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

Abstract

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.

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@article{Chamaillard2003AnER, title={An essential role for NOD1 in host recognition of bacterial peptidoglycan containing diaminopimelic acid.}, author={Mathias Chamaillard and Masahito Hashimoto and Yasuo Horie and Junya Masumoto and Su Qiu and Lisa Saab and Yasunori Ogura and Akiko Kawasaki and Koichi Fukase and Shoichi Kusumoto and Miguel A Valvano and Simon J Foster and Tak W Mak and Gabriel Nu{\~n}ez and Naohiro Inohara}, journal={Nature immunology}, year={2003}, volume={4 7}, pages={702-7} }