Edwardsiella piscicida virulence effector trxlp promotes the NLRC4 inflammasome activation during infection

Xu, Wenting; Gu, Zhaoyan; Zhang, Lingzhi; Zhang, Yuanxing; Liu, Qin; Yang, Dahai

doi:10.1016/j.micpath.2018.08.016

Cited by 10 publications

(4 citation statements)

References 34 publications

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“…NLRC4 and Casp4 are primarily activated by specific PAMP ligands presented by microbial organisms [1,32]. Previous studies have demonstrated that E. tarda components or secreted particles can cause pyroptosis in murine macrophages and human epithelial cells [33][34][35][36][37]. In this study, we found that in the infection model of THP-1 derived human macrophages, which express multiple inflammasomes, E. tarda induced pyroptosis in a manner that depended on NLRC4, NLRP3, ASC, Casp1, and Casp4.…”

Section: Discussionmentioning

confidence: 52%

T3SS translocon induces pyroptosis by direct interaction with NLRC4/NAIP inflammasome

Zhao,

Zhu,

et al. 2024

Preprint

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Type III secretion system (T3SS) is a virulence apparatus existing in many bacterial pathogens. Structurally, T3SS consists of the base, needle, tip, and translocon. The NLRC4 inflammasome is the major receptor for T3SS needle and basal rod proteins. Whether other T3SS components are recognized by NLRC4 is unclear. In this study, usingEdwardsiella tardaas a model intracellular pathogen, we examined T3SS−inflammasome interaction and its effect on cell death.E. tardainduced pyroptosis in a manner that required the bacterial translocon and the host inflammasome proteins of NLRC4, NLRP3, ASC, and caspase 1/4. The translocon protein EseB triggered NLRC4/NAIP-mediated pyroptosis by binding NAIP via its C-terminal region, particularly the terminal 6 residues (T6R). EseB homologs exist widely in T3SS-positive bacteria and share high identities in T6R. LikeE. tardaEseB, all of the representatives of the EseB homologs exhibited T6R-dependent NLRC4 activation ability. Together these results revealed the function and molecular mechanism of EseB to induce host cell pyroptosis and suggested a highly conserved inflammasome-activation mechanism of T3SS translocon in bacterial pathogens.

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Section: Discussionmentioning

confidence: 52%

T3SS translocon induces pyroptosis by direct interaction with NLRC4/NAIP inflammasome

Zhao,

Zhu,

et al. 2024

Preprint

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“…In zebrafish larvae, WDR90 is involved in caspy activation, and acts upstream of ASC and caspy to promote S. Typhimurium resistance ( 58 ). The virulence effector trxlp of E. piscicida , which is an important pathogenic bacterium that causes hemorrhagic septicemia in fish, mainly promotes the NLRC4 but not NLRP3 inflammasome activation during E. piscicida infection in murine macrophages ( 64 ). In response to the infection of Lm-pyro L. monocytogenes , a strain engineered to activate the inflammasome via ectopic expression of flagellin, zebrafish inflammasome is activated, which leads to the recruitment of macrophages to infection sites and confers host protection to bacterial infection.…”

Section: Nlrc4 Inflammasomementioning

confidence: 99%

Emerging mechanisms and functions of inflammasome complexes in teleost fish

Chang

2023

Front. Immunol.

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Inflammasomes are multiprotein complexes, which are assembled in response to a diverse range of exogenous pathogens and endogenous danger signals, leading to produce pro-inflammatory cytokines and induce pyroptotic cell death. Inflammasome components have been identified in teleost fish. Previous reviews have highlighted the conservation of inflammasome components in evolution, inflammasome function in zebrafish infectious and non-infectious models, and the mechanism that induce pyroptosis in fish. The activation of inflammasome involves the canonical and noncanonical pathways, which can play critical roles in the control of various inflammatory and metabolic diseases. The canonical inflammasomes activate caspase-1, and their signaling is initiated by cytosolic pattern recognition receptors. However the noncanonical inflammasomes activate inflammatory caspase upon sensing of cytosolic lipopolysaccharide from Gram-negative bacteria. In this review, we summarize the mechanisms of activation of canonical and noncanonical inflammasomes in teleost fish, with a particular focus on inflammasome complexes in response to bacterial infection. Furthermore, the functions of inflammasome-associated effectors, specific regulatory mechanisms of teleost inflammasomes and functional roles of inflammasomes in innate immune responses are also reviewed. The knowledge of inflammasome activation and pathogen clearance in teleost fish will shed new light on new molecular targets for treatment of inflammatory and infectious diseases.

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“…In mice, NLRP1B inflammasome activation plays a crucial role in the host’s defense against infection with the Gram-positive bacteria Bacillus anthracis [ 90 ] and the intracellular parasite Toxoplasma gondii [ 31 ]. The NLRP3 inflammasome is activated by a wide range of pathogens, including Gram-positive and Gram-negative bacteria (e.g., Staphylococcus aureus [ 91 ], Mycobacterium tuberculosis [ 92 , 93 , 94 ], E. tarda [ 95 , 96 , 97 ], Listeria monocytogenes [ 98 ]) [ 99 ], RNA and DNA viruses (e.g., influenza virus, adenovirus [ 100 ], SARS-CoV-2 [ 101 ]) [ 102 ], fungi (e.g., Candida albicans [ 103 ]), and parasites (e.g., Leishmania amazonensis [ 104 ]) in mammals. The relationship between the inflammasomes and E. piscicida (also known as E. tarda in mammals) and Aeromonas sp.…”

Section: Inflammasome Activation During Pathogenic Infectionmentioning

confidence: 99%

“…However, the LPS-priming step was necessary for activation [ 95 , 97 ]. The E. piscicida virulence effector trxlp also activated the NLRC4 inflammasome in mouse BMDMs and the mouse macrophage-like cell line J774A.1 [ 96 ]. However, the E. piscicida type VI secretion system (T6SS) effector protein (EvpP) suppressed NLRP3 inflammasome activation via ASC oligomerization by inhibiting calcium ion-dependent JNK (c-Jun N-terminal kinase) signals in the J774A.1 cells [ 97 ].…”

Section: Inflammasome Activation During Pathogenic Infectionmentioning

confidence: 99%

Inflammasomes in Teleosts: Structures and Mechanisms That Induce Pyroptosis during Bacterial Infection

Morimoto

Kono

Sakai

et al. 2021

IJMS

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Pattern recognition receptors (PRRs) play a crucial role in inducing inflammatory responses; they recognize pathogen-associated molecular patterns, damage-associated molecular patterns, and environmental factors. Nucleotide-binding oligomerization domain-leucine-rich repeat-containing receptors (NLRs) are part of the PRR family; they form a large multiple-protein complex called the inflammasome in the cytosol. In mammals, the inflammasome consists of an NLR, used as a sensor molecule, apoptosis-associated speck-like protein containing a caspase recruitment domain (ASC) as an adaptor protein, and pro-caspase1 (Casp1). Inflammasome activation induces Casp1 activation, promoting the maturation of proinflammatory cytokines, such as interleukin (IL)-1β and IL-18, and the induction of inflammatory cell death called pyroptosis via gasdermin D cleavage in mammals. Inflammasome activation and pyroptosis in mammals play important roles in protecting the host from pathogen infection. Recently, numerous inflammasome-related genes in teleosts have been identified, and their conservation and/or differentiation between their expression in mammals and teleosts have also been elucidated. In this review, we summarize the current knowledge of the molecular structure and machinery of the inflammasomes and the ASC-spec to induce pyroptosis; moreover, we explore the protective role of the inflammasome against pathogenic infection in teleosts.

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Edwardsiella piscicida virulence effector trxlp promotes the NLRC4 inflammasome activation during infection

Cited by 10 publications

References 34 publications

T3SS translocon induces pyroptosis by direct interaction with NLRC4/NAIP inflammasome

T3SS translocon induces pyroptosis by direct interaction with NLRC4/NAIP inflammasome

Emerging mechanisms and functions of inflammasome complexes in teleost fish

Inflammasomes in Teleosts: Structures and Mechanisms That Induce Pyroptosis during Bacterial Infection

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