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Peptidoglycan-induced modulation of metabolic and inflammatory responses

Peptidoglycan-induced modulation of metabolic and inflammatory responses

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DOI	10.1097/IN9.0000000000000024
刊名	Immunometabolism IJ
年，卷(期)	2023, 5(2)
作者	Wolf, Andrea J.,
作者单位	[Wolf, Andrea J.] Cedars Sinai Med Ctr, F Widjaja Fdn Inflammatory Bowel Dis Inst, Karsh Div Gastroenterol & Hepatol, Los Angeles, CA 90048 USA; [Wolf, Andrea J.] Cedars Sinai Med Ctr, Dept Biomed Sci, Res Div Immunol, Los Angeles, CA 90048 USA
摘要	Bacterial cell wall peptidoglycan is composed of innate immune ligands and, due to its important structural role, also regulates access to many other innate immune ligands contained within the bacteria. There is a growing body of literature demonstrating how innate immune recognition impacts the metabolic functions of immune cells and how metabolic changes are not only important to inflammatory responses but are often essential. Peptidoglycan is primarily sensed in the context of the whole bacteria during lysosomal degradation; consequently, the innate immune receptors for peptidoglycan are primarily intracellular cytosolic innate immune sensors. However, during bacterial growth, peptidoglycan fragments are shed and can be found in the bloodstream of humans and mice, not only during infection but also derived from the abundant bacterial component of the gut microbiota. These peptidoglycan fragments influence cells throughout the body and are important for regulating inflammation and whole-body metabolic function. Therefore, it is important to understand how peptidoglycan-induced signals in innate immune cells and cells throughout the body interact to regulate how the body responds to both pathogenic and nonpathogenic bacteria. This mini-review will highlight key research regarding how cellular metabolism shifts in response to peptidoglycan and how systemic peptidoglycan sensing impacts whole-body metabolic function.
Abstract	Bacterial cell wall peptidoglycan is composed of innate immune ligands and, due to its important structural role, also regulates access to many other innate immune ligands contained within the bacteria. There is a growing body of literature demonstrating how innate immune recognition impacts the metabolic functions of immune cells and how metabolic changes are not only important to inflammatory responses but are often essential. Peptidoglycan is primarily sensed in the context of the whole bacteria during lysosomal degradation; consequently, the innate immune receptors for peptidoglycan are primarily intracellular cytosolic innate immune sensors. However, during bacterial growth, peptidoglycan fragments are shed and can be found in the bloodstream of humans and mice, not only during infection but also derived from the abundant bacterial component of the gut microbiota. These peptidoglycan fragments influence cells throughout the body and are important for regulating inflammation and whole-body metabolic function. Therefore, it is important to understand how peptidoglycan-induced signals in innate immune cells and cells throughout the body interact to regulate how the body responds to both pathogenic and nonpathogenic bacteria. This mini-review will highlight key research regarding how cellular metabolism shifts in response to peptidoglycan and how systemic peptidoglycan sensing impacts whole-body metabolic function.
关键词	peptidoglycan; MDP; NOD1; NOD2; metabolism; inflammation
KeyWord	peptidoglycan; MDP; NOD1; NOD2; metabolism; inflammation
基金项目
页码	1-8

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[1]. Viola A, Munari F, Sánchez-Rodríguez R, et al. The metabolic signature of macrophage responses. Front Immunol. 2019;10:1462. doi: 10.3389/fimmu.2019.01462.

[2]. Garde S, Chodisetti PK, Reddy M. Peptidoglycan: structure, synthesis, and regulation. EcoSal Plus. 2021;9(2). doi: 10.1128/ecosalplus.ESP-0010-2020.

[3]. Vollmer W. Structural variation in the glycan strands of bacterial peptidoglycan. FEMS Microbiol Rev. 2008;32(2):287–306. doi: 10.1111/j.1574-6976.2007.00088.x.

[4]. Vollmer W, Blanot D, De Pedro MA. Peptidoglycan structure and architecture. FEMS Microbiol Rev. 2008;32(2):149–67. doi: 10.1111/j.1574-6976.2007.00094.x.

[5]. Wolf AJ, Reyes CN, Liang W, et al. Hexokinase is an innate immune receptor for the detection of bacterial peptidoglycan. Cell. 2016;166(3):624–36. doi: 10.1016/j.cell.2016.05.076.

[6]. Dziarski R. Recognition of bacterial peptidoglycan by the innate immune system. Cell Mol Life Sci. 2003;60(9):1793–804. doi: 10.1007/s00018-003-3019-6.

[7]. Bersch KL, DeMeester KE, Zagani R, et al. Bacterial peptidoglycan fragments differentially regulate innate immune signaling. Acs Central Sci. 2021;7(4):688–96. doi: 10.1021/acscentsci.1c00200.

[8]. Wolf AJ, Arruda A, Reyes CN, et al. Phagosomal degradation increases TLR access to bacterial ligands and enhances macrophage sensitivity to bacteria. J Immunol. 2011;187(11):6002–10. doi: 10.4049/jimmunol.1100232.

[9]. Ip WKE, Sokolovska A, Charriere GM, et al. Phagocytosis and phagosome acidification are required for pathogen processing and MyD88-dependent responses to Staphylococcus aureus. J Immunol. 2010;184(12):7071–81. doi: 10.4049/jimmunol.1000110.

[10]. Davis KM, Weiser JN. Modifications to the peptidoglycan backbone help bacteria to establish infection. Infect Immun. 2011;79(2):562–70. doi: 10.1128/iai.00651-10.

[11]. Girardin SE, Boneca IG, Carneiro LA, et al. Nod1 detects a unique muropeptide from gram-negative bacterial peptidoglycan. Science. 2003;300(5625):1584–7. doi: 10.1126/science.1084677.

[12]. Chamaillard M, Philpott D, Girardin SE, et al. Gene-environment interaction modulated by allelic heterogeneity in inflammatory diseases. Proc Natl Acad Sci U S A. 2003;100(6):3455–60. doi: 10.1073/pnas.0530276100.

[13]. Caruso R, Warner N, Inohara N, et al. NOD1 and NOD2: signaling, host defense, and inflammatory disease. Immunity. 2014;41(6):898–908. doi: 10.1016/j.immuni.2014.12.010.

[14]. Girardin SE, Travassos LH, Hervé M, et al. Peptidoglycan molecular requirements allowing detection by Nod1 and Nod2. J Biol Chem. 2003;278(43):41702–8. doi: 10.1074/jbc.M307198200.

[15]. Stafford CA, Gassauer A-M, Mann CCO, et al. Phosphorylation of muramyl peptides by NAGK is required for NOD2 activation. Nature. 2022;609(7927):590–6. doi: 10.1038/s41586-022-05125-x.

[16]. Broz P, Dixit VM. Inflammasomes: mechanism of assembly, regulation and signalling. Nat Rev Immunol. 2016;16(7):407–20. doi: 10.1038/nri.2016.58.

[17]. Shimada T, Park BG, Wolf AJ, et al. Staphylococcus aureus evades lysozyme-based peptidoglycan digestion that links phagocytosis, inflammasome activation, and IL-1beta secretion. Cell Host Microbe. 2010;7(1):38–49. doi: 10.1016/j.chom.2009.12.008.

[18]. Bauernfried S, Hornung V. Human NLRP1: from the shadows to center stage. J Exp Med. 2021;219(1). doi: 10.1084/jem.20211405.

[19]. Marina-García N, Franchi L, Kim YG, et al. Pannexin-1-mediated intracellular delivery of muramyl dipeptide induces caspase-1 activation via cryopyrin/NLRP3 independently of Nod2. J Immunol. 2008;180(6):4050–7. doi: 10.4049/jimmunol.180.6.4050.

[20]. Travassos LH, Girardin SE, Philpott DJ, et al. Toll-like receptor 2-dependent bacterial sensing does not occur via peptidoglycan recognition. EMBO Rep. 2004;5(10):1000–6. doi: 10.1038/sj.embor.7400248.

[21]. Wolf AJ, Liu GY, Underhill DM. Inflammatory properties of antibiotic-treated bacteria. J Leukoc Biol. 2017;101(1):127–34. doi: 10.1189/jlb.4MR0316-153RR.

[22]. Hashimoto M, Tawaratsumida K, Kariya H, et al. Lipoprotein is a predominant Toll-like receptor 2 ligand in Staphylococcus aureus cell wall components. Int Immunol. 2006;18(2):355–62. doi: 10.1093/intimm/dxh374.

[23]. Asong J, Wolfert MA, Maiti KK, et al. Binding and cellular activation studies reveal that toll-like receptor 2 can differentially recognize peptidoglycan from gram-positive and gram-negative bacteria*. J Biol Chem. 2009;284(13):8643–53. doi: 10.1074/jbc.M806633200.

[24]. Li Y, Efferson CL, Ramesh R, et al. A peptidoglycan monomer with the glutamine to serine change and basic peptides bind in silico to TLR-2 (403–455). Cancer Immunol Immunother. 2011;60(4):515–24. doi: 10.1007/s00262-010-0959-1.

[25]. Müller-Anstett MA, Müller P, Albrecht T, et al. Staphylococcal peptidoglycan co-localizes with Nod2 and TLR2 and activates innate immune response via both receptors in primary murine keratinocytes. PLoS One. 2010;5(10):e13153. doi: 10.1371/journal.pone.0013153.

[26]. Mukherjee T, Hovingh ES, Foerster EG, et al. NOD1 and NOD2 in inflammation, immunity and disease. Arch Biochem Biophys. 2019;670:69–81. doi: 10.1016/j.abb.2018.12.022.

[27]. Murugina NE, Budikhina AS, Dagil YA, et al. Glycolytic reprogramming of macrophages activated by NOD1 and TLR4 agonists: no association with proinflammatory cytokine production in normoxia. J Biol Chem. 2020;295(10):3099–114. doi: 10.1074/jbc.ra119.010589.

[28]. Lachmandas E, Beigier-Bompadre M, Cheng SC, et al. Rewiring cellular metabolism via the AKT/mTOR pathway contributes to host defence against Mycobacterium tuberculosis in human and murine cells. Eur J Immunol. 2016;46(11):2574–86. doi: 10.1002/eji.201546259.

[29]. Na YR, Gu GJ, Jung D, et al. GM-CSF induces inflammatory macrophages by regulating glycolysis and lipid metabolism. J Immunol. 2016;197(10):4101–9. doi: 10.4049/jimmunol.1600745.

[30]. Everts B, Amiel E, Huang SC, et al. TLR-driven early glycolytic reprogramming via the kinases TBK1-IKKɛ supports the anabolic demands of dendritic cell activation. Nat Immunol. 2014;15(4):323–32. doi: 10.1038/ni.2833.

[31]. Tannahill GM, Curtis AM, Adamik J, et al. Succinate is an inflammatory signal that induces IL-1β through HIF-1α. Nature. 2013;496(7444):238–42. doi: 10.1038/nature11986.

[32]. Dietl K, Renner K, Dettmer K, et al. Lactic acid and acidification inhibit TNF secretion and glycolysis of human monocytes. J Immunol. 2009;184(3):1200–9. doi: 10.4049/jimmunol.0902584.

[33]. Wang A, Huen SC, Luan HH, et al. Opposing effects of fasting metabolism on tissue tolerance in bacterial and viral inflammation. Cell. 2016;166(6):1512–1525.e12.

[34]. Freemerman AJ, Zhao L, Pingili AK, et al. Myeloid Slc2a1-deficient murine model revealed macrophage activation and metabolic phenotype are fueled by GLUT1. J Immunol. 2019;202(4):1265–86. doi: 10.4049/jimmunol.1800002.

[35]. Lee CW, Chung SW, Bae MJ, et al. Peptidoglycan up-regulates CXCL8 expression via multiple pathways in monocytes/macrophages. Biomol Ther. 2015;23(6):564–70. doi: 10.4062/biomolther.2015.053.

[36]. Zhao L, Lee JY, Hwang DH. The phosphatidylinositol 3-kinase/Akt pathway negatively regulates Nod2-mediated NF-κB pathway. Biochem Pharmacol. 2008;75(7):1515–25. doi: 10.1016/j.bcp.2007.12.014.

[37]. Vijayan V, Pradhan P, Braud L, et al. Human and murine macrophages exhibit differential metabolic responses to lipopolysaccharide—a divergent role for glycolysis. Redox Biol. 2019;22:101147. doi: 10.1016/j.redox.2019.101147.

[38]. Chapman TP, Corridoni D, Shiraishi S, et al. Ataxin-3 links NOD2 and TLR2 mediated innate immune sensing and metabolism in myeloid cells. Front Immunol. 2019;10:1495. doi: 10.3389/fimmu.2019.01495.

[39]. Oh SJ, Kim JH, Chung DH. NOD2-mediated suppression of CD55 on neutrophils enhances C5a generation during polymicrobial sepsis. PLoS Pathog. 2013;9(5):e1003351. doi: 10.1371/journal.ppat.1003351.

[40]. Gandotra S, Jang S, Murray PJ, et al. Nucleotide-binding oligomerization domain protein 2-deficient mice control infection with mycobacterium tuberculosis. Infect Immun. 2007;75(11):5127–34. doi: 10.1128/iai.00458-07.

[41]. Palmieri EM, Gonzalez-Cotto M, Baseler WA, et al. Nitric oxide orchestrates metabolic rewiring in M1 macrophages by targeting aconitase 2 and pyruvate dehydrogenase. Nat Commun. 2020;11(1):698. doi: 10.1038/s41467-020-14433-7.

[42]. Baseler WA, Davies LC, Quigley L, et al. Autocrine IL-10 functions as a rheostat for M1 macrophage glycolytic commitment by tuning nitric oxide production. Redox Biol. 2016;10:12–23. doi: 10.1016/j.redox.2016.09.005.

[43]. Ip WKE, Hoshi N, Shouval DS, et al. Anti-inflammatory effect of IL-10 mediated by metabolic reprogramming of macrophages. Science. 2017;356(6337):513–9. doi: 10.1126/science.aal3535.

[44]. Jin C, Flavell RA. Innate sensors of pathogen and stress: linking inflammation to obesity. J Allergy Clin Immun. 2013;132(2):287–94. doi: 10.1016/j.jaci.2013.06.022.

[45]. Tamrakar AK, Schertzer JD, Chiu TT, et al. NOD2 activation induces muscle cell-autonomous innate immune responses and insulin resistance. Endocrinology. 2010;151(12):5624–37. doi: 10.1210/en.2010-0437.

[46]. Zhao L, Hu P, Zhou Y, et al. NOD1 activation induces proinflammatory gene expression and insulin resistance in 3T3-L1 adipocytes. Am J Physiol Endocrinol Metab. 2011;301(4):E587–98. doi: 10.1152/ajpendo.00709.2010.

[47]. Zhou YJ, Tang YS, Song YL, et al. Saturated fatty acid induces insulin resistance partially through nucleotide-binding oligomerization domain 1 signaling pathway in adipocytes. Chin Med Sci J. 2013;28(4):211–7. doi: 10.1016/s1001-9294(14)60004-3.

[48]. Ieronymaki E, Daskalaki MG, Lyroni K, et al. Insulin signaling and insulin resistance facilitate trained immunity in macrophages through metabolic and epigenetic changes. Mini-review. Front Immunol. 2019;10:1330. doi: 10.3389/fimmu.2019.01330.

[49]. Ieronymaki E, Theodorakis EM, Lyroni K, et al. Insulin resistance in macrophages alters their metabolism and promotes an M2-Like phenotype. J Immunol. 2019;202(6):1786–97. doi: 10.4049/jimmunol.1800065.

[50]. Pandey AK, Yang Y, Jiang Z, et al. NOD2, RIP2 and IRF5 play a critical role in the type I interferon response to mycobacterium tuberculosis. PLoS Pathog. 2009;5(7):e1000500. doi: 10.1371/journal.ppat.1000500.

[51]. Olson GS, Murray TA, Jahn AN, et al. Type I interferon decreases macrophage energy metabolism during mycobacterial infection. Cell Rep. 2021;35(9):109195. doi: 10.1016/j.celrep.2021.109195.

[52]. Kaplan A, Ma J, Kyme P, et al. Failure to induce IFN-beta production during Staphylococcus aureus infection contributes to pathogenicity. J Immunol. 2012;189(9):4537–45. doi: 10.4049/jimmunol.1201111.

[53]. Chen B-C, Liao C-C, Hsu M-J, et al. Peptidoglycan-induced IL-6 production in RAW 264.7 macrophages is mediated by Cyclooxygenase-2, PGE2/PGE4 receptors, protein kinase A, IκB kinase, and NF-κB. J Immunol. 2006;177(1):681–93. doi: 10.4049/jimmunol.177.1.681.

[54]. Sanin DE, Matsushita M, Klein Geltink RI, et al. Mitochondrial membrane potential regulates nuclear gene expression in macrophages exposed to prostaglandin E2. Immunity. 2018;49(6):1021–1033.e6. doi: 10.1016/j.immuni.2018.10.011.

[55]. Dahiya Y, Pandey RK, Bhatt KH, et al. Role of prostaglandin E2 in peptidoglycan mediated iNOS expression in mouse peritoneal macrophages in vitro. FEBS Lett. 2010;584(19):4227–32. doi: 10.1016/j.febslet.2010.09.009.

[56]. Palmieri EM, McGinity C, Wink DA, et al. Nitric oxide in macrophage immunometabolism: hiding in plain sight. Metabolites. 2020;10(11):429. doi: 10.3390/metabo10110429.

[57]. Michelucci A, Cordes T, Ghelfi J, et al. Immune-responsive gene 1 protein links metabolism to immunity by catalyzing itaconic acid production. Proc Natl Acad Sci U S A. 2013;110(19):7820–5. doi: 10.1073/pnas.1218599110.

[58]. O’Neill LAJ, Artyomov MN. Itaconate: the poster child of metabolic reprogramming in macrophage function. Nat Rev Immunol. 2019;19(5):273–81. doi: 10.1038/s41577-019-0128-5.

[59]. Lampropoulou V, Sergushichev A, Bambouskova M, et al. Itaconate links inhibition of succinate dehydrogenase with macrophage metabolic remodeling and regulation of inflammation. Cell Metab. 2016;24(1):158–66. doi: 10.1016/j.cmet.2016.06.004.

[60]. Royet J, Gupta D, Dziarski R. Peptidoglycan recognition proteins: modulators of the microbiome and inflammation. Nat Rev Immunol. 2011;11(12):837–51. doi: 10.1038/nri3089.

[61]. Marzi MCD, Todone M, Ganem MB, et al. Peptidoglycan recognition protein–peptidoglycan complexes increase monocyte/macrophage activation and enhance the inflammatory response. Immunology. 2015;145(3):429–42. doi: 10.1111/imm.12460.

[62]. Sun D, Raisley B, Langer M, et al. Anti-peptidoglycan antibodies and Fcγ receptors are the key mediators of inflammation in Gram-positive sepsis. J Immunol. 2012;189(5):2423–31. doi: 10.4049/jimmunol.1201302.

[63]. Jing C, Castro-Dopico T, Richoz N, et al. Macrophage metabolic reprogramming presents a therapeutic target in lupus nephritis. Proc National Acad Sci. 2020;117(26):15160–71. doi: 10.1073/pnas.2000943117.

[64]. Hoepel W, Newling M, Vogelpoel LTC, et al. FcγR-TLR cross-talk enhances TNF production by human monocyte-derived DCs via IRF5-dependent gene transcription and glycolytic reprogramming. Original Research. Front Immunol. 2019;10:739. doi: 10.3389/fimmu.2019.00739.

[65]. Molinaro R, Mukherjee T, Flick R, et al. Trace levels of peptidoglycan in serum underlie the NOD-dependent cytokine response to endoplasmic reticulum stress. J Biol Chem. 2019;294(22):9007–15. doi: 10.1074/jbc.RA119.007997.

[66]. Huang Z, Wang J, Xu X, et al. Antibody neutralization of microbiota-derived circulating peptidoglycan dampens inflammation and ameliorates autoimmunity. Nat Microbiol. 2019;4(5):766–73. doi: 10.1038/s41564-019-0381-1.

[67]. Clarke TB, Davis KM, Lysenko ES, et al. Recognition of peptidoglycan from the microbiota by Nod1 enhances systemic innate immunity. Nat Med. 2010;16(2):228–31. doi: 10.1038/nm.2087.

[68]. Chan KL, Tam TH, Boroumand P, et al. Circulating NOD1 activators and hematopoietic NOD1 contribute to metabolic inflammation and insulin resistance. Cell Rep. 2017;18(10):2415–26. doi: 10.1016/j.celrep.2017.02.027.

[69]. Jutras BL, Lochhead RB, Kloos ZA, et al. Borrelia burgdorferi peptidoglycan is a persistent antigen in patients with Lyme arthritis. Proc Natl Acad Sci U S A. 2019;116(27):13498–507. doi: 10.1073/pnas.1904170116.

[70]. Chi W, Dao D, Lau TC, et al. Bacterial peptidoglycan stimulates adipocyte lipolysis via NOD1. PLoS One. 2014;9(5):e97675e97675. doi: 10.1371/journal.pone.0097675.

[71]. J SP, Hu P, Burke SJ, et al. The effects of NOD activation on adipocyte differentiation. Obesity (Silver Spring). 2013;21(4):737–47. doi: 10.1002/oby.20275.

[72]. Ferrand A, Al Nabhani Z, Tapias NS, et al. NOD2 expression in intestinal epithelial cells protects toward the development of inflammation and associated carcinogenesis. Cell Mol Gastroenterol Hepatol. 2019;7(2):357–69. doi: 10.1016/j.jcmgh.2018.10.009.

[73]. Hugot JP, Chamaillard M, Zouali H, et al. Association of NOD2 leucine-rich repeat variants with susceptibility to Crohn’s disease. Nature. 2001;411(6837):599–603. doi: 10.1038/35079107.

[74]. Ayabe T, Satchell DP, Wilson CL, et al. Secretion of microbicidal alpha-defensins by intestinal Paneth cells in response to bacteria. Nat Immunol. 2000;1(2):113–8. doi: 10.1038/77783.

[75]. Ramanan D, Tang Mei S, Bowcutt R, et al. Bacterial sensor Nod2 prevents inflammation of the small intestine by restricting the expansion of the commensal bacteroides vulgatus. Immunity. 2014;41(2):311–24. doi: 10.1016/j.immuni.2014.06.015.

[76]. Yamamoto-Furusho JK, Barnich N, Hisamatsu T, et al. MDP-NOD2 stimulation induces HNP-1 secretion, which contributes to NOD2 antibacterial function. Inflamm Bowel Dis. 2010;16(5):736–42. doi: 10.1002/ibd.21144.

[77]. Richardson WM, Sodhi CP, Russo A, et al. Nucleotide-binding oligomerization domain-2 inhibits toll-like receptor-4 signaling in the intestinal epithelium. Gastroenterology. 2010;139(3):904–17, 917.e1. doi: 10.1053/j.gastro.2010.05.038.

[78]. Barreau F, Madre C, Meinzer U, et al. Nod2 regulates the host response towards microflora by modulating T cell function and epithelial permeability in mouse Peyer’s patches. Gut. 2010;59(2):207–17. doi: 10.1136/gut.2008.171546.

[79]. Laman JD, Hart BA, Power C, et al. Bacterial peptidoglycan as a driver of chronic brain inflammation. Trends Mol Med. 2020;26(7):670–82. doi: 10.1016/j.molmed.2019.11.006.

[80]. Amar J, Chabo C, Waget A, et al. Intestinal mucosal adherence and translocation of commensal bacteria at the early onset of type 2 diabetes: molecular mechanisms and probiotic treatment. EMBO Mol Med. 2011;3(9):559–72. doi: 10.1002/emmm.201100159.

[81]. Zhao L, Kwon M-J, Huang S, et al. Differential modulation of nods signaling pathways by fatty acids in human colonic epithelial HCT116 cells*. J Biol Chem. 2007;282(16):11618–28. doi: 10.1074/jbc.m608644200.

[82]. Zhang Q, Pan Y, Zeng B, et al. Intestinal lysozyme liberates Nod1 ligands from microbes to direct insulin trafficking in pancreatic beta cells. Cell Res. 2019;29(7):516–32. doi: 10.1038/s41422-019-0190-3.

[83]. Denou E, Lolmède K, Garidou L, et al. Defective NOD2 peptidoglycan sensing promotes diet-induced inflammation, dysbiosis, and insulin resistance. EMBO Mol Med. 2015;7(3):259–74. doi: 10.15252/emmm.201404169.

[84]. Rodriguez-Nunez I, Caluag T, Kirby K, et al. Nod2 and Nod2-regulated microbiota protect BALB/c mice from diet-induced obesity and metabolic dysfunction. Sci Rep. 2017;7(1):548. doi: 10.1038/s41598-017-00484-2.

[85]. Cavallari JF, Barra NG, Foley KP, et al. Postbiotics for NOD2 require nonhematopoietic RIPK2 to improve blood glucose and metabolic inflammation in mice. Am J Physiol Endocrinol Metab. 2020;318(4):E579–85. doi: 10.1152/ajpendo.00033.2020.

[86]. Schwarzer M, Gautam UK, Makki K, et al. Microbe-mediated intestinal NOD2 stimulation improves linear growth of undernourished infant mice. Science. 2023;379(6634):826–33. doi: 10.1126/science.ade9767.

[87]. Gabanyi I, Lepousez G, Wheeler R, et al. Bacterial sensing via neuronal Nod2 regulates appetite and body temperature. Science. 2022;376(6590):eabj3986. doi: 10.1126/science.abj3986.

[88]. Schertzer JD, Tamrakar AK, Magalhães JG, et al. NOD1 activators link innate immunity to insulin resistance. Diabetes. 2011;60(9):2206–15. doi: 10.2337/db11-0004.

[89]. Vandanmagsar B, Youm Y-H, Ravussin A, et al. The NLRP3 inflammasome instigates obesity-induced inflammation and insulin resistance. Nat Med. 2011;17(2):179–88. doi: 10.1038/nm.2279.

[90]. Tada H, Aiba S, Shibata K, et al. Synergistic effect of Nod1 and Nod2 agonists with toll-like receptor agonists on human dendritic cells to generate interleukin-12 and T helper type 1 cells. Infect Immun. 2005;73(12):7967–76. doi: 10.1128/iai.73.12.7967-7976.2005.

[91]. Pei G, Zyla J, He L, et al. Cellular stress promotes NOD1/2-dependent inflammation via the endogenous metabolite sphingosine-1-phosphate. EMBO J. 2021;40(13):e106272. doi: 10.15252/embj.2020106272.

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Wolf, Andrea J.. Peptidoglycan-induced modulation of metabolic and inflammatory responses [J]. Immunometabolism. 2023; 5; (2). 1 - 8.

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