Interferons (IFNs) have been reported in vertebrates from fish to mammals. To date, two types of IFNs, i.e. type I and type II IFNs have been reported in a range of fish species in aquaculture. In fish, type I IFNs are clarified into group I and group II, with two cysteines and four cysteines, and further into subgroups a, d, e, h, and b, c, f, respectively. Group I IFNs appear to exist in all fish species, whereas group II IFNs are discovered only in certain species such as cyprinids, salmonids and perciform fish. It seems preferentially functional that group I IFNs signal through cytokine receptor family B (CRFB) 5 and CRFB1, while group II IFNs through CRFB5 and CRFB2. But they all initiate a same signalling pathway for the expression of interferon induced genes. The information about the production and the function of type I IFNs in fish are further summarized in the review. Interestingly, two members of type II IFNs, IFN-gamma and a unique member, IFN-gamma related gene (IFN-gamma rel) exist in fish, and IFN-gamma and IFN-gamma rel can separately become homodimers for signalling through CRFB13, CRFB17, CRFB6 and CRFB17, respectively. In addition, the variation in the composition of type I and type II IFNs as well as in their receptors in some cyprinid and salmonid fish has also been reviewed. It is suggested that future perspectives for the research on type I and type II IFNs in fish are outlined from a comparative and evolutionary point of view.

https://onlinelibrary.wiley.com/doi/pdf/10.1111/raq.12349

Fish type I and type II interferons: composition, receptor usage, production and function

Pre-mRNA splicing is the process by which introns are removed and the protein coding elements assembled into mature mRNAs. Alternative pre-mRNA splicing provides an important source of transcriptome and proteome complexity through selectively joining different coding elements to form mRNAs, which encode proteins with similar or distinct functions. In mammals, previous studies have shown the role of alternative splicing in regulating the function of the immune system, especially in the regulation of T-cell activation and function. As lower vertebrates, teleost fish mainly rely on a large family of pattern recognition receptors (PRRs) to recognize pathogen-associated molecular patterns (PAMPs) from various invading pathogens. In this review, we summarize recent advances in our understanding of alternative splicing of piscine PRRs including peptidoglycan recognition proteins (PGRPs), nucleotide binding and oligomerization domain (NOD)-like receptors (NLRs), retinoic acid-inducible gene-I (RIG-I)-like receptors (RLRs) and their downstream signaling molecules, compared to splicing in mammals. We also discuss what is known and unknown about the function of splicing isoforms in the innate immune responses against pathogens infection in mammals and teleost fish. Finally, we highlight the consequences of alternative splicing in the innate immune system and give our view of important directions for future studies.

Alternative Pre-mRNA Splicing in Mammals and Teleost Fish: A Effective Strategy for the Regulation of Immune Responses Against Pathogen Infection

TBK1 of black carp plays an important role in host innate immune response against SVCV and GCRV.

Hepatitis C virus NS4B protein targets STING and abrogates RIG-I-mediated type I interferon-dependent innate immunity

SVCV infection triggers fish IFN response through RLR signaling pathway

The antiviral signaling mediated by black carp MDA5 is positively regulated by LGP2

Tumor necrosis factor receptor-associated factor 3 (TRAF3) is a main regulator of antiviral and anti-inflammatory pathways in mammals, which is considered to induce type I interferon (IFN) activation and negatively regulate the activation of the canonical and non-canonical NF-κB pathways To elucidate its function in teleost fish, TRAF3 homologue of black carp ( Mylopharyngodon piceus ) has been cloned and characterized in this study The open reading frame (ORF) of black carp TRAF3 (bcTRAF3) consists of 1722 nucleotides and bcTRAF3 contains 574 amino acids bcTRAF3 protein migrated around 65 KDa in immunoblot analysis of both EPC and HEK293T cells bcTRAF3 was identified as a cytosolic protein and suggested to form aggregates or be associated with vesicles scattering in the cytoplasm It was interesting that both NF-κB and IFN transcription was activated by bcTRAF3 in reporter assay When co-expressed with black carp STING (bcSTING), bcTRAF3 was redistributed in the cytoplasm and its subcellular location overlapped with that of bcSTING no matter what the cells was infected with GCRV or not, which suggested the association between these two molecules bcSTING-mediated IFN production was up-regulated by bcTRAF3 in a dose dependent manner in reporter assay Accordingly, EPC cells transfected with both bcSTING and bcTRAF3 showed enhanced antiviral activity comparing EPC cells expressing bcSTING alone Taken together, the data generated in this paper supported the conclusion that bcTRAF3 was recruited into host innate immune activation and positively regulated bcSTING-mediated antiviral signaling

TRAF3 enhances STING-mediated antiviral signaling during the innate immune activation of black carp.

Black carp STING functions importantly in innate immune defense against RNA virus.

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The antiviral signaling mediated by black carp MDA5 is positively regulated by LGP2

TRAF3 enhances STING-mediated antiviral signaling during the innate immune activation of black carp.

Black carp STING functions importantly in innate immune defense against RNA virus.