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Endosomes are specialized platforms for bacterial sensing and NOD2 signalling
Abstract
The detection of microbial pathogens involves the recognition of conserved microbial components by host cell sensors such as Toll-like receptors (TLRs) and NOD-like receptors (NLRs). TLRs are membrane receptors that survey the extracellular environment for microbial infections, whereas NLRs are cytosolic complexes that detect microbial products that reach the cytosol. Upon detection, both sensor classes trigger innate inflammatory responses and allow the engagement of adaptive immunity. Endo-lysosomes are the entry sites for a variety of pathogens, and therefore the sites at which the immune system first senses their presence. Pathogens internalized by endocytosis are well known to activate TLRs 3 and 7-9 that are localized to endocytic compartments and detect ligands present in the endosomal lumen. Internalized pathogens also activate sensors in the cytosol such as NOD1 and NOD2 (ref. 2), indicating that endosomes also provide for the translocation of bacterial components across the endosomal membrane. Despite the fact that NOD2 is well understood to have a key role in regulating innate immune responses and that mutations at the NOD2 locus are a common risk factor in inflammatory bowel disease and possibly other chronic inflammatory states, little is known about how its ligands escape from endosomes. Here we show that two endo-lysosomal peptide transporters, SLC15A3 and SLC15A4, are preferentially expressed by dendritic cells, especially after TLR stimulation. The transporters mediate the egress of bacterially derived components, such as the NOD2 cognate ligand muramyl dipeptide (MDP), and are selectively required for NOD2 responses to endosomally derived MDP. Enhanced expression of the transporters also generates endosomal membrane tubules characteristic of dendritic cells, which further enhanced the NOD2-dependent response to MDP. Finally, sensing required the recruitment of NOD2 and its effector kinase RIPK2 (refs 8, 9) to the endosomal membrane, possibly by forming a complex with SLC15A3 or SLC15A4. Thus, dendritic cell endosomes are specialized platforms for both the lumenal and cytosolic sensing of pathogens.
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“Previously, oligopeptide transporters encoded by SLC15A3 and SLC15A4 were reported to be responsible for transporting small peptidoglycan (PGN) fragments into macrophages (Nakamura et al., 2014).”
From Intestinal microbiota modulates adrenomedullary response through Nod1 sensing in chromaffin cells (2021) · cites this paper as Nakamura et al., 2014
In the citing paper
“It was previously reported that oligopeptide transporters encoded by SLC15A3 and SLC15A4 are responsible for transporting small PGN fragments into macrophages (Nakamura et al., 2014).”
From Intestinal microbiota modulates adrenomedullary response through Nod1 sensing in chromaffin cells (2021) · cites this paper as Nakamura et al., 2014
Citations
Cites
Association of NOD2 leucine-rich repeat variants with susceptibility to Crohn's disease
Hugot, J.-P., Chamaillard, M., Zouali, H., Lesage, S., Cézard, J.-P., Belaiche, J., Almer, S., Tysk, C., O'Morain, C. A., Gassull, M., et al. (2001) · Nature · doi:10.1038/35079107 · Cited by 5,591
A frameshift mutation in NOD2 associated with susceptibility to Crohn's disease
Ogura, Y., Bonen, D. K., Inohara, N., Nicolae, D. L., Chen, F. F., Ramos, R., Britton, H., Moran, T., Karaliuskas, R., Duerr, R. H., et al. (2001) · Nature · doi:10.1038/35079114 · Cited by 5,030
Large-scale analysis of the yeast proteome by multidimensional protein identification technology
Washburn, M. P., Wolters, D. A., & Yates, J. R. (2001) · Nature Biotechnology · doi:10.1038/85686 · Cited by 4,768
Toll-like receptors and their crosstalk with other innate receptors in infection and immunity
Kawai, T., & Akira, S. (2011) · Immunity · doi:10.1016/j.immuni.2011.05.006 · Cited by 3,658
A Model for Random Sampling and Estimation of Relative Protein Abundance in Shotgun Proteomics
Liu, H., Sadygov, R. G., & Yates, J. R. (2004) · Analytical Chemistry · doi:10.1021/ac0498563 · Cited by 2,534
Nod2 Is a General Sensor of Peptidoglycan through Muramyl Dipeptide (MDP) Detection
Girardin, S. E., Boneca, I. G., Viala, J., Chamaillard, M., Labigne-Roussel, A., Thomas, G. D., Philpott, D. J., & Sansonetti, P. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c200651200 · Cited by 2,397
ACIDIFICATION OF THE ENDOCYTIC AND EXOCYTIC PATHWAYS
Mellman, I., Fuchs, R., & Helenius, A. (1986) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.55.070186.003311 · Cited by 2,045
Self-citationSignals for Sorting of Transmembrane Proteins to Endosomes and Lysosomes
Bonifacino, J. S., & Traub, L. M. (2003) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.72.121801.161800 · Cited by 2,040
Host Recognition of Bacterial Muramyl Dipeptide Mediated through NOD2
Inohara, N., Ogura, Y., Fontalba, A., Gutierrez, O., Pons, F., Crespo, J., Fukase, K., Inamura, S., Kusumoto, S., Hashimoto, M., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c200673200 · Cited by 1,694
Nod1 Detects a Unique Muropeptide from Gram-Negative Bacterial Peptidoglycan
Girardin, S. E., Boneca, I. G., Carneiro, L. A. M., Antignac, A., Jéhanno, M., Viala, J., Tedin, K., Taha, M., Labigne-Roussel, A., Zäthringer, U., et al. (2003) · Science · doi:10.1126/science.1084677 · Cited by 1,625
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Parkhouse, R., Boyle, J. P., & Monie, T. P. (2014) · FEBS Letters · doi:10.1016/j.febslet.2014.07.029 · Cited by 40
Pulica, R., Aquib, A., Varsanyi, C., Gadiyar, V., Wang, Z., Frederick, T., Calianese, D. C., Patel, B., de Dios, K. V., Poalasin, V., et al. (2025) · Cell Communication and Signaling · doi:10.1186/s12964-025-02090-6 · Cited by 41
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Odendall, C., & Kagan, J. C. (2017) · Microbes and Infection · doi:10.1016/j.micinf.2017.01.003 · Cited by 41
Molecular actions of NLR immune receptors in plants and animals
Wang, J., & Chai, J. (2020) · Science China Life Sciences · doi:10.1007/s11427-019-1687-6 · Cited by 40
Gobec, M., Tomašič, T., Štimac, A., Frkanec, R., Trontelj, J., Anderluh, M., Mlinarič‐Raščan, I., & Jakopin, Ž. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b01052 · Cited by 40
Kuss-Duerkop, S. K., & Keestra, A. M. (2020) · Infection and Immunity · doi:10.1128/iai.00898-19 · Cited by 39
Liu, Z., Zhang, Y., Jin, T., Yi, C., Ocansey, D. K. W., & Mao, F. (2022) · International Immunopharmacology · doi:10.1016/j.intimp.2022.109466 · Cited by 37
Wang, Y., Hu, Y., Li, P., Weng, Y., Kamada, N., Jiang, H., & Smith, D. E. (2018) · Biochemical Pharmacology · doi:10.1016/j.bcp.2017.12.025 · Cited by 35
Balasubramanian, I., & Gao, N. (2017) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00330.2016 · Cited by 34
Ng, P. Y., Ribet, A. B. P., Guo, Q., Mullin, B. H., Tan, J., Landao‐Bassonga, E., Stephens, S., Chen, K., Yuan, J., Abudulai, L. N., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36484-2 · Cited by 36
Song, F., Hu, Y., Wang, Y., Smith, D. E., & Jiang, H. (2017) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.7b00728 · Cited by 33
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Ag/FeCo/Ag Core/Shell/Shell Magnetic Nanoparticles with Plasmonic Imaging Capability
Takahashi, M. I., Mohan, P., Nakade, A., Higashimine, K., Mott, D. M., Hamada, T., Matsumura, K., Taguchi, T., & Maenosono, S. (2015) · Langmuir · doi:10.1021/la5046805 · Cited by 32
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Katewa, A., Suto, E., Hui, J., Heredia, J. E., Liang, J., Hackney, J. A., Anderson, K. R., Alcantar, T. M., Bacarro, N., Dunlap, D. Y., et al. (2021) · PLoS ONE · doi:10.1371/journal.pone.0244439 · Cited by 32
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He, L., Wang, B., Li, Y., Zhu, L., Li, P., Zou, F., & Bin, L. (2018) · Journal of Immunology Research · doi:10.1155/2018/5214187 · Cited by 31
Membrane Association Dictates Ligand Specificity for the Innate Immune Receptor NOD2
Schaefer, A. K., Melnyk, J. E., Baksh, M. M., Bersch, K. L., Finn, M. G., & Grimes, C. L. (2017) · ACS Chemical Biology · doi:10.1021/acschembio.7b00469 · Cited by 34
Joo, Y. B., Lim, J., Tsao, B. P., Nath, S. K., Kim, K.-W., & Bae, S. (2018) · Scientific Reports · doi:10.1038/s41598-018-28128-z · Cited by 31
XIAP controls RIPK2 signaling by preventing its deposition in speck-like structures
Ellwanger, K., Briese, S., Arnold, C. M., Kienes, I., Heim, V. J., Nachbur, U., & Kufer, T. A. (2019) · Life Science Alliance · doi:10.26508/lsa.201900346 · Cited by 32
Kufer, T. A., Nigro, G., & Sansonetti, P. J. (2016) · Microbiology Spectrum · doi:10.1128/microbiolspec.mchd-0021-2015 · Cited by 30
Suzuki, H., Yamazaki, T., Ohshio, K., Sugamata, M., Yoshikawa, M., Kanauchi, O., & Morita, Y. (2020) · The Journal of Immunology · doi:10.4049/jimmunol.1900657 · Cited by 30
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Gobec, M., Mlinarič‐Raščan, I., Dolenc, M. S., & Jakopin, Ž. (2016) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2016.03.030 · Cited by 28
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Yu, L. C. (2015) · Tissue Barriers · doi:10.1080/21688370.2015.1008895 · Cited by 26
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Khan, A., Singh, V. K., Mishra, A., Soudani, E., Bakhru, P., Singh, C. R., Zhang, D., Canaday, D. H., Sheri, A., Padmanabhan, S., et al. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.592333 · Cited by 24
Bai, F., McCormack, R., Hower, S., Plano, G. V., Lichtenheld, M. G., & Munson, G. P. (2018) · The Journal of Immunology · doi:10.4049/jimmunol.1800365 · Cited by 23
Vanaki, N., Golmohammadi, T., Jamshidi, A., Akhtari, M., Vojdanian, M., Mostafaei, S., Poursani, S., Ahmadzadeh, N., & Mahmoudi, M. (2018) · Immunopharmacology and Immunotoxicology · doi:10.1080/08923973.2018.1510963 · Cited by 23
Nozawa, T., Aikawa, C., Minowa‐Nozawa, A., & Nakagawa, I. (2017) · Autophagy · doi:10.1080/15548627.2017.1358343 · Cited by 23
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Hardman, C. S., Chen, Y., Salimi, M., Nahler, J., Corridoni, D., Jagielowicz, M., Fonseka, C. L., Johnson, D., Repapi, E., Cousins, D. J., et al. (2021) · Science Immunology · doi:10.1126/sciimmunol.abe5084 · Cited by 22
Loh, L. N., Gao, G., & TUOMANEN, E. I. (2017) · mBio · doi:10.1128/mbio.02030-16 · Cited by 22
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Sun, Y., Ho, C., & Zhang, X. (2023) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.2c07742 · Cited by 21
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Post, S., Rueschpler, L., & Schloer, S. (2025) · Pharmacological Research · doi:10.1016/j.phrs.2025.108051 · Cited by 20
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Yoshikawa, M., Yamada, S., Sugamata, M., Kanauchi, O., & Morita, Y. (2021) · Scientific Reports · doi:10.1038/s41598-021-97087-9 · Cited by 20
Mylvaganam, S., & Freeman, S. A. (2023) · Immunological Reviews · doi:10.1111/imr.13260 · Cited by 23
Ragland, S. A., & Kagan, J. C. (2021) · Molecular Microbiology · doi:10.1111/mmi.14841 · Cited by 22
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Bonham, K. S., & Kagan, J. C. (2014) · Cell Host & Microbe · doi:10.1016/j.chom.2014.05.001 · Cited by 21
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Custódio, T. F., Killer, M., Yu, D., Puente, V., Teufel, D. P., Pautsch, A., Schnapp, G., Grundl, M., Kosinski, J., & Löw, C. (2023) · Nature Communications · doi:10.1038/s41467-023-41420-5 · Cited by 19
Protein Lipidation by Palmitate Controls Macrophage Function
Guns, J., Vanherle, S., Hendriks, J. J. A., & Bogie, J. F. J. (2022) · Cells · doi:10.3390/cells11030565 · Cited by 18
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Saeki, A., SUGIYAMA, M., Hasebe, A., Suzuki, T., & Shibata, K. (2018) · Molecular Oral Microbiology · doi:10.1111/omi.12225 · Cited by 18
Zhang, J., He, J. N., Johnson, J. L., Napolitano, G., Ramadass, M., Rahman, F., & Catz, S. D. (2019) · Autophagy · doi:10.1080/15548627.2019.1596475 · Cited by 18
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Dixon, C. L., Martin, N. R., Niphakis, M. J., Cravatt, B. F., & Fairn, G. D. (2025) · Cellular and Molecular Gastroenterology and Hepatology · doi:10.1016/j.jcmgh.2025.101491 · Cited by 17
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Oji, S., Nicolussi, E.-M., Kaufmann, N. C., Zeka, B., Schanda, K., Fujihara, K., Illés, Z., Dahle, C., Reindl, M., Lassmann, H., et al. (2016) · PLoS ONE · doi:10.1371/journal.pone.0151244 · Cited by 17
Zhang, M., Chen, F., Zhang, D., Zhai, Z., & Hao, F. (2016) · Genetic Testing and Molecular Biomarkers · doi:10.1089/gtmb.2015.0289 · Cited by 17
Wang, X.-X., Hu, Y., Keep, R. F., Toyama‐Sorimachi, N., & Smith, D. E. (2016) · Biochemical Pharmacology · doi:10.1016/j.bcp.2016.11.012 · Cited by 17
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Merselis, L. C., Rivas, Z. P., & Munson, G. P. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.597951 · Cited by 17
Zuckermann, F. A., Husmann, R. J., Chen, W., Roady, P. J., Pfeiff, J., Leistikow, K. R., Duersteler, M., Son, S., King, M. R., & Augspurger, N. R. (2022) · Infection and Immunity · doi:10.1128/iai.00574-21 · Cited by 19
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Chen, Y.-G., Yuan, K., Zhang, Z.-Z., Yuan, F.-H., Weng, S., Yue, H.-T., He, J.-G., & Chen, Y.-H. (2016) · Developmental and Comparative Immunology · doi:10.1016/j.dci.2015.12.005 · Cited by 19
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Hruška, K., & Pavlík, I. (2014) · Veterinární Medicína · doi:10.17221/7822-vetmed · Cited by 16
Intestinal microbiota modulates adrenomedullary response through Nod1 sensing in chromaffin cells
Xiang, C., Chen, P., Zhang, Q., Li, Y., Pan, Y., Xie, W., Sun, J., & Liu, Z. (2021) · iScience · doi:10.1016/j.isci.2021.102849 · Cited by 15
Lysosomal control of dendritic cell function
Yang, J., Rong, S.-J., Zhou, H., Yang, C., Sun, F., & Li, J. (2023) · Journal of Leukocyte Biology · doi:10.1093/jleuko/qiad117 · Cited by 15
Wheeler, R., & Boneca, I. G. (2024) · Gut Microbes · doi:10.1080/19490976.2024.2395099 · Cited by 16
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Miyake, K., Saitoh, S.-I., Sato, R., Shibata, T., Fukui, R., & Murakami, Y. (2019) · Journal of Leukocyte Biology · doi:10.1002/jlb.mr0119-020r · Cited by 17
Capo, F., Chaduli, D., Viallat-Lieutaud, A., Charroux, B., & Royet, J. (2017) · Journal of Innate Immunity · doi:10.1159/000475771 · Cited by 15
Schlam, D., & Canton, J. (2016) · Small GTPases · doi:10.1080/21541248.2016.1197873 · Cited by 18
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Delgado, M. L. O., Magalhaes, J. G., Morra, R., & Cultrone, A. (2024) · Gut Microbes · doi:10.1080/19490976.2024.2418412 · Cited by 14
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Jungnickel, K. E. J., Guelle, O., Iguchi, M., Dong, W., Kotov, V., Gabriel, F., Debacker, C., Dairou, J., McCort‐Tranchepain, I., Laqtom, N. N., et al. (2024) · Nature Cell Biology · doi:10.1038/s41556-024-01436-5 · Cited by 15
Compeer, E. B., & Boes, M. L. (2014) · Communicative & Integrative Biology · doi:10.4161/19420889.2014.994969 · Cited by 13
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Li, L., Ng, A. W. R., Adamson, C., Hayashi, H., Li, C., Lim, H., & Qiao, Y. (2022) · ACS Chemical Biology · doi:10.1021/acschembio.2c00468 · Cited by 13
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Chen, K., Yang, C.-Y., Shu, S.-G., Lo, Y.-C., Lee, K.-W., Wang, L.-C., Chen, J.-B., Shih, M.-C., Chang, H.-C., Hsiao, Y.-J., et al. (2024) · Science Advances · doi:10.1126/sciadv.adq0660 · Cited by 12
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Metadata
- Authors
- Nakamura, N., Lill, J. R., Phung, Q., Jiang, Z., Bakalarski, C., de Mazière, A., Klumperman, J., Schlatter, M., Delamarre, L., & Mellman, I.
- Affiliations
- Genentech (US)
- University Medical Center Utrecht (NL)
- Corresponding author
- Mellman, Ira
- ORCID
- Venue
- Nature
- Published
- 2014-03-30
- Volume
- 509
- Issue
- 7499
- Pages
- 240-244
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2031113436
- Cited by
- 313
- References
- 40
- Citations by year
- 2026: 13 · 2025: 22 · 2024: 18 · 2023: 33 · 2022: 29 · 2021: 27 · 2020: 23 · 2019: 23 · 2018: 32 · 2017: 30 · 2016: 25 · 2015: 21 · 2014: 16
- FWCI
- 14.15
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Immunology and Microbiology › Immunology › Immunotherapy and Immune Responses
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Keywords
- signaling, endosomes, SLC15A4, dendritic cells, muramyl dipeptide, NOD-like receptors, NOD1, innate immunity, endosomal escape, TLR stimulation, inflammatory bowel disease, endocytosis, pattern recognition receptors
- MeSH terms
- Acetylmuramyl-Alanyl-Isoglutamine, Animals, Carrier Proteins, Cytoplasm, Dendritic Cells, Immunity, Innate, Inflammation, Ligands, Lysosomes, Nerve Tissue Proteins, Phagosomes, Endosomes, Salmonella typhimurium, Inflammatory Bowel Diseases, Membrane Transport Proteins, Mice, Nod2 Signaling Adaptor Protein
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