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 tha...
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| Veröffentlicht in: | Nature immunology 2003-07, Vol.4 (7), p.702-707 |
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| creator | Inohara, Naohiro Chamaillard, Mathias Hashimoto, Masahito Horie, Yasuo Masumoto, Junya Qiu, Su Saab, Lisa Ogura, Yasunori Kawasaki, Akiko Fukase, Koichi Kusumoto, Shoichi Valvano, Miguel A Foster, Simon J Mak, Tak W Nuñez, Gabriel |
| description | 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. |
| doi_str_mv | 10.1038/ni945 |
| format | Article |
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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.</description><identifier>ISSN: 1529-2908</identifier><identifier>EISSN: 1529-2916</identifier><identifier>DOI: 10.1038/ni945</identifier><identifier>PMID: 12796777</identifier><language>eng</language><publisher>United States: Nature Publishing Group</publisher><subject>Adaptor Proteins, Signal Transducing ; Animals ; Bacteria ; Bacterial Infections - immunology ; Carrier Proteins - physiology ; Cell Line ; Cytokines - biosynthesis ; Diaminopimelic Acid - metabolism ; Female ; Humans ; Immunity, Innate - physiology ; Intracellular Signaling Peptides and Proteins ; Lipopolysaccharides - metabolism ; Mice ; Mice, Inbred C57BL ; Nod1 Signaling Adaptor Protein ; Nod2 Signaling Adaptor Protein ; Peptidoglycan - metabolism ; Vertebrates</subject><ispartof>Nature immunology, 2003-07, Vol.4 (7), p.702-707</ispartof><rights>COPYRIGHT 2003 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Jul 2003</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c490t-ffe56b54c9f34d2ad465948c98c4e79987d4fe24d2fd2e2159d8d15784f254e93</citedby><cites>FETCH-LOGICAL-c490t-ffe56b54c9f34d2ad465948c98c4e79987d4fe24d2fd2e2159d8d15784f254e93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,781,785,2728,27929,27930</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12796777$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Inohara, Naohiro</creatorcontrib><creatorcontrib>Chamaillard, Mathias</creatorcontrib><creatorcontrib>Hashimoto, Masahito</creatorcontrib><creatorcontrib>Horie, Yasuo</creatorcontrib><creatorcontrib>Masumoto, Junya</creatorcontrib><creatorcontrib>Qiu, Su</creatorcontrib><creatorcontrib>Saab, Lisa</creatorcontrib><creatorcontrib>Ogura, Yasunori</creatorcontrib><creatorcontrib>Kawasaki, Akiko</creatorcontrib><creatorcontrib>Fukase, Koichi</creatorcontrib><creatorcontrib>Kusumoto, Shoichi</creatorcontrib><creatorcontrib>Valvano, Miguel A</creatorcontrib><creatorcontrib>Foster, Simon J</creatorcontrib><creatorcontrib>Mak, Tak W</creatorcontrib><creatorcontrib>Nuñez, Gabriel</creatorcontrib><title>An essential role for NOD1 in host recognition of bacterial peptidoglycan containing diaminopimelic acid</title><title>Nature immunology</title><addtitle>Nat Immunol</addtitle><description>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.</description><subject>Adaptor Proteins, Signal Transducing</subject><subject>Animals</subject><subject>Bacteria</subject><subject>Bacterial Infections - immunology</subject><subject>Carrier Proteins - physiology</subject><subject>Cell Line</subject><subject>Cytokines - biosynthesis</subject><subject>Diaminopimelic Acid - metabolism</subject><subject>Female</subject><subject>Humans</subject><subject>Immunity, Innate - physiology</subject><subject>Intracellular Signaling Peptides and Proteins</subject><subject>Lipopolysaccharides - metabolism</subject><subject>Mice</subject><subject>Mice, Inbred C57BL</subject><subject>Nod1 Signaling Adaptor Protein</subject><subject>Nod2 Signaling Adaptor Protein</subject><subject>Peptidoglycan - metabolism</subject><subject>Vertebrates</subject><issn>1529-2908</issn><issn>1529-2916</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqF0UtrHSEUAOChtDSP5hcUihQa6OKm6uioy0v6CoQG-lgPXj1ODDM6VQeaf19v55KSbooLRb9z1HOa5ozgC4Jb-S54xfiT5phwqjZUke7pwxrLo-Yk5zuMCRMde94cESpUJ4Q4bm63AUHOEIrXI0pxBORiQl9u3hPkA7qNuaAEJg7BFx8Dig7ttCmQ9nyGuXgbh_He6IBMDEX74MOArNeTD3H2E4zeIG28fdE8c3rMcHaYT5sfHz98v_y8ub75dHW5vd4YpnDZOAe823FmlGuZpdqyjismjZKGgVBKCssc0HrkLAVKuLLSEi4kc5QzUO1pc77mnVP8uUAu_eSzgXHUAeKSe9GyVnAm_wuJlJh3sqvw9T_wLi4p1E_0lFLBiZCkoosVDXqE3gcXS9KmDguTr5UB5-v-tiaVWNbba8DbRwH76sGvMugl5_7q29fH9s1qTYo5J3D9nPyk031PcL_vfv-n-9W9Orx02U1g_6pDuyt4uYKgy5LgAazhvwGoMLIr</recordid><startdate>20030701</startdate><enddate>20030701</enddate><creator>Inohara, Naohiro</creator><creator>Chamaillard, Mathias</creator><creator>Hashimoto, Masahito</creator><creator>Horie, Yasuo</creator><creator>Masumoto, Junya</creator><creator>Qiu, Su</creator><creator>Saab, Lisa</creator><creator>Ogura, Yasunori</creator><creator>Kawasaki, Akiko</creator><creator>Fukase, Koichi</creator><creator>Kusumoto, Shoichi</creator><creator>Valvano, Miguel A</creator><creator>Foster, Simon J</creator><creator>Mak, Tak W</creator><creator>Nuñez, Gabriel</creator><general>Nature Publishing Group</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>ISR</scope><scope>3V.</scope><scope>7QP</scope><scope>7QR</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>20030701</creationdate><title>An essential role for NOD1 in host recognition of bacterial peptidoglycan containing diaminopimelic acid</title><author>Inohara, Naohiro ; Chamaillard, Mathias ; Hashimoto, Masahito ; Horie, Yasuo ; Masumoto, Junya ; Qiu, Su ; Saab, Lisa ; Ogura, Yasunori ; Kawasaki, Akiko ; Fukase, Koichi ; Kusumoto, Shoichi ; Valvano, Miguel A ; Foster, Simon J ; Mak, Tak W ; Nuñez, Gabriel</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c490t-ffe56b54c9f34d2ad465948c98c4e79987d4fe24d2fd2e2159d8d15784f254e93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Adaptor Proteins, Signal Transducing</topic><topic>Animals</topic><topic>Bacteria</topic><topic>Bacterial Infections - 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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.</abstract><cop>United States</cop><pub>Nature Publishing Group</pub><pmid>12796777</pmid><doi>10.1038/ni945</doi><tpages>6</tpages></addata></record> |
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| subjects | Adaptor Proteins, Signal Transducing Animals Bacteria Bacterial Infections - immunology Carrier Proteins - physiology Cell Line Cytokines - biosynthesis Diaminopimelic Acid - metabolism Female Humans Immunity, Innate - physiology Intracellular Signaling Peptides and Proteins Lipopolysaccharides - metabolism Mice Mice, Inbred C57BL Nod1 Signaling Adaptor Protein Nod2 Signaling Adaptor Protein Peptidoglycan - metabolism Vertebrates |
| title | An essential role for NOD1 in host recognition of bacterial peptidoglycan containing diaminopimelic acid |
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