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

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書誌事項

公開日
2003-06-06
権利情報
  • http://www.springer.com/tdm
DOI
  • 10.1038/ni945
公開者
Springer Science and Business Media LLC

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説明

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.

収録刊行物

  • Nature Immunology

    Nature Immunology 4 (7), 702-707, 2003-06-06

    Springer Science and Business Media LLC

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