The NLRP3 inflammasome in viral infection (Review)
- Authors:
- Published online on: July 6, 2023 https://doi.org/10.3892/mmr.2023.13047
- Article Number: 160
-
Copyright: © Zheng et al. This is an open access article distributed under the terms of Creative Commons Attribution License.
Abstract
Introduction
Inflammasomes are a group of multiprotein complexes that recognize both extracellular and cytoplasmic intracellular pathogens and danger signals. The assembly of the specific inflammasomes is induced by various pattern-recognition receptors (PRRs) in response to pathogen associated molecular patterns (PAMPs) or damage-associated molecular patterns (DAMPs), and results in the induction of pro-inflammatory cytokines, such as IL-1β and IL-18 (1–3). In addition, inflammasomes have been proposed to regulate other key events in inflammation and tissue repair, such as pyroptosis, a highly inflammatory form of programmed cell death. Therefore, the inflammasomes play an important role in a variety of human pathophysiological processes, including antimicrobial response and development of metabolic syndromes, cancer, autoimmune and neurodegenerative diseases (4).
To date, the following five types of PRRs have been identified: Toll-like receptors (TLRs), retinoic acid-inducible gene (RIG)-I-like receptors, C-type lectin receptors (CLRs), DNA sensors [DNA-dependent activator of IFN-regulatory factors and absent in melanoma 2], and the nucleotide-binding domain (NBD), leucine-rich repeat-containing (LRR) proteins (NLRs) (1,2). Several studies have demonstrated that the NLR family includes NLR proteins (NLRP) 1, 2, 3, 6, 12, the NLR family caspase activation and recruitment domain (CARD), and the nucleotide-binding oligomerization domain-containing protein 2 (5–9). Among them, the NLRP3 inflammasome can be activated by a wide variety of stimuli, including DAMPs, PAMPs and bacterial toxins. In the present review, the biological process of the NLRP3 inflammasome assembly, its activation, and the recent developments of its involvement in viral infection are reviewed. The findings highlight the research challenges and future directions on this scientific field.
The NLRP3 inflammasome
NLR structure
NLRs consist of three separate domains, including an N-terminal pyrin domain (PYD), a central NBD, and a C-terminal LRR (Fig. 1). The N terminal domain is a caspase recruitment domain, a CARD, or a baculovirus inhibitory repeat domain, which has been applied as a structural subclassification of the NLR family (1,10). NLRP3 (NLR family, pyrin domain containing 3), which is also called cryopyrin, NALP3, CIAS1, CLR1.1, and PYPAF1 contains a PYD, a central NACHT (nucleotide-binding domain or NAIP, CIITA, HET-E and TP1) and a C-terminal LRR, which lacks CARD and cannot recruit pro-caspase-1 in the absence of the adaptor molecule caspase recruitment domain (ASC) (1). The NACHT domain is primarily responsible for dNTPase activity and oligomerization, while the PYD domain mediates downstream signaling of homotypic protein-protein interactions. LRR has been involved in ligand-sensing and autoregulation. All three domains are involved in the protein interaction networks (7).
NLRP3 complex
In addition to the inflammasome sensor molecules, ASCs are present that connect caspase 1 in the NLRP3 inflammasome complex. ASC contains two death-fold domains: One PYD and one CARD. The interaction between the upstream inflammasome sensor molecules triggers ASC assembly via the pyrin domain into a large protein complex (11,12). ASC brings procaspase 1 into close proximity with CARD, which initiates caspase 1 self-cleavage and activation (13,14).
Caspase 1
The cysteine protease caspase 1 is a key player of the inflammatory response. Procaspase-1 recruitment to the ASC speck enables its dimerization and autoactivation (1). The CARD domain is separated by a CARD domain linker from the C-terminal catalytic domain, containing large (p20) and small (p10) subunits (15). A cleavage product, p33 (CARD + p20), is generated by the interdomain linker between p20 and p10. It is confirmed that the active species of caspase 1 in macrophages is a transient tetramer composed of p33 and p10 subunits (p33/p10). The complex removes the CARD domain by self-cleavage, leading to the release of p20/p10 and the loss of enzymatic activity (15).
IL-1β and IL-18
Active caspase 1 further processes pro-IL-1β and pro-IL-18 into their mature forms. Serine proteinases including cathepsin G, elastase, and proteinase 3 can cleave pro-IL-1β except for caspase-1 (16). Furthermore, mast cell chymase is able to cleave pro-IL-18 (17). IL-1 family cytokines are key initiators and regulators of immune responses and inflammation. IL-1β and IL-18 are significant cytokines that regulate innate and adaptive immune responses (18). IL-18 plays a major role in the induction of the Th1 response, while IL-1β contributes to the T-helper 17 response (19). In various cases, the secretion of IL-1 cytokines is closely linked to cell death. Previous studies have suggested that cell lysis is the primary release mechanism for IL-1β and IL-18 (19,20). However, recently, a common secretory pathway in the absence of cell death and cell lysis was identified, which depended on membrane permeability (20). The secretion of IL-1β and IL-18 indicates the important role of the NLRP3 inflammasome in inflammatory and infectious diseases.
Except for the cytokine release, inflammasomes also trigger pyroptosis, which is induced by inflammatory caspases (murine caspase 1 and caspase 11 or human caspase 4 and caspase 5) (21). Pyroptosis is a necrotic form of infected cell death that is different from classical apoptosis or necrosis and is characterized by cell swelling, osmotic lysis and the subsequent release of intracellular content (21). Gasdermin D is required for the induction of pyroptosis and its N-terminal fragment indicates the intrinsic pyroptosis-inducing activity (22).
Activation and regulation of the NLRP3 inflammasome
NLRP3 is known to respond to a variety of stimuli, including PAMPs, DAMPs and bacterial toxins. These PAMPs include fungi, such as Candida albicans and Saccharomyces cerevisiae (23); bacteria, including Staphylococcus aureus (S. aureus), Listeria monocytogenes and Neisseria gonorrhoeae (24–26); and viruses, such as Sendai, influenza, encephalomyocarditis viruses and adenovirus (7,27–29). In addition, several host-derived molecules, which are indicative of cellular injury or stress can also activate the NLRP3 inflammasome, including ATP released from necrotic cells, hyaluronan, glucose, monosodium urate, myeloid-β, skin irritants, imidazoquinoline compounds, silica, asbestos and alum (Fig. 2) (30). In certain cases, the inflammasome is activated by individual microbial components, such as, the α-toxin of S. aureus (24,31–33).
Canonical activation
Despite these findings, a universal activation mechanism for NLRP3 has not been reported. Extracellular ATP stimulates the P2X purinoceptor 7, triggering efflux of potassium and inducing the progressive recruitment of the membrane pore pannexin-1 (34). Under the second model, phagocytes engulf the inflammasomal activators, such as silica, monosodium urate, amyloid-β, asbestos, and alum, leading to lysosomal damage. The cytosolic release of lysosomal contents is sensed by the NLRP3 inflammasome (35,36). At last, nearly all NLRP3 agonists induce the generation of reactive oxygen species (ROS) (37–39). ROS blockade by chemical scavengers inhibit NLRP3 inflammasome activation (23,40,41). In addition, mitochondrial dysfunction induces changes in intracellular calcium levels, and the release of oxidized mitochondrial DNA can lead to NLRP3 activation (42).
ROS
Inflammasome activation can be triggered by ROS; however, the exact mechanism remains unclear. A nicotinamide adenine dinucleotide phosphate (NADPH) oxidase is involved in the process, since NLRP3 inflammasome is inhibited upon suppression of NADPH oxidase common p22 subunit (39). A recent study suggests that thioredoxin-interacting protein (TXNIP/VDUP1) is implicated in NLRP3 activation. Inflammasome activators induce the ROS-dependent TXNIP dissociation from thioredoxin. TXNIP further binds to NLRP3 and its deficiency impairs activation of the inflammasome and subsequent secretion of IL-1β (30).
Oxidized mitochondrial DNA (mtDNA)
The oxidized mtDNA from stressed mitochondria is also suggested to be the cytoplasmic activator of the NLRP3 inflammasome. A previous study conducted by Shimada et al (43) revealed that oxidized mtDNA could bind directly and activate the NLRP3 inflammasome, while macrophages lacking mtDNA severely reduced IL-1β production. In addition, ROS may also be of mitochondrial origin. However, whether ROS or oxidized mtDNA acts as a direct activator of the NLRP3 inflammasome or as its cofactor remains unknown.
Non-canonical activation
In complement with the canonical inflammasome pathway, the non-canonical pathway is mediated by murine caspase 11 and caspase 4 or caspase 5 in human cells in response to Gram-negative bacteria (44–47). Lipopolysaccharide (LPS, a component of the Gram-negative bacterial cell wall) was shown to induce the activation of caspase 11 in mice and of caspase 4 or caspase 5 in human cells, which was previously attributed to the LPS receptor TLR4 (45–47). However, recent studies have shown that host cells have developed TLR4-independent mechanisms to recognize the cytoplasmic LPS. It was found that TLR4(−/-) mice primed with the TLR3 agonist polyinosinic: Polycytidylic acid induced pro-caspase-11 expression, which could possibly explain this discrepancy (45–47). The activation of caspases 4, 5 and 11 initiates pyroptosis similarly to caspase 1, which is not responsible for cleaving pro-IL-1β or pro-IL-18 (44,48). Upon activation, these caspases also promote the assembly of the NLRP3 inflammasome (44,49,50).
In the absence of microbial stimulation, exposure to TNF-α significantly promotes ATP or silica-mediated caspase 1 activation and IL-1 secretion in macrophages and dendritic cells (51). Signals provided by NF-κB activators are not sufficient for NLRP3 activation (52). Certain studies have shown that NIMA-related kinase 7 is an important component of the NLRP3 complex, which is required for NLRP3 activation, responding to both canonical and non-canonical stimuli (53–55). The kinase spleen tyrosine kinase (SYK) is essential for NLRP3 inflammasome activation (23,41).
Positive regulation
Over the past decade, numerous studies have uncovered the role and regulation of inflammasomes during certain pathophysiological processes. The regulatory mechanisms include transcriptional, post-transcriptional regulation, post-translational modifications and regulatory proteins that target the receptors, ASC or the caspases. Furthermore, several other studies have highlighted the microbial evolution of inflammasome inhibitors.
The integration with PRRs or cytokine receptors highly influences the NLRP3 inflammasome activation and pro-IL-1β availability (51,52). In response to PRR stimulation, NLRP3 deubiquitylation, which is mediated by the K63-specific deubiquitinase BRCA1-BRCA2-containing complex subunit 3, also induces inflammasome signaling (56,57). The double-stranded RNA-dependent protein kinase R or eukaryotic translation initiation factor 2-α kinase 2 was shown to control NLRP3 inflammasome activity (58). Selective activation of the NLRP3 inflammasome was promoted by guanylate binding protein 5, in responses to pathogenic and soluble bacteria but not in response to crystalline inflammasome priming substances (59). These data suggest that small heterodimer partner is a key mediator in controlling NLRP3 inflammasome activation via mechanisms that interact with NLRP3 and maintain mitochondrial homeostasis (60).
The SYK and JNK enzymes phosphorylate the inflammasome adaptor ASC, which further contributes to the activation of caspase 1 (61). It has also been shown that SYK promotes NLRP3-dependent caspase 1 activation during infections with Candida albicans (23). The TGFβ-activated kinase 1 (TAK1 or MAP3K7)-JNK pathway was activated by ruptured lysosomes and promoted NLRP3 inflammasome activation, through the oligomerization of an adapter protein and apoptosis-associated speck-like protein including ASC (62).
Negative regulation
A number of proteins containing a CARD or a PYD have been proposed to inhibit inflammasome activity by blocking inflammasome component recruitment. Certain CARD-only proteins (COPs), such as human CARD16 (also known as COP or PSEUDO-ICE), CARD17 (also known as INCA), and CARD18 (also known as ICEBERG), are highly similar to the CARD of caspase 1 (63–65). They are suggested to suppress inflammasome activation by sequestering caspase 1. In addition, they may also regulate other signaling pathways. For instance, CARD16 and CARD18 activate receptor-interacting serine/threonine protein kinase 2 (63–65). Caspase 12 is an inhibitor of caspase 1 and its overexpression appears to abrogate caspase 1 activity (66).
PYD-only proteins (POPs), including pyrin, POP1 (PYDC1), POP2 (PYDC2) and POP3 (PYDC5), regulate inflammasome signaling at the molecular level of the PYD-PYD interaction (67–70). It was shown that binding of POP1 to ASC inhibited ASC-dependent inflammasome assembly by preventing inflammasome nucleation, and consequently reducing IL-1β release. Although mice do not have the ortholog of POP1, its transgenic expression can protect them from PAMP-triggered inflammation. Moreover, POP1 was regulated by TLR and IL-1 receptor signaling; therefore, it was proposed that POP1 would provide a regulatory feedback loop and shut down excessive inflammatory responses (70). An additional member of POPs, POP2, binds to ASC and PAN1, and inhibits the formation of cryopyrin and inflammasomes (68). In addition, it also inhibits NF-κB activation (67). The other PYD-only protein, POP3 was identified to compete with ASC for recruitment of liver regeneration-associated proteins, further reducing inflammasome activation (69).
The kinase IκB kinase-α, is involved in the negative regulation of ASC by controlling its subcellular localization in resting macrophages; however, it is not clear whether this process is associated with ASC phosphorylation (71).
Viral infection and NLRP3 inflammasome
The NLRP3 inflammasome is critical in the host anti-viral immune function. Previous studies have shown that infection from both RNA and DNA viruses can induce activation of the NLRP3 inflammasome and promote the secretion of IL-1β and IL-18 (72), such as Rift Valley fever virus, encephalomyocarditis virus (EMCV), foot-and-mouth disease virus, Mayaro virus (MAYV), hepatitis B and C viruses, Zika virus (ZIKV), H7N9 influenza A virus, Dengue virus and varicella-zoster virus (72–80). When viruses invade their hosts, the NLRP3 inflammasome can be activated by sensing viral components, including RNA, DNA and proteins. However, the mechanisms of the NLRP3 inflammasome activation during a viral infection are still debatable.
Viroporins are a group of low-molecular-weight proteins, which are important for innate immune responses, notably for the activation of the NLRP3 inflammasome, such as P7 viroporin of the hepatitis C virus, viroporin 2B of EMCV, and envelope (E) protein of severe acute respiratory syndrome coronavirus viroporin 3a (72,81–83). During the infection, viroporins can increase the cell membrane permeability, facilitate viral invasion, and cause imbalance of ion concentration levels, such as Ca2+, which in turn produces ion fluxes and promotes the activation of NLRP3 (84). Angiotensin converting enzyme 2, which is expressed in injured type II alveolar epithelial cells may lead to NLRP3 activation during coronavirus disease (COVID)-19 infection (85).
A subsequent study revealed that certain infections from RNA viruses could cause potassium efflux, which is a trigger for the activation of the NLRP3 inflammasome (86). Infection by murine hepatitis viral strain-3 can induce the quick release of ROS, which may act as a trigger for NLRP3 inflammasome activation (87). ROS also plays an important role in human immunodeficiency virus (HIV)-1 infection. HIV-1 will promote ROS production and induce inflammasome activation (88). MAYV infection can induce ROS release and potassium efflux, which subsequently triggers the activation of the NLRP3 inflammasome. Human parainfluenza virus type 3 infection can induce NLRP3 inflammasome activation via TLR2 activation and potassium efflux (89). The M2 and PB1-F2 proteins of the influenza virus can activate the NLRP3 inflammasome by regulating intracellular ionic and mitochondrial ROS production. During this process, oxidized DNA plays an important role and influenza viruses can induce oxidized DNA release (90). Influenza viral infection will also induce lysosomal damage through the lysosomal pathway, further activating NLRP3 (29). Adenoviral infections release lysosomal cathepsin B into the cytoplasm, which can cause the activation of the NLRP3 inflammasome (91).
The RNase L system can sense double-stranded RNAs and generate RNA cleavage products to activate the NLRP3 inflammasome. DExD/H-box helicase and the mitochondria-associated molecule mitochondrial antiviral-signaling protein (MAVS) participate in this process (92). MAVS can recruit NLRP3 to the mitochondria and promote the secretion of IL-1β (93). DEAD/H-box RNA helicases (DDX), DDX33 and DDX19A act as RNA sensors involved in NLRP3 inflammasome activation (94). The RNA helicase RIG-I acts as a sensor to certain RNA viruses, such as vesicular stomatitis and influenza viruses, through the NF-κB pathway to activate the NLRP3 inflammasome (29). Certain RNA viruses activate NLRP3 via the RIP1-receptor-interacting serine/threonine-protein kinase 3 (RIP3)-DRP1 pathway. The RIP1-RIP3 complex is assembled, which induces mitochondrial damage and activates NLRP3 (95).
Viruses have also evolved multiple mechanisms to evade the host immune response. Certain viral proteins can suppress the NLRP3 inflammasome-associated immune response, such as the V protein of measles virus. Sendai virus can inhibit activation of the NLRP3 inflammasome and reduce secretion of IL-1β by interacting with NLRP3 (96,97). The influenza A viral NS1 protein suppresses ASC ubiquitination and speck formation via the RIG-I/type I IFN pathway to inhibit NLRP3 inflammasome activation and reduce the production of IL-1β (98,99). The PB1-F2 protein of avian influenza A suppresses NLRP3 inflammasome-dependent IL-1β secretion by targeting the MAVS-NLRP3 interaction (100). RNA I of adenovirus VA inhibits the activation of the NLRP3 inflammasome by suppressing ASC phosphorylation and oligomerization (101). The non-structural protein NS3 of ZIKV reduces NLRP3-mediated IL-1β secretion (102). An Epstein-Barr virus microRNA (miR) can inhibit the NLRP3 inflammasome by targeting the miR-223 site (103). Enterovirus 71 can cleave NLRP3 by activation of proteases 2A and 3C, which will inhibit NLRP3 and IL-1β secretion (104). Hepatitis B viral infection can inhibit NF-κB phosphorylation and ROS production. Hepatitis B e-antigen suppresses the activation of NLRP3 and IL-1β production (105). Herpes simplex virus 1 has evolved mechanisms to block the NLRP3 activity (106).
Conclusion
The NLRP3 inflammasome has been widely studied in innate immune responses. However, the exact mechanisms of NLRP3 inflammasome activation and regulation remain unclear, notably during the viral infection process. In the present review, the current knowledge of the NLRP3 assembly process and its regulatory mechanisms during viral infection were summarized. The findings indicate that viruses can evade the host immune response by inhibiting the NLRP3 cytokine storm. As a result, it is of value to elucidate the immunological balance and the underlying mechanism of this process. Certain studies have supported the hypothesis that targeting the NLRP3 pathway can be used in the development of therapeutic strategies for viral infection, notably for COVID-19. The development of antiviral therapies requires additional studies that will explore the molecular pathogenesis of NLRP3 inflammasome activation in response to viral infection.
Acknowledgements
Not applicable.
Funding
The present study was supported by the Young Scientists Fund of the National Natural Science Foundation of China (grant no. 81801992), and the Medical and Health Science and Technology Project of Zhejiang (grant nos. 2018256428 and 2022514972).
Availability of data and materials
Not applicable.
Authors' contributions
QZ and HC conceived and designed the study. QZ, CH and QL collected data. QZ, CH and QL prepared the draft of the manuscript. HC reviewed and edited the manuscript. All authors read and approved the final version of the manuscript. Data authentication is not applicable.
Ethics approval and consent to participate
Not applicable.
Patient consent for publication
Not applicable.
Competing interests
The authors declare that they have no competing interests.
References
|
Schroder K and Tschopp J: The inflammasomes. Cell. 140:821–832. 2010. View Article : Google Scholar : PubMed/NCBI | |
|
Fusco R, Siracusa R, Genovese T, Cuzzocrea S and Di Paola R: Focus on the role of NLRP3 inflammasome in diseases. Int J Mol Sci. 21:42232020. View Article : Google Scholar : PubMed/NCBI | |
|
Farag NS, Breitinger U, Breitinger HG and El Azizi MA: Viroporins and inflammasomes: A key to understand virus-induced inflammation. Int J Biochem Cell Biol. 122:1057382020. View Article : Google Scholar : PubMed/NCBI | |
|
Kelley N, Jeltema D, Duan Y and He Y: The NLRP3 inflammasome: An overview of mechanisms of activation and regulation. Int J Mol Sci. 20:33282019. View Article : Google Scholar : PubMed/NCBI | |
|
Barnett KC, Li S, Liang K and Ting JPY: A 360° view of the inflammasome: Mechanisms of activation, cell death, and diseases. Cell. 186:2288–2312. 2023. View Article : Google Scholar : PubMed/NCBI | |
|
Chou WC, Jha S, Linhoff MW and Ting JPY: The NLR gene family: from discovery to present day. Nat Rev Immunol. Mar 27–2023.(Epub ahead of print). View Article : Google Scholar | |
|
Chai R, Li Y, Shui L, Ni L and Zhang A: The role of pyroptosis in inflammatory diseases. Front Cell Dev Biol. 11:11732352023. View Article : Google Scholar : PubMed/NCBI | |
|
Zhan X, Li Q, Xu G, Xiao X and Bai Z: The mechanism of NLRP3 inflammasome activation and its pharmacological inhibitors. Front Immunol. 13:11099382023. View Article : Google Scholar : PubMed/NCBI | |
|
Agostini L, Martinon F, Burns K, McDermott MF, Hawkins PN and Tschopp J: NALP3 forms an IL-1beta-processing inflammasome with increased activity in Muckle-Wells autoinflammatory disorder. Immunity. 20:319–325. 2004. View Article : Google Scholar : PubMed/NCBI | |
|
Song JY, Park YM and Choi SY: Type 2 human papillomavirus E7 attenuates E-cadherin expression in human keratinocytes. J Microbiol. 59:616–625. 2021. View Article : Google Scholar : PubMed/NCBI | |
|
Yu TG, Cha JS, Kim G, Sohn YK, Yoo Y, Kim U, Song JJ, Cho HS and Kim HS: Oligomeric states of ASC specks regulate inflammatory responses by inflammasome in the extracellular space. Cell Death Discov. 9:1422023. View Article : Google Scholar : PubMed/NCBI | |
|
Proell M, Gerlic M, Mace PD, Reed JC and Riedl SJ: The CARD plays a critical role in ASC foci formation and inflammasome signalling. Biochem J. 449:613–621. 2013. View Article : Google Scholar : PubMed/NCBI | |
|
Guo Y, Gu D, Huang T, Li A, Zhou Y, Kang X, Meng C, Xiong D, Song L, Jiao X and Pan Z: Salmonella Enteritidis T1SS protein SiiD inhibits NLRP3 inflammasome activation via repressing the mtROS-ASC dependent pathway. PLoS Pathog. 19:e10113812023. View Article : Google Scholar : PubMed/NCBI | |
|
de Souza JG, Starobinas N and Ibañez OCM: Unknown/enigmatic functions of extracellular ASC. Immunology. 163:377–388. 2021. View Article : Google Scholar : PubMed/NCBI | |
|
Ross C, Chan AH, von Pein JB, Maddugoda MP, Boucher D and Schroder K: Inflammatory caspases: Toward a unified model for caspase activation by inflammasomes. Annu Rev Immunol. 40:249–269. 2022. View Article : Google Scholar : PubMed/NCBI | |
|
Triantafilou K: Enigmatic inflammasomes. Immunology. 162:249–251. 2021. View Article : Google Scholar : PubMed/NCBI | |
|
Wang C, Yang T, Xiao J, Xu C, Alippe Y, Sun K, Kanneganti TD, Monahan JB, Abu-Amer Y, Lieberman J and Mbalaviele G: NLRP3 inflammasome activation triggers gasdermin D-independent inflammation. Sci Immunol. 6:eabj38592021. View Article : Google Scholar : PubMed/NCBI | |
|
Zhen Y and Zhang H: NLRP3 inflammasome and inflammatory bowel disease. Front Immunol. 10:2762019. View Article : Google Scholar : PubMed/NCBI | |
|
Voet S, Srinivasan S, Lamkanfi M and van Loo G: Inflammasomes in neuroinflammatory and neurodegenerative diseases. EMBO Mol Med. 11:e102482019. View Article : Google Scholar : PubMed/NCBI | |
|
Tapia VS, Daniels MJD, Palazón-Riquelme P, Dewhurst M, Luheshi NM, Rivers-Auty J, Green J, Redondo-Castro E, Kaldis P, Lopez-Castejon G and Brough D: The three cytokines IL-1β, IL-18, and IL-1α share related but distinct secretory routes. J Biol Chem. 294:8325–8335. 2019. View Article : Google Scholar : PubMed/NCBI | |
|
Long J, Sun Y, Liu S, Yang S, Chen C, Zhang Z, Chu S, Yang Y, Pei G, Lin M, et al: Targeting pyroptosis as a preventive and therapeutic approach for stroke. Cell Death Discov. 9:1552023. View Article : Google Scholar : PubMed/NCBI | |
|
Devant P and Kagan JC: Molecular mechanisms of gasdermin D pore-forming activity. Nat Immunol. Jun 5–2023.(Epub ahead of print). View Article : Google Scholar : PubMed/NCBI | |
|
Li Y, Song W, Tong Y, Zhang X, Zhao J, Gao X, Yong J and Wang H: Isoliquiritin ameliorates depression by suppressing NLRP3-mediated pyroptosis via miRNA-27a/SYK/NF-κB axis. J Neuroinflammation. 18:12021. View Article : Google Scholar : PubMed/NCBI | |
|
Mariathasan S, Weiss DS, Newton K, McBride J, O'Rourke K, Roose-Girma M, Lee WP, Weinrauch Y, Monack DM and Dixit VM: Cryopyrin activates the inflammasome in response to toxins and ATP. Nature. 440:228–232. 2006. View Article : Google Scholar : PubMed/NCBI | |
|
Guo Y, Li L, Xu T, Guo X, Wang C, Li Y, Yang Y, Yang D, Sun B, Zhao X, et al: HUWE1 mediates inflammasome activation and promotes host defense against bacterial infection. J Clin Invest. 130:6301–6316. 2020. View Article : Google Scholar : PubMed/NCBI | |
|
Zhang S, Zhang Y, Gan L, Wei F, Chai B, A Aljaafreh AAH, Liu X, Duan X, Jiang J, Wang X, et al: Progesterone suppresses Neisseria gonorrhoeae-induced inflammation through inhibition of NLRP3 inflammasome pathway in THP-1 cells and murine models. Front Microbiol. 12:5700932021. View Article : Google Scholar : PubMed/NCBI | |
|
Muruve DA, Pétrilli V, Zaiss AK, White LR, Clark SA, Ross PJ, Parks RJ and Tschopp J: The inflammasome recognizes cytosolic microbial and host DNA and triggers an innate immune response. Nature. 452:103–107. 2008. View Article : Google Scholar : PubMed/NCBI | |
|
Allen IC, Scull MA, Moore CB, Holl EK, McElvania-TeKippe E, Taxman DJ, Guthrie EH, Pickles RJ and Ting JP: The NLRP3 inflammasome mediates in vivo innate immunity to influenza A virus through recognition of viral RNA. Immunity. 30:556–565. 2009. View Article : Google Scholar : PubMed/NCBI | |
|
Poeck H, Bscheider M, Gross O, Finger K, Roth S, Rebsamen M, Hannesschläger N, Schlee M, Rothenfusser S, Barchet W, et al: Recognition of RNA virus by RIG-I results in activation of CARD9 and inflammasome signaling for interleukin 1 beta production. Nat Immunol. 11:63–69. 2010. View Article : Google Scholar : PubMed/NCBI | |
|
Zhou R, Tardivel A, Thorens B, Choi I and Tschopp J: Thioredoxin-interacting protein links oxidative stress to inflammasome activation. Nat Immunol. 11:136–140. 2010. View Article : Google Scholar : PubMed/NCBI | |
|
Walev I, Reske K, Palmer M, Valeva A and Bhakdi S: Potassium-inhibited processing of IL-1 beta in human monocytes. EMBO J. 14:1607–1614. 1995. View Article : Google Scholar : PubMed/NCBI | |
|
Gurcel L, Abrami L, Girardin S, Tschopp J and van der Goot FG: Caspase-1 activation of lipid metabolic pathways in response to bacterial pore-forming toxins promotes cell survival. Cell. 126:1135–1145. 2006. View Article : Google Scholar : PubMed/NCBI | |
|
Liu R, Liu Y, Liu C, Gao A, Wang L, Tang H, Wu Q, Wang X, Tian D, Qi Z and Shen Y: NEK7-mediated activation of NLRP3 inflammasome is coordinated by potassium Efflux/Syk/JNK signaling during Staphylococcus aureus infection. Front Immunol. 12:7473702021. View Article : Google Scholar : PubMed/NCBI | |
|
Pelegrin P: P2X7 receptor and the NLRP3 inflammasome: Partners in crime. Biochem Pharmacol. 187:1143852021. View Article : Google Scholar : PubMed/NCBI | |
|
Halle A, Hornung V, Petzold GC, Stewart CR, Monks BG, Reinheckel T, Fitzgerald KA, Latz E, Moore KJ and Golenbock DT: The NALP3 inflammasome is involved in the innate immune response to amyloid-beta. Nat Immunol. 9:857–865. 2008. View Article : Google Scholar : PubMed/NCBI | |
|
Hornung V, Bauernfeind F, Halle A, Samstad EO, Kono H, Rock KL, Fitzgerald KA and Latz E: Silica crystals and aluminum salts activate the NALP3 inflammasome through phagosomal destabilization. Nat Immunol. 9:847–856. 2008. View Article : Google Scholar : PubMed/NCBI | |
|
Cruz CM, Rinna A, Forman HJ, Ventura ALM, Persechini PM and Ojcius DM: ATP activates a reactive oxygen species-dependent oxidative stress response and secretion of proinflammatory cytokines in macrophages. J Biol Chem. 282:2871–2879. 2007. View Article : Google Scholar : PubMed/NCBI | |
|
Cassel SL, Eisenbarth SC, Iyer SS, Sadler JJ, Colegio OR, Tephly LA, Carter AB, Rothman PB, Flavell RA and Sutterwala FS: The Nalp3 inflammasome is essential for the development of silicosis. Proc Natl Acad Sci USA. 105:9035–9040. 2008. View Article : Google Scholar : PubMed/NCBI | |
|
Dostert C, Pétrilli V, Van Bruggen R, Steele C, Mossman BT and Tschopp J: Innate immune activation through Nalp3 inflammasome sensing of asbestos and silica. Science. 320:674–677. 2008. View Article : Google Scholar : PubMed/NCBI | |
|
Koumangoye R: The role of Cl− and K+ efflux in NLRP3 inflammasome and innate immune response activation. Am J Physiol Cell Physiol. 322:C645–C652. 2022. View Article : Google Scholar : PubMed/NCBI | |
|
Shio MT, Eisenbarth SC, Savaria M, Vinet AF, Bellemare MJ, Harder KW, Sutterwala FS, Bohle DS, Descoteaux A, Flavell RA and Olivier M: Malarial hemozoin activates the NLRP3 inflammasome through Lyn and Syk kinases. PLoS Pathog. 5:e10005592009. View Article : Google Scholar : PubMed/NCBI | |
|
Latz E, Xiao TS and Stutz A: Activation and regulation of the inflammasomes. Nat Rev Immunol. 13:397–411. 2013. View Article : Google Scholar : PubMed/NCBI | |
|
Shimada K, Crother TR, Karlin J, Dagvadorj J, Chiba N, Chen S, Ramanujan VK, Wolf AJ, Vergnes L, Ojcius DM, et al: Oxidized mitochondrial DNA activates the NLRP3 inflammasome during apoptosis. Immunity. 36:401–414. 2012. View Article : Google Scholar : PubMed/NCBI | |
|
Cabral A, Cabral JE, Wang A, Zhang Y, Liang H, Nikbakht D, Corona L, Hoffman HM and McNulty R: Differential binding of NLRP3 to non-oxidized and Ox-mtDNA mediates NLRP3 inflammasome activation. Commun Biol. 6:5782023. View Article : Google Scholar : PubMed/NCBI | |
|
Zamyatina A and Heine H: Lipopolysaccharide recognition in the crossroads of TLR4 and caspase-4/11 mediated inflammatory pathways. Front Immunol. 11:5851462020. View Article : Google Scholar : PubMed/NCBI | |
|
Rathinam VAK, Zhao Y and Shao F: Innate immunity to intracellular LPS. Nat Immunol. 20:527–533. 2019. View Article : Google Scholar : PubMed/NCBI | |
|
Downs KP, Nguyen H, Dorfleutner A and Stehlik C: An overview of the non-canonical inflammasome. Mol Aspects Med. 76:1009242020. View Article : Google Scholar : PubMed/NCBI | |
|
Naseer N, Zhang J, Bauer R, Constant DA, Nice TJ, Brodsky IE, Rauch I and Shin S: Salmonella enterica serovar typhimurium induces NAIP/NLRC4- and NLRP3/ASC-independent, caspase-4-dependent inflammasome activation in human intestinal epithelial cells. Infect Immun. 90:e00663212022. View Article : Google Scholar : PubMed/NCBI | |
|
Baker PJ, Boucher D, Bierschenk D, Tebartz C, Whitney PG, D'Silva DB, Tanzer MC, Monteleone M, Robertson AA, Cooper MA, et al: NLRP3 inflammasome activation downstream of cytoplasmic LPS recognition by both caspase-4 and caspase-5. Eur J Immunol. 45:2918–2926. 2015. View Article : Google Scholar : PubMed/NCBI | |
|
Schmid-Burgk JL, Gaidt MM, Schmidt T, Ebert TS, Bartok E and Hornung V: Caspase-4 mediates non-canonical activation of the NLRP3 inflammasome in human myeloid cells. Eur J Immunol. 45:2911–2917. 2015. View Article : Google Scholar : PubMed/NCBI | |
|
Franchi L, Eigenbrod T and Núñez G: Cutting edge: TNF-alpha mediates sensitization to ATP and silica via the NLRP3 inflammasome in the absence of microbial stimulation. J Immunol. 183:792–796. 2009. View Article : Google Scholar : PubMed/NCBI | |
|
Bauernfeind FG, Horvath G, Stutz A, Alnemri ES, MacDonald K, Speert D, Fernandes-Alnemri T, Wu J, Monks BG, Fitzgerald KA, et al: Cutting edge: NF-kappaB activating pattern recognition and cytokine receptors license NLRP3 inflammasome activation by regulating NLRP3 expression. J Immunol. 183:787–791. 2009. View Article : Google Scholar : PubMed/NCBI | |
|
Chen X, Liu G, Yuan Y, Wu G, Wang S and Yuan L: NEK7 interacts with NLRP3 to modulate the pyroptosis in inflammatory bowel disease via NF-κB signaling. Cell Death Dis. 10:9062019. View Article : Google Scholar : PubMed/NCBI | |
|
Liu G, Chen X, Wang Q and Yuan L: NEK7: A potential therapy target for NLRP3-related diseases. Biosci Trends. 14:74–82. 2020. View Article : Google Scholar : PubMed/NCBI | |
|
Sharif H, Wang L, Wang WL, Magupalli VG, Andreeva L, Qiao Q, Hauenstein AV, Wu Z, Núñez G, Mao Y and Wu H: Structural mechanism for NEK7-licensed activation of NLRP3 inflammasome. Nature. 570:338–343. 2019. View Article : Google Scholar : PubMed/NCBI | |
|
Juliana C, Fernandes-Alnemri T, Kang S, Farias A, Qin F and Alnemri ES: Non-transcriptional priming and deubiquitination regulate NLRP3 inflammasome activation. J Biol Chem. 287:36617–36622. 2012. View Article : Google Scholar : PubMed/NCBI | |
|
Py BF, Kim MS, Vakifahmetoglu-Norberg H and Yuan J: Deubiquitination of NLRP3 by BRCC3 critically regulates inflammasome activity. Mol Cell. 49:331–338. 2013. View Article : Google Scholar : PubMed/NCBI | |
|
Lu B, Nakamura T, Inouye K, Li J, Tang Y, Lundbäck P, Valdes-Ferrer SI, Olofsson PS, Kalb T, Roth J, et al: Novel role of PKR in inflammasome activation and HMGB1 release. Nature. 488:670–674. 2012. View Article : Google Scholar : PubMed/NCBI | |
|
Li Y, Lin X, Wang W, Wang W, Cheng S, Huang Y, Zou Y, Ke J and Zhu L: The proinflammatory role of guanylate-binding protein 5 in inflammatory bowel diseases. Front Microbiol. 13:9269152022. View Article : Google Scholar : PubMed/NCBI | |
|
Yang CS, Kim JJ, Kim TS, Lee PY, Kim SY, Lee HM, Shin DM, Nguyen LT, Lee MS, Jin HS, et al: Small heterodimer partner interacts with NLRP3 and negatively regulates activation of the NLRP3 inflammasome. Nat Commun. 6:61152015. View Article : Google Scholar : PubMed/NCBI | |
|
Hara H, Tsuchiya K, Kawamura I, Fang R, Hernandez-Cuellar E, Shen Y, Mizuguchi J, Schweighoffer E, Tybulewicz V and Mitsuyama M: Phosphorylation of the adaptor ASC acts as a molecular switch that controls the formation of speck-like aggregates and inflammasome activity. Nat Immunol. 14:1247–1255. 2013. View Article : Google Scholar : PubMed/NCBI | |
|
Okada M, Matsuzawa A, Yoshimura A and Ichijo H: The lysosome rupture-activated TAK1-JNK pathway regulates NLRP3 inflammasome activation. J Biol Chem. 289:32926–32936. 2014. View Article : Google Scholar : PubMed/NCBI | |
|
Humke EW, Shriver SK, Starovasnik MA, Fairbrother WJ and Dixit VM: ICEBERG: A novel inhibitor of interleukin-1beta generation. Cell. 103:99–111. 2000. View Article : Google Scholar : PubMed/NCBI | |
|
Druilhe A, Srinivasula SM, Razmara M, Ahmad M and Alnemri ES: Regulation of IL-1beta generation by Pseudo-ICE and ICEBERG, two dominant negative caspase recruitment domain proteins. Cell Death Differ. 8:649–657. 2001. View Article : Google Scholar : PubMed/NCBI | |
|
Lamkanfi M, Denecker G, Kalai M, D'hondt K, Meeus A, Declercq W, Saelens X and Vandenabeele P: INCA, a novel human caspase recruitment domain protein that inhibits interleukin-1beta generation. J Biol Chem. 279:51729–51738. 2004. View Article : Google Scholar : PubMed/NCBI | |
|
Saleh M, Mathison JC, Wolinski MK, Bensinger SJ, Fitzgerald P, Droin N, Ulevitch RJ, Green DR and Nicholson DW: Enhanced bacterial clearance and sepsis resistance in caspase-12-deficient mice. Nature. 440:1064–1068. 2006. View Article : Google Scholar : PubMed/NCBI | |
|
Bedoya F, Sandler LL and Harton JA: Pyrin-only protein 2 modulates NF-kappaB and disrupts ASC:CLR interactions. J Immunol. 178:3837–3845. 2007. View Article : Google Scholar : PubMed/NCBI | |
|
Dorfleutner A, Bryan NB, Talbott SJ, Funya KN, Rellick SL, Reed JC, Shi X, Rojanasakul Y, Flynn DC and Stehlik C: Cellular pyrin domain-only protein 2 is a candidate regulator of inflammasome activation. Infect Immun. 75:1484–1492. 2007. View Article : Google Scholar : PubMed/NCBI | |
|
Khare S, Ratsimandresy RA, de Almeida L, Cuda CM, Rellick SL, Misharin AV, Wallin MC, Gangopadhyay A, Forte E, Gottwein E, et al: The PYRIN domain-only protein POP3 inhibits ALR inflammasomes and regulates responses to infection with DNA viruses. Nat Immunol. 15:343–353. 2014. View Article : Google Scholar : PubMed/NCBI | |
|
de Almeida L, Khare S, Misharin AV, Patel R, Ratsimandresy RA, Wallin MC, Perlman H, Greaves DR, Hoffman HM, Dorfleutner A and Stehlik C: The PYRIN domain-only protein POP1 inhibits inflammasome assembly and ameliorates inflammatory disease. Immunity. 43:264–276. 2015. View Article : Google Scholar : PubMed/NCBI | |
|
Martin BN, Wang C, Willette-Brown J, Herjan T, Gulen MF, Zhou H, Bulek K, Franchi L, Sato T, Alnemri ES, et al: IKKα negatively regulates ASC-dependent inflammasome activation. Nat Commun. 5:49772014. View Article : Google Scholar : PubMed/NCBI | |
|
Ito M, Yanagi Y and Ichinohe T: Encephalomyocarditis virus viroporin 2B activates NLRP3 inflammasome. PLoS Pathog. 8:e10028572012. View Article : Google Scholar : PubMed/NCBI | |
|
Ermler ME, Traylor Z, Patel K, Schattgen SA, Vanaja SK, Fitzgerald KA and Hise AG: Rift Valley fever virus infection induces activation of the NLRP3 inflammasome. Virology. 449:174–180. 2014. View Article : Google Scholar : PubMed/NCBI | |
|
Pinar A, Dowling JK, Bitto NJ, Robertson AA, Latz E, Stewart CR, Drummond GR, Cooper MA, McAuley JL, Tate MD and Mansell A: PB1-F2 peptide derived from avian influenza A virus H7N9 induces inflammation via activation of the NLRP3 inflammasome. J Biol Chem. 292:826–836. 2017. View Article : Google Scholar : PubMed/NCBI | |
|
Xu J, Zhou Z, Zheng Y, Yang S, Huang K and Li H: Roles of inflammasomes in viral myocarditis. Front Cell Infect Microbiol. 13:11499112023. View Article : Google Scholar : PubMed/NCBI | |
|
Wang W, Li G, De Wu, Luo Z, Pan P, Tian M, Wang Y, Xiao F, Li A, Wu K, et al: Zika virus infection induces host inflammatory responses by facilitating NLRP3 inflammasome assembly and interleukin-1β secretion. Nat Commun. 9:1062018. View Article : Google Scholar : PubMed/NCBI | |
|
de Castro-Jorge LA, de Carvalho RVH, Klein TM, Hiroki CH, Lopes AH, Guimarães RM, Fumagalli MJ, Floriano VG, Agostinho MR, Slhessarenko RD, et al: The NLRP3 inflammasome is involved with the pathogenesis of Mayaro virus. PLoS Pathog. 15:e10079342019. View Article : Google Scholar : PubMed/NCBI | |
|
Shrivastava G, Visoso-Carvajal G, Garcia-Cordero J, Leon-Juarez M, Chavez-Munguia B, Lopez T, Nava P, Villegas-Sepulveda N and Cedillo-Barron L: Dengue virus serotype 2 and its non-structural proteins 2A and 2B activate NLRP3 inflammasome. Front Immunol. 11:3522020. View Article : Google Scholar : PubMed/NCBI | |
|
Xie WH, Ding J, Xie XX, Yang XH, Wu XF, Chen ZX, Guo QL, Gao WY, Wang XZ and Li D: Hepatitis B virus X protein promotes liver cell pyroptosis under oxidative stress through NLRP3 inflammasome activation. Inflamm Res. 69:683–696. 2020. View Article : Google Scholar : PubMed/NCBI | |
|
Zhi X, Zhang Y, Sun S, Zhang Z, Dong H, Luo X, Wei Y, Lu Z, Dou Y, Wu R, et al: NLRP3 inflammasome activation by Foot-and-mouth disease virus infection mainly induced by viral RNA and non-structural protein 2B. RNA Biol. 17:335–349. 2020. View Article : Google Scholar : PubMed/NCBI | |
|
Zhao C and Zhao W: NLRP3 inflammasome-A key player in antiviral responses. Front Immunol. 11:2112020. View Article : Google Scholar : PubMed/NCBI | |
|
Harris J and Borg NA: The multifaceted roles of NLRP3-modulating proteins in virus infection. Front Immunol. 13:9874532022. View Article : Google Scholar : PubMed/NCBI | |
|
Chen IY, Moriyama M, Chang MF and Ichinohe T: Severe acute respiratory syndrome coronavirus viroporin 3a activates the NLRP3 inflammasome. Front Microbiol. 10:502019. View Article : Google Scholar : PubMed/NCBI | |
|
Guo HC, Jin Y, Zhi XY, Yan D and Sun SQ: NLRP3 inflammasome activation by viroporins of animal viruses. Viruses. 7:3380–3391. 2015. View Article : Google Scholar : PubMed/NCBI | |
|
Freeman TL and Swartz TH: Targeting the NLRP3 inflammasome in Severe COVID-19. Front Immunol. 11:15182020. View Article : Google Scholar : PubMed/NCBI | |
|
da Costa LS, Outlioua A, Anginot A, Akarid K and Arnoult D: RNA viruses promote activation of the NLRP3 inflammasome through cytopathogenic effect-induced potassium efflux. Cell Death Dis. 10:3462019. View Article : Google Scholar : PubMed/NCBI | |
|
Guo S, Yang C, Diao B, Huang X, Jin M, Chen L, Yan W, Ning Q, Zheng L, Wu Y and Chen Y: The NLRP3 inflammasome and IL-1β accelerate immunologically mediated pathology in experimental viral fulminant hepatitis. PLoS Pathog. 11:e10051552015. View Article : Google Scholar : PubMed/NCBI | |
|
Guo H, Gao J, Taxman DJ, Ting JPY and Su L: HIV-1 infection induces interleukin-1β production via TLR8 protein-dependent and NLRP3 inflammasome mechanisms in human monocytes. J Biol Chem. 289:21716–21726. 2014. View Article : Google Scholar : PubMed/NCBI | |
|
Shil NK, Pokharel SM, Banerjee AK, Hoffman M and Bose S: Inflammasome antagonism by human parainfluenza virus type 3 c protein. J Virol. 92:e01776–17. 2018. View Article : Google Scholar : PubMed/NCBI | |
|
Moriyama M, Nagai M, Maruzuru Y, Koshiba T, Kawaguchi Y and Ichinohe T: Influenza virus-induced oxidized DNA activates inflammasomes. iScience. 23:1012702020. View Article : Google Scholar : PubMed/NCBI | |
|
Barlan AU, Danthi P and Wiethoff CM: Lysosomal localization and mechanism of membrane penetration influence nonenveloped virus activation of the NLRP3 inflammasome. Virology. 412:306–314. 2011. View Article : Google Scholar : PubMed/NCBI | |
|
Chakrabarti A, Banerjee S, Franchi L, Loo YM, Gale M Jr, Núñez G and Silverman RH: RNase L activates the NLRP3 inflammasome during viral infections. Cell Host Microbe. 17:466–477. 2015. View Article : Google Scholar : PubMed/NCBI | |
|
Subramanian N, Natarajan K, Clatworthy MR, Wang Z and Germain RN: The adaptor MAVS promotes NLRP3 mitochondrial localization and inflammasome activation. Cell. 153:348–361. 2013. View Article : Google Scholar : PubMed/NCBI | |
|
Li J, Hu L, Liu Y, Huang L, Mu Y, Cai X and Weng C: DDX19A senses viral RNA and mediates NLRP3-dependent inflammasome activation. J Immunol. 195:5732–5749. 2015. View Article : Google Scholar : PubMed/NCBI | |
|
Wang X, Jiang W, Yan Y, Gong T, Han J, Tian Z and Zhou R: RNA viruses promote activation of the NLRP3 inflammasome through a RIP1-RIP3-DRP1 signaling pathway. Nat Immunol. 15:1126–1133. 2014. View Article : Google Scholar : PubMed/NCBI | |
|
Komune N, Ichinohe T, Ito M and Yanagi Y: Measles virus V protein inhibits NLRP3 inflammasome-mediated interleukin-1β secretion. J Virol. 85:13019–13026. 2011. View Article : Google Scholar : PubMed/NCBI | |
|
Komatsu T, Tanaka Y, Kitagawa Y, Koide N, Naiki Y, Morita N, Gotoh B and Yokochi T: Sendai virus V protein inhibits the secretion of interleukin-1β by preventing NLRP3 inflammasome assembly. J Virol. 92:e00842–18. 2018. View Article : Google Scholar : PubMed/NCBI | |
|
Pothlichet J, Meunier I, Davis BK, Ting JP, Skamene E, von Messling V and Vidal SM: Type I IFN triggers RIG-I/TLR3/NLRP3-dependent inflammasome activation in influenza A virus infected cells. PLoS Pathog. 9:e10032562013. View Article : Google Scholar : PubMed/NCBI | |
|
Park HS, Liu G, Thulasi Raman SN, Landreth SL, Liu Q and Zhou Y: NS1 protein of 2009 pandemic influenza A virus inhibits porcine NLRP3 inflammasome-mediated interleukin-1 beta production by suppressing ASC ubiquitination. J Virol. 92:e00022–18. 2018. View Article : Google Scholar : PubMed/NCBI | |
|
Cheung PHH, Ye ZW, Lee TWT, Chen H, Chan CP and Jin DY: PB1-F2 protein of highly pathogenic influenza A (H7N9) virus selectively suppresses RNA-induced NLRP3 inflammasome activation through inhibition of MAVS-NLRP3 interaction. J Leukoc Biol. 108:1655–1663. 2020. View Article : Google Scholar : PubMed/NCBI | |
|
Darweesh M, Kamel W, Gavrilin MA, Akusjärvi G and Svensson C: Adenovirus VA RNAI blocks ASC oligomerization and inhibits NLRP3 inflammasome activation. Front Immunol. 10:27912019. View Article : Google Scholar : PubMed/NCBI | |
|
Gim E, Shim DW, Hwang I, Shin OS and Yu JW: Zika virus impairs host NLRP3-mediated inflammasome activation in an NS3-dependent manner. Immune Netw. 19:e402019. View Article : Google Scholar : PubMed/NCBI | |
|
Haneklaus M, Gerlic M, Kurowska-Stolarska M, Rainey AA, Pich D, McInnes IB, Hammerschmidt W, O'Neill LA and Masters SL: Cutting edge: miR-223 and EBV miR-BART15 regulate the NLRP3 inflammasome and IL-1β production. J Immunol. 189:3795–3799. 2012. View Article : Google Scholar : PubMed/NCBI | |
|
Wang H, Lei X, Xiao X, Yang C, Lu W, Huang Z, Leng Q, Jin Q, He B, Meng G and Wang J: Reciprocal regulation between enterovirus 71 and the NLRP3 inflammasome. Cell Rep. 12:42–48. 2015. View Article : Google Scholar : PubMed/NCBI | |
|
Yu X, Lan P, Hou X, Han Q, Lu N, Li T, Jiao C, Zhang J, Zhang C and Tian Z: HBV inhibits LPS-induced NLRP3 inflammasome activation and IL-1β production via suppressing the NF-κB pathway and ROS production. J Hepatol. 66:693–702. 2017. View Article : Google Scholar : PubMed/NCBI | |
|
Johnson KE, Chikoti L and Chandran B: Herpes simplex virus 1 infection induces activation and subsequent inhibition of the IFI16 and NLRP3 inflammasomes. J Virol. 87:5005–5018. 2013. View Article : Google Scholar : PubMed/NCBI |
