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An essential role for NOD1 in host recognition of bacterial peptidoglycan containing diaminopimelic acid.

Nucleotide-binding oligomerization domain protein 1 (NOD1) belongs to a family that includes multiple members with NOD and leucine-rich repeats in vertebrates and plants. NOD1 has been suggested to have a role in innate immune responses, but the mechanism involved remains unknown. Here we report that NOD1 mediates the recognition of peptidoglycan derived primarily from Gram-negative bacteria. Biochemical and functional analyses using highly purified and synthetic compounds indicate that the core structure recognized by NOD1 is a dipeptide, gamma-D-glutamyl-meso-diaminopimelic acid (iE-DAP). Murine macrophages deficient in NOD1 did not secrete cytokines in response to synthetic iE-DAP and did not prime the lipopolysaccharide response. Thus, NOD1 mediates selective recognition of bacteria through detection of iE-DAP-containing peptidoglycan.

Pubmed ID: 12796777


  • Chamaillard M
  • Hashimoto M
  • Horie Y
  • Masumoto J
  • Qiu S
  • Saab L
  • Ogura Y
  • Kawasaki A
  • Fukase K
  • Kusumoto S
  • Valvano MA
  • Foster SJ
  • Mak TW
  • Nuñez G
  • Inohara N


Nature immunology

Publication Data

July 27, 2003

Associated Grants


Mesh Terms

  • Adaptor Proteins, Signal Transducing
  • Animals
  • Bacterial Infections
  • Carrier Proteins
  • Cell Line
  • Cytokines
  • Diaminopimelic Acid
  • Female
  • Humans
  • Immunity, Innate
  • Intracellular Signaling Peptides and Proteins
  • Lipopolysaccharides
  • Mice
  • Mice, Inbred C57BL
  • Nod1 Signaling Adaptor Protein
  • Nod2 Signaling Adaptor Protein
  • Peptidoglycan