Salmonella exploits NLRP12-dependent innate immune signaling to suppress host defenses during infection

Proc Natl Acad Sci U S A. 2014 Jan 7;111(1):385-90. doi: 10.1073/pnas.1317643111. Epub 2013 Dec 17.

Abstract

The nucleotide-binding oligomerization domain (NOD)-like receptor family pyrin domain containing 12 (NLRP12) plays a protective role in intestinal inflammation and carcinogenesis, but the physiological function of this NLR during microbial infection is largely unexplored. Salmonella enterica serovar Typhimurium (S. typhimurium) is a leading cause of food poisoning worldwide. Here, we show that NLRP12-deficient mice were highly resistant to S. typhimurium infection. Salmonella-infected macrophages induced NLRP12-dependent inhibition of NF-κB and ERK activation by suppressing phosphorylation of IκBα and ERK. NLRP12-mediated down-regulation of proinflammatory and antimicrobial molecules prevented efficient clearance of bacterial burden, highlighting a role for NLRP12 as a negative regulator of innate immune signaling during salmonellosis. These results underscore a signaling pathway defined by NLRP12-mediated dampening of host immune defenses that could be exploited by S. typhimurium to persist and survive in the host.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bone Marrow Cells / immunology
  • Bone Marrow Cells / microbiology
  • Extracellular Signal-Regulated MAP Kinases / metabolism
  • Host-Pathogen Interactions
  • Immunity, Innate*
  • Inflammation
  • Intracellular Signaling Peptides and Proteins / metabolism*
  • Liver / metabolism
  • Macrophages / microbiology
  • Male
  • Mice
  • Mice, Transgenic
  • Models, Biological
  • NF-kappa B / metabolism
  • Nitric Oxide / chemistry
  • Nucleotides / chemistry
  • Protein Structure, Tertiary
  • Salmonella Infections, Animal / immunology*
  • Salmonella Infections, Animal / microbiology*
  • Salmonella typhimurium / metabolism*
  • Signal Transduction
  • Time Factors

Substances

  • Intracellular Signaling Peptides and Proteins
  • NF-kappa B
  • NLRP12 protein, mouse
  • Nucleotides
  • Nitric Oxide
  • Extracellular Signal-Regulated MAP Kinases