Recognition of RNA virus by RIG-I results in activation of CARD9 and inflammasome signaling for interleukin 1β production

Poeck, Hendrik; Bscheider, Michael; Groß, Olaf; Finger, Katrin; Roth, Susanne; Rebsamen, Manuele; Hannesschläger, Nicole; Schlee, Martin; Rothenfußer, Simon; Barchet, Winfried; Kato, Hiroki; Akira, Shizuo; Inoue, Satoshi; Endres, Stefan; Peschel, Christian; Hartmann, Gunther; Hornung, Veit; Ruland, Jürgen

doi:10.1038/ni.1824

Cited by 477 publications

(476 citation statements)

References 50 publications

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“…It has been demonstrated that rhabdovirus VSV infection in murine DCs induces RIG-1-dependent production of IL-1b and IL-18 via NF-jB, caspase-1, and caspase-3 activation; thus, RIG-1 is an inflammasome activator. Furthermore, DCs from RIG-1 knockdown mice are not able to secrete IL-1b [95]. However, the results of this study conflict with that of another report, which demonstrated that VSV is recognised by NLRP3 and not by RIG-1 [46].…”

Section: Rig-1contrasting

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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Section: Rig-1contrasting

confidence: 99%

Inflammasomes and its importance in viral infections

León-Juárez²,

et al. 2016

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“…Infl ammasome is formed with the participation of certain pattern recognition receptors and senses various danger signals (Martinon et al, 2002;Agostini et al, 2004;Mariathasan et al, 2004;Poeck et al, 2010). As a large protein complex, infl ammasome controls the activation of the proteolytic enzyme caspase-1 through the apoptosis-associated speck-like protein containing a CARD (ASC), which subsequently regulates the maturation of the pro-inflammatory cytokines interleukin-1β (IL-1β) and IL-18 (Agostini et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

Cellular localization of NLRP3 inflammasome

et al. 2013

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Infl ammasome is a large protein complex activated upon cellular stress or microbial infection, which triggers maturation of pro-inflammatory cytokines interleukin-1β and interleukin-18 through caspase-1 activation. Nod-like receptor family protein 3 (NLRP3) is the most characterized infl ammasome activated by various stimuli. However, the mechanism of its activation is unclear and its exact cellular localization is still unknown. We examined the potential co-localization of NLRP3 infl ammasome with mitochondria and seven other organelles under adenosine triphosphate, nigericin or monosodium urate stimulation in mouse peritoneal macrophages using confocal microscopy approach. Our results revealed that the activated endogenous apoptosis-associated speck-like protein containing a CARD (ASC) pyroptosome forms in the cytoplasm and co-localizes with NLRP3 and caspase-1, but not with any of the organelles screened. This study indicates that the ASC pyroptosome universally localizes within the cytoplasm rather than with any specifi c organelles.

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“…IL‐1β that is produced from activated macrophages and helper T cells is an important cytokine indicator of inflammatory response 30, 31, 32, 33. The serum samples were collected from the live mice above at predetermined points for 72 h after the IV injection of PBS, HBVC (50 µg), and ABP‐HBVC (50 µg), as described in Figure 4 A.…”

Section: Resultsmentioning

confidence: 99%

Nonimmunogenetic Viral Capsid Carrier with Cancer Targeting Activity

Lee

Yoon

et al. 2018

Advanced Science

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Although protein nanoparticles (PNPs) (e.g., viral capsids) capable of delivering a broad range of drug agents have shown distinctive advantages over synthetic nanomaterials, PNPs have an intrinsic drawback that hampers their clinical application, that is, potential immunogenicity. Here, a novel method for resolving the immunogenicity problem of PNPs, which is based on the genetic presentation of albumin‐binding peptides (ABPs) on the surface of PNP, is reported. ABPs are inserted into the surface of a viral capsid (hepatitis B virus capsid/HBVC) while preserving the native self‐assembly function of HBVC. The ABPs effectively gather human serum albumins around HBVC and significantly reduce both inflammatory response and immunoglobulin titer in live mice compared to ABP‐free HBVC. Furthermore, ABP‐conjugated HBVCs remain within tumors for a longer period than HBVCs conjugated to tumor cell receptor‐bindingpeptides, indicating that the ABPs are also capable of enhancing tumor‐targeting performance. Although applied to HBVC for proof of concept, this novel approach may provide a general platform for resolving immunogenicity and cancer‐targeting problems of PNPs, which enables the development of a variety of PNP‐based drug delivery carriers with high safety and efficacy.

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Recognition of RNA virus by RIG-I results in activation of CARD9 and inflammasome signaling for interleukin 1β production

Cited by 477 publications

References 50 publications

Inflammasomes and its importance in viral infections

Inflammasomes and its importance in viral infections

Cellular localization of NLRP3 inflammasome

Nonimmunogenetic Viral Capsid Carrier with Cancer Targeting Activity

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