PUBLICATION
RIPK3 collaborates with RIPK1 to inhibit MAVS-mediated signaling during black carp antiviral innate immunity
- Authors
- Dai, Y., Cao, Y., Chen, Z., Huang, J., Xiao, J., Zou, J., Feng, H.
- ID
- ZDB-PUB-210622-37
- Date
- 2021
- Source
- Fish & shellfish immunology 115: 142-149 (Journal)
- Registered Authors
- Keywords
- Black carp, Interferon, MAVS, RIPK3
- MeSH Terms
-
- Adaptor Proteins, Signal Transducing/chemistry
- Adaptor Proteins, Signal Transducing/genetics
- Adaptor Proteins, Signal Transducing/immunology
- Amino Acid Sequence
- Animals
- Cyprinidae/genetics*
- Cyprinidae/immunology*
- Fish Diseases/immunology*
- Fish Proteins/genetics*
- Fish Proteins/immunology*
- Gene Expression Profiling/veterinary
- Gene Expression Regulation/immunology*
- Immunity, Innate/genetics*
- Phylogeny
- Receptor-Interacting Protein Serine-Threonine Kinases/chemistry
- Receptor-Interacting Protein Serine-Threonine Kinases/genetics
- Receptor-Interacting Protein Serine-Threonine Kinases/immunology
- Rhabdoviridae/physiology
- Rhabdoviridae Infections/immunology
- Rhabdoviridae Infections/veterinary
- Sequence Alignment/veterinary
- PubMed
- 34147612 Full text @ Fish Shellfish Immunol.
Citation
Dai, Y., Cao, Y., Chen, Z., Huang, J., Xiao, J., Zou, J., Feng, H. (2021) RIPK3 collaborates with RIPK1 to inhibit MAVS-mediated signaling during black carp antiviral innate immunity. Fish & shellfish immunology. 115:142-149.
Abstract
Both the activation and attenuation of MAVS/IFN signaling are critical for host defensing against viral infection and thus lead to an elaborate regulation of MAVS-mediated signaling. However, the regulatory mechanisms concerning MAVS/IFN signaling in teleost fish are not well understood. RIPK3 has been identified as a key regulator of necroptosis, apoptosis, and inflammatory signaling in human and mammals. Here we report the identification of the RIPK3 homologue from black carp Mylopharyngodon piceus (bcRIPK3) and describe its role in regulating MAVS/IFN signaling. qPCR results demonstrated that bcRIPK3 was transcriptionally activated in response to poly (I:C) or LPS stimulation. Immunoblot assay and immunofluorescent staining assay showed that bcRIPK3 was a cytosolic protein with molecular weights of 47 kDa. Like its mammalian counterparts, bcRIPK3 exhibited a conserved function in inducing cell death. The reporter assay and plaque assay showed that overexpression of bcRIPK3 restricted bcMAVS-activated transcription of the interferon promoters of black carp and zebrafish, and suppressed bcMAVS-mediated antiviral activity. Notably, EPC cells co-expressing bcRIPK3, bcRIPK1 and bcMAVS presented much attenuated antiviral activity than the cells co-expressing bcRIPK3 and bcMAVS; and the subsequent co-IP assay identified the interaction between bcRIPK3 and bcRIPK1. Our findings collectively elucidate for the first time in teleost that black carp RIPK3 interacts with RIPK1 to inhibit MAVS-mediated antiviral signaling.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping