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- Publisher Website: 10.1038/ni945
- Scopus: eid_2-s2.0-0038824980
- PMID: 12796777
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Article: An essential role for NOD1 in host recognition of bacterial peptidoglycan containing diaminopimelic acid
Title | An essential role for NOD1 in host recognition of bacterial peptidoglycan containing diaminopimelic acid |
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Authors | |
Issue Date | 2003 |
Citation | Nature Immunology, 2003, v. 4, n. 7, p. 702-707 How to Cite? |
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, γ-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. |
Persistent Identifier | http://hdl.handle.net/10722/291652 |
ISSN | 2023 Impact Factor: 27.7 2023 SCImago Journal Rankings: 11.274 |
DC Field | Value | Language |
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dc.contributor.author | Chamaillard, Mathias | - |
dc.contributor.author | Hashimoto, Masahito | - |
dc.contributor.author | Horie, Yasuo | - |
dc.contributor.author | Masumoto, Junya | - |
dc.contributor.author | Qiu, Su | - |
dc.contributor.author | Saab, Lisa | - |
dc.contributor.author | Ogura, Yasunori | - |
dc.contributor.author | Kawasaki, Akiko | - |
dc.contributor.author | Fukase, Koichi | - |
dc.contributor.author | Kusumoto, Shoichi | - |
dc.contributor.author | Valvano, Miguel A. | - |
dc.contributor.author | Foster, Simon J. | - |
dc.contributor.author | Mak, Tak W. | - |
dc.contributor.author | Nuñez, Gabriel | - |
dc.contributor.author | Inohara, Naohiro | - |
dc.date.accessioned | 2020-11-17T14:54:49Z | - |
dc.date.available | 2020-11-17T14:54:49Z | - |
dc.date.issued | 2003 | - |
dc.identifier.citation | Nature Immunology, 2003, v. 4, n. 7, p. 702-707 | - |
dc.identifier.issn | 1529-2908 | - |
dc.identifier.uri | http://hdl.handle.net/10722/291652 | - |
dc.description.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, γ-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. | - |
dc.language | eng | - |
dc.relation.ispartof | Nature Immunology | - |
dc.title | An essential role for NOD1 in host recognition of bacterial peptidoglycan containing diaminopimelic acid | - |
dc.type | Article | - |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1038/ni945 | - |
dc.identifier.pmid | 12796777 | - |
dc.identifier.scopus | eid_2-s2.0-0038824980 | - |
dc.identifier.volume | 4 | - |
dc.identifier.issue | 7 | - |
dc.identifier.spage | 702 | - |
dc.identifier.epage | 707 | - |
dc.identifier.f1000 | 1014164 | - |
dc.identifier.issnl | 1529-2908 | - |