The Immune Receptor NOD1 and Kinase RIP2 Interact with Bacterial Peptidoglycan on Early Endosomes to Promote Autophagy and Inflammatory Signaling
The intracellular innate immune receptor NOD1 detects Gram-negative bacterial peptidoglycan (PG) to induce autophagy and inflammatory responses in host cells. To date, the intracellular compartment in which PG is detected by NOD1 and whether NOD1 directly interacts with PG are two questions that rem...
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Published in | Cell host & microbe Vol. 15; no. 5; pp. 623 - 635 |
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Main Authors | , , , , , , , , , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
United States
Elsevier Inc
14.05.2014
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Subjects | |
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Abstract | The intracellular innate immune receptor NOD1 detects Gram-negative bacterial peptidoglycan (PG) to induce autophagy and inflammatory responses in host cells. To date, the intracellular compartment in which PG is detected by NOD1 and whether NOD1 directly interacts with PG are two questions that remain to be resolved. To address this, we used outer membrane vesicles (OMVs) from pathogenic bacteria as a physiological mechanism to deliver PG into the host cell cytosol. We report that OMVs induced autophagosome formation and inflammatory IL-8 responses in epithelial cells in a NOD1- and RIP2-dependent manner. PG contained within OMVs colocalized with both NOD1 and RIP2 in EEA1-positive early endosomes. Further, we provide evidence for direct interactions between NOD1 and PG. Collectively, these findings demonstrate that NOD1 detects PG within early endosomes, thereby promoting RIP2-dependent autophagy and inflammatory signaling in response to bacterial infection.
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•Bacterial outer membrane vesicles (OMVs) induce autophagy in epithelial cells•NOD1 and RIP2 are essential for autophagy and inflammatory IL-8 responses to OMVs•NOD1 and RIP2 associate with OMV peptidoglycan (PG) in EEA1-positive early endosomes•NOD1 interacts directly with PG-OMVs and RIP2 at early endosomes
The intracellular innate immune receptor NOD1 detects Gram-negative bacterial peptidoglycan; however, details regarding the mechanisms whereby this process occurs remain unknown. Irving et al. identify that NOD1 interacts with bacterial delivered peptidoglycan and RIP2 in early endosomes, facilitating the development of autophagy and IL-8 production in a RIP2-dependent manner. |
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AbstractList | The intracellular innate immune receptor NOD1 detects Gram-negative bacterial peptidoglycan (PG) to induce autophagy and inflammatory responses in host cells. To date, the intracellular compartment in which PG is detected by NOD1 and whether NOD1 directly interacts with PG are two questions that remain to be resolved. To address this, we used outer membrane vesicles (OMVs) from pathogenic bacteria as a physiological mechanism to deliver PG into the host cell cytosol. We report that OMVs induced autophagosome formation and inflammatory IL-8 responses in epithelial cells in a NOD1- and RIP2-dependent manner. PG contained within OMVs colocalized with both NOD1 and RIP2 in EEA1-positive early endosomes. Further, we provide evidence for direct interactions between NOD1 and PG. Collectively, these findings demonstrate that NOD1 detects PG within early endosomes, thereby promoting RIP2-dependent autophagy and inflammatory signaling in response to bacterial infection. The intracellular innate immune receptor NOD1 detects Gram-negative bacterial peptidoglycan (PG) to induce autophagy and inflammatory responses in host cells. To date, the intracellular compartment in which PG is detected by NOD1 and whether NOD1 directly interacts with PG are two questions that remain to be resolved. To address this, we used outer membrane vesicles (OMVs) from pathogenic bacteria as a physiological mechanism to deliver PG into the host cell cytosol. We report that OMVs induced autophagosome formation and inflammatory IL-8 responses in epithelial cells in a NOD1- and RIP2-dependent manner. PG contained within OMVs colocalized with both NOD1 and RIP2 in EEA1-positive early endosomes. Further, we provide evidence for direct interactions between NOD1 and PG. Collectively, these findings demonstrate that NOD1 detects PG within early endosomes, thereby promoting RIP2-dependent autophagy and inflammatory signaling in response to bacterial infection. [Display omitted] •Bacterial outer membrane vesicles (OMVs) induce autophagy in epithelial cells•NOD1 and RIP2 are essential for autophagy and inflammatory IL-8 responses to OMVs•NOD1 and RIP2 associate with OMV peptidoglycan (PG) in EEA1-positive early endosomes•NOD1 interacts directly with PG-OMVs and RIP2 at early endosomes The intracellular innate immune receptor NOD1 detects Gram-negative bacterial peptidoglycan; however, details regarding the mechanisms whereby this process occurs remain unknown. Irving et al. identify that NOD1 interacts with bacterial delivered peptidoglycan and RIP2 in early endosomes, facilitating the development of autophagy and IL-8 production in a RIP2-dependent manner. |
Author | Thomas, Belinda J. Casillas, Linda N. Gantier, Michael P. Kaparakis-Liaskos, Maria Lo, Camden Votta, Bartholomew J. Malosse, Christian Bertin, John Kufer, Thomas A. Ferrero, Richard L. Sasakawa, Chihiro Turner, Lorinda J. Boneca, Ivo G. Philpott, Dana J. Wheeler, Richard Irving, Aaron T. Mimuro, Hitomi |
Author_xml | – sequence: 1 givenname: Aaron T. surname: Irving fullname: Irving, Aaron T. organization: Centre for Cancer Research, Monash Institute of Medical Research, Clayton, VIC 3168, Australia – sequence: 2 givenname: Hitomi surname: Mimuro fullname: Mimuro, Hitomi organization: Division of Bacteriology, Department of Infectious Diseases Control, International Research Center for Infectious Diseases, Institute of Medical Science, The University of Tokyo, Tokyo 108-8639, Japan – sequence: 3 givenname: Thomas A. surname: Kufer fullname: Kufer, Thomas A. organization: Institute for Medical Microbiology, Immunology and Hygiene, University of Cologne, Köln 50931, Germany – sequence: 4 givenname: Camden surname: Lo fullname: Lo, Camden organization: Monash Micro Imaging, Clayton, VIC 3168, Australia – sequence: 5 givenname: Richard surname: Wheeler fullname: Wheeler, Richard organization: Institut Pasteur, Unité Biologie et Génétique de la Paroi Bactérienne, Paris 75015, France – sequence: 6 givenname: Lorinda J. surname: Turner fullname: Turner, Lorinda J. organization: Centre for Innate Immunity and Infectious Diseases, Monash Institute of Medical Research, Clayton, VIC 3168, Australia – sequence: 7 givenname: Belinda J. surname: Thomas fullname: Thomas, Belinda J. organization: Centre for Innate Immunity and Infectious Diseases, Monash Institute of Medical Research, Clayton, VIC 3168, Australia – sequence: 8 givenname: Christian surname: Malosse fullname: Malosse, Christian organization: Institut Pasteur, Structural Mass Spectrometry and Proteomics Unit, Paris 75015, France – sequence: 9 givenname: Michael P. surname: Gantier fullname: Gantier, Michael P. organization: Centre for Cancer Research, Monash Institute of Medical Research, Clayton, VIC 3168, Australia – sequence: 10 givenname: Linda N. surname: Casillas fullname: Casillas, Linda N. organization: Pattern Recognition Receptor Discovery Performance Unit, Immuno-Inflammation Therapy Area, GlaxoSmithKline, Collegeville, PA 19426-0989, USA – sequence: 11 givenname: Bartholomew J. surname: Votta fullname: Votta, Bartholomew J. organization: Pattern Recognition Receptor Discovery Performance Unit, Immuno-Inflammation Therapy Area, GlaxoSmithKline, Collegeville, PA 19426-0989, USA – sequence: 12 givenname: John surname: Bertin fullname: Bertin, John organization: Pattern Recognition Receptor Discovery Performance Unit, Immuno-Inflammation Therapy Area, GlaxoSmithKline, Collegeville, PA 19426-0989, USA – sequence: 13 givenname: Ivo G. surname: Boneca fullname: Boneca, Ivo G. organization: Institut Pasteur, Unité Biologie et Génétique de la Paroi Bactérienne, Paris 75015, France – sequence: 14 givenname: Chihiro surname: Sasakawa fullname: Sasakawa, Chihiro organization: Division of Bacterial Infection Biology, Institute of Medical Science, The University of Tokyo, Tokyo 108-8639, Japan – sequence: 15 givenname: Dana J. surname: Philpott fullname: Philpott, Dana J. organization: Department of Immunology, University of Toronto, Toronto, ON M5S 1A8, Canada – sequence: 16 givenname: Richard L. surname: Ferrero fullname: Ferrero, Richard L. organization: Centre for Innate Immunity and Infectious Diseases, Monash Institute of Medical Research, Clayton, VIC 3168, Australia – sequence: 17 givenname: Maria surname: Kaparakis-Liaskos fullname: Kaparakis-Liaskos, Maria email: maria.liaskos@monash.edu organization: Centre for Innate Immunity and Infectious Diseases, Monash Institute of Medical Research, Clayton, VIC 3168, Australia |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/24746552$$D View this record in MEDLINE/PubMed |
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Title | The Immune Receptor NOD1 and Kinase RIP2 Interact with Bacterial Peptidoglycan on Early Endosomes to Promote Autophagy and Inflammatory Signaling |
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