LMP7 inhibits the activation of NLRP3 inflammasome through interaction with NLRP3

Biochem Biophys Res Commun. 2020 Oct 15;531(2):152-159. doi: 10.1016/j.bbrc.2020.07.091. Epub 2020 Aug 8.

Abstract

The innate immune system recognizes pathogen-associated molecular patterns (PAMPs) and damage-associated molecular patterns (DAMPs) by coding pattern recognition receptors (PRRs). As a well-known inflammasome, NLRP3 plays an essential role in helping the host immune response and driving antiviral processes. Low molecular mass polypeptide (LMP7) is a critical component of the immunoproteasome that participates in host antiviral activity, as well as T cell function and development. This is the first study to report the direct interaction between LMP7 and NLRP3. Also, LMP7 was found to inhibit the activation of the NLRP3 inflammasome, which is of great significance in exploring the role of the immune proteasome in regulating the activation of NLRP3.

Keywords: Immune proteasome; Low molecular mass polypeptide LMP7; NACHT LRR and PYD domains-Containing protein 3 NLRP3.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Line
  • Cytoplasm / metabolism
  • Humans
  • Inflammasomes / metabolism*
  • NLR Family, Pyrin Domain-Containing 3 Protein / chemistry
  • NLR Family, Pyrin Domain-Containing 3 Protein / metabolism*
  • Proteasome Endopeptidase Complex / genetics
  • Proteasome Endopeptidase Complex / metabolism*
  • Protein Binding
  • Protein Domains
  • Two-Hybrid System Techniques

Substances

  • Inflammasomes
  • NLR Family, Pyrin Domain-Containing 3 Protein
  • LMP7 protein
  • Proteasome Endopeptidase Complex