andrew Sandstrom, Russell E. Vance

Research output: Contribution to journalReview articlepeer-review

83 Scopus citations


Nucleotide-binding domain, leucine-rich repeat (NLR)proteins constitute a diverse class of innate immune sensors that detect pathogens or stress-associated stimuli in plants and animals. Some NLRs are activated upon direct binding to pathogen-derived ligands. In contrast, we focus here on a vertebrate NLR called NLRP1 that responds to the enzymatic activities of pathogen effectors. We discuss a newly proposed ‘functional degradation’ mechanism that explains activation and assembly of NLRP1 into an oligomeric complex called an inflammasome. We also discuss how NLRP1 is activated by non-pathogen-associated triggers such as the anti-cancer drug Val-boroPro, or by human disease-associated mutations. Finally, we discuss how research on NLRP1 has led to additional biological insights, including the unexpected discovery of a new CARD8 inflammasome.

Original languageEnglish (US)
Pages (from-to)37-45
Number of pages9
JournalCurrent Opinion in Immunology
StatePublished - Oct 2019
Externally publishedYes

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology


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