NLRP12 is a neutrophil-specific, negative regulator of in vitro cell migration but does not modulate LPS- or infection-induced NF-κB or ERK signalling

Zamoshnikova, Alina; Groß, Christina; Schuster, Steffen; Chen, Kaiwen; Tacchini‐Cottier, Fabienne; Schroder, Kate

doi:10.1016/j.imbio.2015.10.001

Cited by 36 publications

(27 citation statements)

References 19 publications

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“…demonstrated an in vitro migration defect of NLPR12-deficient neutrophils to CXCL1. In contrast, Zamoshnikova et al 22. demonstrated an increase in neutrophil migration in vitro to the higher of two doses of CXCL1, but not in migration to Leishmania major .…”

Section: Discussionmentioning

confidence: 83%

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Nlrp12 mutation causes C57BL/6J strain-specific defect in neutrophil recruitment

et al. 2016

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The inbred mouse strain C57BL/6J is widely used in models of immunological and infectious diseases. Here we show that C57BL/6J mice have a defect in neutrophil recruitment to a range of inflammatory stimuli compared with the related C57BL/6N substrain. This immune perturbation is associated with a missense mutation in Nlrp12 in C57BL/6J mice. Both C57BL/6J and NLRP12-deficient mice have increased susceptibility to bacterial infection that correlates with defective neutrophil migration. C57BL/6J and NLRP12-deficient macrophages have impaired CXCL1 production and the neutrophil defect observed in C57BL/6J and NLRP12-deficient mice is rescued by restoration of macrophage NLRP12. These results demonstrate that C57BL/6J mice have a functional defect in NLRP12 and that macrophages require NLRP12 expression for effective recruitment of neutrophils to inflammatory sites.

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Section: Discussionmentioning

confidence: 83%

“…and Zamoshnikova et al . suggest there may be an additional neutrophil intrinsic role for NLRP12 (refs 21, 22). …”

Section: Discussionmentioning

confidence: 99%

Nlrp12 mutation causes C57BL/6J strain-specific defect in neutrophil recruitment

et al. 2016

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“…Additionally, COPs such as INCA, COP, and ICE-BERG, as well as caspase-12, can inhibit the processing of pro-IL-1b and activation of caspase-1 by preventing the recruitment of ASC during inflammasome assembly [118][119][120]. Furthermore, NLRP12 can inhibit NF-jB and ERK signalling in dendritic cells and macrophages [124]. A previous report suggested that cellular K ?…”

Section: Negative Regulation Of Inflammasome Assemblymentioning

confidence: 99%

Inflammasomes and its importance in viral infections

León-Juárez²,

et al. 2016

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A complex interplay between pathogen and host determines the immune response during viral infection. A set of cytosolic sensors are expressed by immune cells to detect viral infection. NOD-like receptors (NLRs) comprise a large family of intracellular pattern recognition receptors. Members of the NLR family assemble into large multiprotein complexes, termed inflammasomes, which induce downstream immune responses to specific pathogens, environmental stimuli, and host cell damage. Inflammasomes are composed of cytoplasmic sensor molecules such as NLRP3 or absent in melanoma 2 (AIM2), the adaptor protein ASC (apoptosis-associated speck-like protein containing caspase recruitment domain), and the effector protein procaspase-1. The inflammasome operates as a platform for caspase-1 activation, resulting in caspase-1-dependent proteolytic maturation and secretion of interleukin (IL)-1b and IL-18. This, in turn, activates the expression of other immune genes and facilitates lymphocyte recruitment to the site of primary infection, thereby controlling invading pathogens. Moreover, inflammasomes counter viral replication and remove infected immune cells through an inflammatory cell death, program termed as pyroptosis. As a countermeasure, viral pathogens have evolved virulence factors to antagonise inflammasome pathways. In this review, we discuss the role of inflammasomes in sensing viral infection as well as the evasion strategies that viruses have developed to evade inflammasome-dependent immune responses. This information summarises our understanding of host defence mechanisms against viruses and highlights research areas that can provide new approaches to interfere in the pathogenesis of viral diseases.

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“…Priming is also sometimes necessary to induce expression of pyrin [96], which Gavrilin and colleagues [97] showed to be lost in macrophages upon differentiation; however, monocytes and PBMCs, differentiated in the presence of additional growth factors, restore pyrin expression. Likewise, NLRP12 may have low expression in fully differentiated macrophages but is present in neutrophils [98]. For these reasons, inflammasome studies in any cell line should be carefully scrutinized for appropriate expression of relevant components.…”

Section: Heterogeneity Of Inflammasome Structure Activation and Regmentioning

confidence: 99%

Bacterial secretion systems and regulation of inflammasome activation

Ratner

Orning

Lien

2016

Journal of Leukocyte Biology

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Innate immunity is critical for host defenses against pathogens, but many bacteria display complex ways of interacting with innate immune signaling, as they may both activate and evade certain pathways. Gram-negative bacteria can exhibit specialized nanomachine secretion systems for delivery of effector proteins into mammalian cells. Bacterial types III, IV, and VI secretion systems (T3SS, T4SS, and T6SS) are known for their impact on caspase-1-activating inflammasomes, necessary for producing bioactive inflammatory cytokines IL-1β and IL-18, key participants of anti-bacterial responses. Here, we discuss how these secretion systems can mediate triggering and inhibition of inflammasome signaling. We propose that a fine balance between secretion system-mediated activation and inhibition can determine net activation of inflammasome activity and control inflammation, clearance, or spread of the infection.

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NLRP12 is a neutrophil-specific, negative regulator of in vitro cell migration but does not modulate LPS- or infection-induced NF-κB or ERK signalling

Cited by 36 publications

References 19 publications

Nlrp12 mutation causes C57BL/6J strain-specific defect in neutrophil recruitment

Nlrp12 mutation causes C57BL/6J strain-specific defect in neutrophil recruitment

Inflammasomes and its importance in viral infections

Bacterial secretion systems and regulation of inflammasome activation

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