Emerging Insights into Noncanonical Inflammasome Recognition of Microbes

Russo, Ashley J.; Behl, Bharat; Banerjee, Ishita; Rathinam, Vijay

doi:10.1016/j.jmb.2017.10.003

Cited by 45 publications

(45 citation statements)

References 69 publications

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“…For instance, E. coli and Shigella flexneri contain hexa-acylated lipid A that strongly activates caspase-11. 31 In addition, hexa-acylated lipid A derived from Yersinia pestis grown at 25 • C is detected by caspase-11, in contrast with tetraacylated lipid A from pathogen grown at 37 • C. Thus, this bacterium may exploit temperature-dependent lipid A acylation state in order to escape caspase-11 recognition during infection in the host. 27 The activation of noncanonical inflammasome prompts host immune system to control bacterial infections in different TA B L E 1 Caspase-11-dependent host protection during bacterial infections in mice accompanied by a reduction in IL-1 production, a critical cytokine for the recruitment of neutrophil in this model.…”

Section: Caspase 11: the Noncanonical Inflammasome Receptormentioning

confidence: 99%

“…Taken together, the acylation state of lipid A may be used to predict the level of noncanonical inflammasome activation. For instance, E. coli and Shigella flexneri contain hexa‐acylated lipid A that strongly activates caspase‐11 . In addition, hexa‐acylated lipid A derived from Yersinia pestis grown at 25°C is detected by caspase‐11, in contrast with tetra‐acylated lipid A from pathogen grown at 37°C.…”

Section: Caspase 11: the Noncanonical Inflammasome Receptormentioning

confidence: 99%

“…Accordingly, it was demonstrated that caspase‐11 activates a canonical NLRP3 inflammasome by promoting K + efflux, suggesting that canonical and noncanonical inflammasomes work in concert to protect the host against intracellular pathogens . In fact, GSDMD depletes intracellular K + via membrane pores formation and, hence, it is tempt to hypothesize that GSDMD activated by caspase‐11 induces K + efflux leading to NLRP3 activation …”

Section: Potassium Efflux: Connecting Caspase‐11 To Nlrp3 Activationmentioning

confidence: 99%

“…84 In fact, GSDMD depletes intracellular K + via membrane pores formation 36,106 and, hence, it is tempt to hypothesize that GSDMD activated by caspase-11 induces K + efflux leading to NLRP3 activation. 31 However, in addition to NLRP3, other inflammasomes could be…”

Section: Potassium Efflux: Connecting Caspase-11 To Nlrp3 Activationmentioning

confidence: 99%

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Guanylate-binding proteins at the crossroad of noncanonical inflammasome activation during bacterial infections

Gomes

Cerqueira

Guimarães

et al. 2019

Journal of Leukocyte Biology

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The immune system is armed with a broad range of receptors to detect and initiate the elimination of bacterial pathogens. Inflammasomes are molecular platforms that sense a diverse range of microbial insults to develop appropriate host response. In that context, noncanonical inflammasome arose as a sensor for Gram‐negative bacteria‐derived LPS leading to the control of infections. This review describes the role of caspase‐11/gasdermin‐D‐dependent immune response against Gram‐negative bacteria and presents an overview of guanylate‐binding proteins (GBPs) at the interface of noncanonical inflammasome activation. Indeed, caspase‐11 acts as a receptor for LPS and this interaction elicits caspase‐11 autoproteolysis that is required for its optimal catalytic activity. Gasdermin‐D is cleaved by activated caspase‐11 generating an N‐terminal domain that is inserted into the plasmatic membrane to form pores that induce pyroptosis, a cell death program involved in intracellular bacteria elimination. This mechanism also promotes IL‐1β release and potassium efflux that connects caspase‐11 to NLRP3 activation. Furthermore, GBPs display many features to allow LPS recognition by caspase‐11, initiating the noncanonical inflammasome response prompting the immune system to control bacterial infections. In this review, we discuss the recent findings and nuances related to this mechanism and its biological functions.

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Section: Caspase 11: the Noncanonical Inflammasome Receptormentioning

confidence: 99%

Section: Caspase 11: the Noncanonical Inflammasome Receptormentioning

confidence: 99%

Section: Potassium Efflux: Connecting Caspase‐11 To Nlrp3 Activationmentioning

confidence: 99%

Section: Potassium Efflux: Connecting Caspase-11 To Nlrp3 Activationmentioning

confidence: 99%

See 2 more Smart Citations

Guanylate-binding proteins at the crossroad of noncanonical inflammasome activation during bacterial infections

Gomes

Cerqueira

Guimarães

et al. 2019

Journal of Leukocyte Biology

View full text Add to dashboard Cite

show abstract

“…The inflammasomes are multiprotein signaling platforms that allow the activation of inflammatory caspases (caspase-1, -4, -5, -11) in response to infections and endogenous danger signals (Martinon et al, 2002;Latz et al, 2013;Broz and Dixit, 2016;Russo et al, 2018). Activation of cytosolic pattern recognition receptors that are contained within canonical inflammasomes promotes activation of caspase-1 (CASP1) and interleukin-1β (IL1β) maturation (Afonina et al, 2015).…”

Section: Introductionmentioning

confidence: 99%

Extracellular mycobacterial DNA drives disease progression by triggering Caspase-11-dependent pyroptosis of infected macrophages

Varela

Vaart

Groenewoud

et al. 2019

Preprint

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Deregulated inflammation seriously complicates life-threatening microbial infections, including tuberculosis (TB). Assembly of multiprotein inflammasome complexes is an important trigger of inflammation, but how this impacts TB progression remains unknown. Here, in vivo imaging in the zebrafish TB model revealed that mycobacterial expansion in TB granulomas is driven by inflammasomes and ensuing pyroptotic cell death of infected macrophages. We show that an Asc-independent pathway induces macrophage pyroptosis and impairs host resistance, in contrast to host-protective roles of Asc-dependent inflammasome activation and Il1b secretion. Using ASC-deficient murine macrophages, we demonstrate extracellular bacterial DNA to induce CASP11-dependent pyroptosis in a manner dependent on phagosome permeabilization. Finally, we propose that mycobacteria induce pyroptosis to escape cell-in-cell structures, formed within granulomas when living infected cells are engulfed by neighbor cells. This study provides new insight into the role of pyroptosis in TB pathogenesis and reveals a novel link between nucleic acid sensing and CASP11-dependent pyroptosis.

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What role does pyroptosis play in microbial infection?

Xia

Wang

Zheng

et al. 2018

Journal Cellular Physiology

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Pyroptosis, a type of programmed cell death mediated by gasdermin, is characterized by the swelling and rupture of cells, release of cellular contents and a strong inflammatory response, which is critical for controlling microbial infection. Pattern recognition receptors recognize the intracellular and extracellular pathogenic microbial components and stimulate the organism's inflammatory response by activating the pyroptosis signaling pathway and releasing interleukin‐1β (IL‐1β), IL‐18, and other inflammatory factors to promote pathogen clearance and prevent infection. In the process of continuous evolution, pathogens have developed multiple strategies to modulate the occurrence of pyroptosis and thus enhance their ability to induce disease; that is, the competition between host cells and pathogens controls the occurrence of pyroptosis. Competition can directly affect tissue inflammation outbreaks and even alter cell survival. Studies have shown that various bacterial infections, including Shigella flexneri, Salmonella, Listeria monocytogenes, and Legionella pneumophila, can lead to pyroptosis. Pyroptosis is associated with the occurrence and development of various diseases caused by microbial infection, and the identification of molecules related to the pyroptosis signaling pathway may provide new drug targets for the treatment of related diseases. This study reviews the molecular mechanisms of pyroptosis and the role of pyroptosis in microbial infection‐related diseases.

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Emerging Insights into Noncanonical Inflammasome Recognition of Microbes

Cited by 45 publications

References 69 publications

Guanylate-binding proteins at the crossroad of noncanonical inflammasome activation during bacterial infections

Guanylate-binding proteins at the crossroad of noncanonical inflammasome activation during bacterial infections

Extracellular mycobacterial DNA drives disease progression by triggering Caspase-11-dependent pyroptosis of infected macrophages

What role does pyroptosis play in microbial infection?

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