Nucleotide-binding oligomerization domain-1 and -2 play no role in controlling Brucella abortus infection in mice

Clin Dev Immunol. 2012:2012:861426. doi: 10.1155/2012/861426. Epub 2011 Nov 30.

Abstract

Nucleotide-binding oligomerization domain proteins (NODs) are modular cytoplasmic proteins implicated in the recognition of peptidoglycan-derived molecules. Further, several in vivo studies have demonstrated a role for Nod1 and Nod2 in host defense against bacterial pathogens. Here, we demonstrated that macrophages from NOD1-, NOD2-, and Rip2-deficient mice produced lower levels of TNF-α following infection with live Brucella abortus compared to wild-type mice. Similar reduction on cytokine synthesis was not observed for IL-12 and IL-6. However, NOD1, NOD2, and Rip2 knockout mice were no more susceptible to infection with virulent B. abortus than wild-type mice. Additionally, spleen cells from NOD1-, NOD2-, and Rip2-deficient mice showed unaltered production of IFN-γ compared to C57BL/6 mice. Taken together, this study demonstrates that NOD1, NOD2 and Rip2 are dispensable for the control of B. abortus during in vivo infection.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Brucella abortus*
  • Brucellosis / genetics
  • Brucellosis / immunology*
  • Interferon-gamma / biosynthesis
  • Interferon-gamma / immunology
  • Macrophages / immunology
  • Macrophages / metabolism
  • Mice
  • Mice, Inbred C57BL
  • Mice, Knockout
  • Nod1 Signaling Adaptor Protein / genetics*
  • Nod1 Signaling Adaptor Protein / metabolism
  • Nod2 Signaling Adaptor Protein / genetics*
  • Nod2 Signaling Adaptor Protein / metabolism
  • Receptor-Interacting Protein Serine-Threonine Kinase 2
  • Receptor-Interacting Protein Serine-Threonine Kinases / genetics
  • Receptor-Interacting Protein Serine-Threonine Kinases / metabolism
  • Spleen / immunology
  • Spleen / metabolism
  • Tumor Necrosis Factor-alpha / biosynthesis
  • Tumor Necrosis Factor-alpha / immunology

Substances

  • Nod1 Signaling Adaptor Protein
  • Nod2 Signaling Adaptor Protein
  • Tumor Necrosis Factor-alpha
  • Interferon-gamma
  • Receptor-Interacting Protein Serine-Threonine Kinase 2
  • Receptor-Interacting Protein Serine-Threonine Kinases
  • Ripk2 protein, mouse