Multifaceted Functions of NOD-Like Receptor Proteins in Myeloid Cells at the Intersection of Innate and Adaptive Immunity
- Authors: Thomas A. Kufer1, Giulia Nigro2,3, Philippe J. Sansonetti4,5,6
- Editor: Siamon Gordon7
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VIEW AFFILIATIONS HIDE AFFILIATIONSAffiliations: 1: Institute of Nutritional Medicine, Department of Immunology, University of Hohenheim, 70593 Stuttgart, Germany; 2: Institut Pasteur, Unité de Pathogénie Microbienne Moléculaire, 75724 Paris, France; 3: INSERM, U1202, 75015 Paris, France; 4: Institut Pasteur, Unité de Pathogénie Microbienne Moléculaire, 75724 Paris, France; 5: INSERM, U1202, 75015 Paris, France; 6: Collège de France, 75005 Paris, France; 7: Oxford University, Oxford, United Kingdom
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Received 17 August 2015 Accepted 04 May 2016 Published 29 July 2016
- Correspondence: Philippe J. Sansonetti, [email protected]

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Abstract:
NOD-like receptor (NLR) proteins, as much as Toll-like receptor proteins, play a major role in modulating myeloid cells in their immune functions. There is still, however, limited knowledge on the expression and function of several of the mammalian NLR proteins in myeloid lineages. Still, the function of pyrin domain-containing NLR proteins and NLRC4/NAIP as inflammasome components that drive interleukin-1β (IL-1β) and IL-18 maturation and secretion upon pathogen stimulation is well established. NOD1, NOD2, NLRP3, and NLRC4/NAIP act as bona fide pattern recognition receptors (PRRs) that sense microbe-associated molecular patterns (MAMPs) but also react to endogenous danger-associated molecular patterns (DAMPs). Ultimately, activation of these receptors achieves macrophage activation and maturation of dendritic cells to drive antigen-specific adaptive immune responses. Upon infection, sensing of invading pathogens and likely of DAMPs that are released in response to tissue injury is a process that involves multiple PRRs in both myeloid and epithelial cells, and these act in concert to design tailored, pathogen-adapted immune responses by induction of different cytokine profiles, giving rise to appropriate lymphocyte polarization.
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Citation: Kufer T, Nigro G, Sansonetti P. 2016. Multifaceted Functions of NOD-Like Receptor Proteins in Myeloid Cells at the Intersection of Innate and Adaptive Immunity. Microbiol Spectrum 4(4):MCHD-0021-2015. doi:10.1128/microbiolspec.MCHD-0021-2015.




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Abstract:
NOD-like receptor (NLR) proteins, as much as Toll-like receptor proteins, play a major role in modulating myeloid cells in their immune functions. There is still, however, limited knowledge on the expression and function of several of the mammalian NLR proteins in myeloid lineages. Still, the function of pyrin domain-containing NLR proteins and NLRC4/NAIP as inflammasome components that drive interleukin-1β (IL-1β) and IL-18 maturation and secretion upon pathogen stimulation is well established. NOD1, NOD2, NLRP3, and NLRC4/NAIP act as bona fide pattern recognition receptors (PRRs) that sense microbe-associated molecular patterns (MAMPs) but also react to endogenous danger-associated molecular patterns (DAMPs). Ultimately, activation of these receptors achieves macrophage activation and maturation of dendritic cells to drive antigen-specific adaptive immune responses. Upon infection, sensing of invading pathogens and likely of DAMPs that are released in response to tissue injury is a process that involves multiple PRRs in both myeloid and epithelial cells, and these act in concert to design tailored, pathogen-adapted immune responses by induction of different cytokine profiles, giving rise to appropriate lymphocyte polarization.

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FIGURE 1
Different functions of NLRs in myeloid cells and progenitors. The circulating MAMPs, particularly peptidoglycan (PGN), contribute to activation and differentiation of HSCs. Stimulation by MAMPs, particularly PGN, activates innate immunity through recognition by PRR receptors, inducing their maturation and production of cytokines, such as IL-6 and TNF. NLRs also stimulate the adaptive immunity, particularly in regulating MHC expression levels and in stimulating the inflammasome.
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