• Register
Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.


Leaving Community

Are you sure you want to leave this community? Leaving the community will revoke any permissions you have been granted in this community.


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