NOD1 and NOD2: Signaling, Host Defense, and Inflammatory Disease
Open accessAbstract
The nucleotide-binding oligomerization domain (NOD) proteins NOD1 and NOD2, the founding members of the intracellular NOD-like receptor family, sense conserved motifs in bacterial peptidoglycan and induce proinflammatory and antimicrobial responses. Here, we discuss recent developments about the mechanisms by which NOD1 and NOD2 are activated by bacterial ligands, the regulation of their signaling pathways, and their role in host defense and inflammatory disease. Several routes for the entry of peptidoglycan ligands to the host cytosol to trigger activation of NOD1 and NOD2 have been elucidated. Furthermore, genetic screens and biochemical analyses have revealed mechanisms that regulate NOD1 and NOD2 signaling. Finally, recent studies have suggested several mechanisms to account for the link between NOD2 variants and susceptibility to Crohn's disease. Further understanding of NOD1 and NOD2 should provide new insight into the pathogenesis of disease and the development of new strategies to treat inflammatory and infectious disorders.
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NOD2 signaling activates NF-κB and MAPK phosphorylation cascades through RIPK2 and TAK1.
“NOD2 signal transduction occurs through the activation of transcription factor NF-κB and mitogen-activated protein kinase (MAPK) phosphorylation cascades via RIPK2 and TAK1 (Fig. 4F) (29, 30).”
From <i>Enterococcus</i> peptidoglycan remodeling promotes checkpoint inhibitor cancer immunotherapy (2021) · cites this paper as [30]
Nod2 expression was infrequent but detectable across multiple myeloid populations.
“Infrequent but detectable Nod2 expression was observed across multiple myeloid populations as expected (29, 30) (Fig. S14D).”
From <i>Enterococcus</i> peptidoglycan remodeling promotes checkpoint inhibitor cancer immunotherapy (2021) · cites this paper as [30]
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Park, J., Kim, Y., Shaw, M. H., et al. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.179.1.514 · Cited by 192 · see citing works
Burberry, A., Zeng, M. Y., Ding, L., Wicks, I. P., Inohara, N., Morrison, S. J., & Núñez, G. (2014) · Cell Host & Microbe · doi:10.1016/j.chom.2014.05.004 · Cited by 191 · see citing works
Self-citationDavis, K. M., Nakamura, S., & Weiser, J. N. (2011) · Journal of Clinical Investigation · doi:10.1172/jci57761 · Cited by 190 · see citing works
Nod2-Dependent Th2 Polarization of Antigen-Specific Immunity
Magalhaes, J. G., Fritz, J. H., Bourhis, L. L., Sellge, G., Travassos, L. H., Selvanantham, T., Girardin, S. E., Gommerman, J. L., & Philpott, D. J. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.181.11.7925 · Cited by 188 · see citing works
Hasegawa, M., Yamazaki, T., Kamada, N., Tawaratsumida, K., Kim, Y., Núñez, G., & Inohara, N. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1003761 · Cited by 187 · see citing works
Self-citationHelicobacter pylori Induces MAPK Phosphorylation and AP-1 Activation via a NOD1-Dependent Mechanism
Allison, C. C., Kufer, T. A., Kremmer, E., Kaparakis‐Liaskos, M., & Ferrero, R. L. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0900664 · Cited by 180 · see citing works
Hasegawa, M., Yang, K., Hashimoto, M., Park, J., Kim, Y., Fujimoto, Y., Núñez, G., Fukase, K., & Inohara, N. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602638200 · Cited by 175 · see citing works
Self-citationMo, J., Boyle, J. P., Howard, C. B., Monie, T. P., Davis, B. K., & Duncan, J. A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.344283 · Cited by 168 · see citing works
Nod1 Participates in the Innate Immune Response to Pseudomonas aeruginosa
Travassos, L. H., Carneiro, L. A. M., Girardin, S. E., Boneca, I. G., Lemos, R., Bozza, M. T., Domingues, R. M. C. P., Coyle, A. J., Bertin, J., Philpott, D. J., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501649200 · Cited by 166 · see citing works
Roles of NOD1 (NLRC1) and NOD2 (NLRC2) in innate immunity and inflammatory diseases
Correa, R. G., Milutinovic, S., & Reed, J. C. (2012) · Bioscience Reports · doi:10.1042/bsr20120055 · Cited by 165 · see citing works
XIAP variants in male Crohn's disease
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Role for Erbin in Bacterial Activation of Nod2
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Disease‐causing mutations in the XIAP BIR2 domain impair NOD2‐dependent immune signalling
Damgaard, R. B., Fiil, B. K., Speckmann, C., Yabal, M., Stadt, U. Z., Bekker‐Jensen, S., Jost, P. J., Ehl, S. R., Mailand, N., & Gyrd‐Hansen, M. (2013) · EMBO Molecular Medicine · doi:10.1002/emmm.201303090 · Cited by 148 · see citing works
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ITCH K63-Ubiquitinates the NOD2 Binding Protein, RIP2, to Influence Inflammatory Signaling Pathways
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Induction of Bone Loss by Pathobiont-Mediated Nod1 Signaling in the Oral Cavity
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Self-citationBarnich, N., Hisamatsu, T., Aguirre, J. E., Xavier, R. J., Reinecker, H., & Podolsky, D. K. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413776200 · Cited by 134 · see citing works
Role of AmiA in the Morphological Transition of Helicobacter pylori and in Immune Escape
Chaput, C., Ecobichon, C., Cayet, N., Girardin, S. E., Werts, C., Guadagnini, S., Prévost, M., Mengin‐Lecreulx, D., Labigne-Roussel, A., & Boneca, I. G. (2006) · PLoS Pathogens · doi:10.1371/journal.ppat.0020097 · Cited by 126 · see citing works
Nod1-dependent control of tumor growth
Correia, J. D. S., Miranda, Y., Austin-Brown, N., Hsu, J. C., Mathison, J. C., Xiang, R., Zhou, H., Li, Q., Han, J., & Ulevitch, R. J. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0509228103 · Cited by 121 · see citing works
Zilbauer, M., Dorrell, N., Elmi, A., Lindley, K. J., Schüller, S., Jones, H. E., Klein, N. J., Núñez, G., Wren, B. W., & Bajaj‐Elliott, M. (2007) · Cellular Microbiology · doi:10.1111/j.1462-5822.2007.00969.x · Cited by 120 · see citing works
Self-citationTRIM27 Negatively Regulates NOD2 by Ubiquitination and Proteasomal Degradation
Zurek, B., Schoultz, I., Neerincx, A., Napolitano, L. M. R., Birkner, K., Bennek, E., Sellge, G., Lerm, M., Meroni, G., Söderholm, J. D., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0041255 · Cited by 115 · see citing works
In Vivo Inhibition of RIPK2 Kinase Alleviates Inflammatory Disease
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Sasawatari, S., Okamura, T., Kasumi, E., Furuyama-Tanaka, K., Yanobu‐Takanashi, R., Shirasawa, S., Kato, N., & Toyama‐Sorimachi, N. (2011) · Gastroenterology · doi:10.1053/j.gastro.2011.01.041 · Cited by 114 · see citing works
Structural mechanisms in NLR inflammasome signaling
Lechtenberg, B. C., Mace, P. D., & Riedl, S. J. (2014) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2014.08.011 · Cited by 112 · see citing works
Mouse Paneth cell antimicrobial function is independent of Nod2
Shanahan, M. T., Carroll, I. M., Grossniklaus, E. J., White, A., von Furstenberg, R. J., Barner, R., Fodor, A. A., Henning, S., Sartor, R. B., & Gulati, A. (2013) · Gut · doi:10.1136/gutjnl-2012-304190 · Cited by 105 · see citing works
Pellino3 ubiquitinates RIP2 and mediates Nod2-induced signaling and protective effects in colitis
Yang, S., Wang, B., Humphries, F., Jackson, R. P., Healy, M. E., Bergin, R., Aviello, G., Hall, B. J., McNamara, D. A., Darby, T. M., et al. (2013) · Nature Immunology · doi:10.1038/ni.2669 · Cited by 100 · see citing works
Frutuoso, M. S., Hori, J. I., Pereira, M. S. F., Lima-Junior, D. S., Sônego, F., Kobayashi, K. S., Flavell, R. A., Cunha, F. Q., & Zamboni, D. S. (2010) · Microbes and Infection · doi:10.1016/j.micinf.2010.05.006 · Cited by 97 · see citing works
Laroui, H., Yan, Y., Narui, Y., Ingersoll, S. A., Ayyadurai, S., Charania, M. A., Zhou, F., Wang, B., Salaita, K. S., Sitaraman, S. V., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.257501 · Cited by 97 · see citing works
Impaired dendritic cell function in Crohn’s disease patients with NOD2 3020insC mutation
Kramer, M., Netea, M. G., de Jong, D. J., Kullberg, B. J., & Adema, G. J. (2006) · Journal of Leukocyte Biology · doi:10.1189/jlb.0805484 · Cited by 94 · see citing works
Innate signals from Nod2 block respiratory tolerance and program TH2-driven allergic inflammation
Duan, W., Mehta, A. K., Magalhaes, J. G., Ziegler, S. F., Dong, C., Philpott, D. J., & Croft, M. (2010) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2010.09.021 · Cited by 94 · see citing works
Proteasomal Degradation of Nod2 Protein Mediates Tolerance to Bacterial Cell Wall Components
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Magalhaes, J. G., Rubino, S. J., Travassos, L. H., Bourhis, L. L., Duan, W., Sellge, G., Geddes, K., Reardon, C., Lechmann, M., Carneiro, L. A. M., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1015063108 · Cited by 83 · see citing works
Lipinski, S., Grabe, N., Jacobs, G., Billmann-Born, S., Till, A., Häsler, R., Aden, K., Paulsen, M., Arlt, A., Kraemer, L., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1209673109 · Cited by 68 · see citing works
Marinis, J. M., Homer, C. R., McDonald, C., & Abbott, D. W. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.189308 · Cited by 65 · see citing works
Genotypes and phenotypes in Crohn’s disease: do they help in clinical management?
Gasché, C., & Grundtner, P. (2004) · Gut · doi:10.1136/gut.2003.035600 · Cited by 61 · see citing works
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Kim, Y., Shaw, M. H., Warner, N. E., Park, J., Chen, F., Ogura, Y., & Núñez, G. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1001854 · Cited by 59 · see citing works
Self-citationIdentification of Inhibitors of NOD1-Induced Nuclear Factor-κB Activation
Khan, P. M., Correa, R. G., Divlianska, D. B., Peddibhotla, S., Sessions, E. H., Magnuson, G., Brown, B. T., Suyama, E., Yuan, H., Mangravita-Novo, A., et al. (2011) · ACS Medicinal Chemistry Letters · doi:10.1021/ml200158b · Cited by 59 · see citing works
RIP2 activity in inflammatory disease and implications for novel therapeutics
Jun, J., Cominelli, F., & Abbott, D. W. (2013) · Journal of Leukocyte Biology · doi:10.1189/jlb.0213109 · Cited by 57 · see citing works
Discovery and Characterization of 2-Aminobenzimidazole Derivatives as Selective NOD1 Inhibitors
Correa, R. G., Khan, P. M., Askari, N., Zhai, D., Gerlic, M., Brown, B. T., Magnuson, G., Spreafico, R., Albani, S., Sergienko, E. A., et al. (2011) · Chemistry & Biology · doi:10.1016/j.chembiol.2011.06.009 · Cited by 55 · see citing works
Rickard, D. J., Sehon, C. A., Kasparcova, V., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0069619 · Cited by 54 · see citing works
Heul, A. V., Fowler, C. A., Ramaswamy, S., & Piper, R. C. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.413781 · Cited by 43 · see citing works
Warner, N. E., Burberry, A., Pliakas, M. C., McDonald, C., & Núñez, G. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.574756 · Cited by 43 · see citing works
Self-citationKim, Y., Park, J., Daignault, S. D., et al. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.181.6.4340 · Cited by 43 · see citing works
Agnihotri, G., Ukani, R., Malladi, S. S., Warshakoon, H. J., Balakrishna, R., Wang, X., & David, S. A. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm101535e · Cited by 39 · see citing works
Salucci, V., Rimoldi, M., Penati, C., et al. (2008) · Inflammatory Bowel Diseases · doi:10.1002/ibd.20390 · Cited by 38 · see citing works
Emerging roles of immunostimulatory oral bacteria in periodontitis development
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Self-citationJakopin, Ž., Gobec, M., Mlinarič‐Raščan, I., et al. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm300503b · Cited by 37 · see citing works
Identification of a synthetic muramyl peptide derivative with enhanced Nod2 stimulatory capacity
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Anti‐inflammatory AreneChromium Complexes Acting as Specific Inhibitors of NOD2 Signalling
Bielig, H., Velder, J., Saiai, A., Menning, M., Meemboor, S., Kalka-Moll, W. M., Krönke, M., Schmalz, H., & Kufer, T. A. (2010) · ChemMedChem · doi:10.1002/cmdc.201000320 · Cited by 32 · see citing works
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The E3 Ligase RNF34 is a Novel Negative Regulator of the NOD1 Pathway
Zhang, R., Zhao, J., Song, Y., Wang, X., Wang, L., Xu, J., Song, C. H., & Liu, F. (2014) · Cellular Physiology and Biochemistry · doi:10.1159/000362972 · Cited by 27 · see citing works
IKKα Contributes to Canonical NF-κB Activation Downstream of Nod1-Mediated Peptidoglycan Recognition
Kim, M. L., Jeong, H. G., Kasper, C. A., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015371 · Cited by 26 · see citing works
Crystal Structure of a Complex of NOD1 CARD and Ubiquitin
Heul, A. V., Gakhar, L., Piper, R. C., & Ramaswamy, S. (2014) · PLoS ONE · doi:10.1371/journal.pone.0104017 · Cited by 15 · see citing works
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Gut microbiota: Role in pathogen colonization, immune responses, and inflammatory disease
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“In immunological terms, it is also known that immune cells can elicit the innate immune response by detecting damage-associated molecular patterns (DAMPs) or pathogenassociated molecular patterns (PAMPs) using Pattern Recognition Receptors (PRRs) [107], such as Toll-like receptors (TLRs) [108,109], NOD-like receptors…”
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- Authors
- Caruso, R., Warner, N., Inohara, N., & Núñez, G.
- Affiliations
- University of Michigan (US)
- Corresponding author
- Núñez, Gabriel
- Venue
- Immunity
- Publisher
- Elsevier BV
- Published
- 2014-12
- Volume
- 41
- Issue
- 6
- Pages
- 898-908
- ISSN
- 1074-7613 (ISSN-L)
- PMC
- PMC4272446
- OpenAlex
- W2001166572
- Cited by
- 830
- References
- 134
- Citations by year
- 2026: 59 · 2025: 76 · 2024: 74 · 2023: 88 · 2022: 101 · 2021: 93 · 2020: 81 · 2019: 71 · 2018: 66 · 2017: 54 · 2016: 46 · 2015: 20 · 2014: 1
- FWCI
- 3.97
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Immunity (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK061707)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Keywords
- NOD1, NOD2, NOD-like receptors, peptidoglycan sensing, intracellular signaling, host defense, inflammatory diseases, Crohn's disease, genetic susceptibility, innate immunity, antimicrobial response
- MeSH terms
- Animals, Antigens, Bacterial, Bacterial Infections, Humans, Immunity, Innate, Inflammation, Peptidoglycan, Signal Transduction, Receptors, Pattern Recognition, Nod2 Signaling Adaptor Protein, Nod1 Signaling Adaptor Protein, Host-Pathogen Interactions
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