CRISPR/Cas9-induced knockout of tumor necrosis factor-alpha-type I augments viral infection in zebrafish.

Tumor necrosis factor-alpha (TNF-α) is a pleiotropic cytokine with critical roles in inflammation, cell survival, and defense. As a member of the TNF superfamily, it exerts its effects by binding to transmembrane receptors and triggering various downstream signaling pathways. Although TNF-α's involvement in antiviral responses in mammals is well-established, its role in teleost remains poorly understood.

Exploring the immunological functions of thioredoxin domain-containing protein 17 (TXNDC17) in chub mackerel (Scomber japonicus): Immune response and cellular redox homeostasis.

All organisms have evolved sophisticated antioxidant networks and enzymes to counteract reactive radicals, among which thioredoxin (Trx) systems are especially noteworthy. Thioredoxin domain-containing protein 17 (TXNDC17) is a ubiquitously expressed enzyme with oxidoreductase activity belonging to the Trx protein family. This study successfully uncovered and analyzed the TXNDC17 gene in Scomber japonicus (SjTXNDC17).

Characterization of tumor necrosis factor receptor-associated factor 2 (TRAF2) in red-spotted grouper (Epinephelus akaara): In vivo and in vitro investigation of its role in the regulation of antiviral immunity and cell death.

Tumor necrosis factor receptor-associated factor 2 (TRAF2) is a key adaptor molecule in tumor necrosis factor receptor signaling complexes, facilitating downstream immune-related signaling cascades. This study aimed to elucidate its function in teleost fish by characterizing the TRAF2 homolog of the red-spotted grouper (Epinephelus akaara, EaTraf2). The open reading frame of EaTraf2 encodes a putative protein of 520 amino acids, containing several characteristic domains of TRAF2.

Characterization of tripartite motif containing 59 (TRIM59) in Epinephelus akaara: Insights into its immune involvement and functional properties in viral pathogenesis, macrophage polarization, and apoptosis regulation.

The tripartite motif-containing (TRIM) superfamily is the largest family of RING-type E3 ubiquitin ligases that is conserved across the metazoan kingdom. Previous studies in mammals have demonstrated that TRIM59 possesses ubiquitin-protein ligase activity and acts as a negative regulator of NF-κB signaling. However, TRIM59 has rarely been characterized in fish.

Molecular depiction and functional delineation of E3 ubiquitin ligase MARCH5 in yellowtail clownfish (Amphiprion clarkii).

Membrane-associated Ring-CH 5 (MARCH5) is a mitochondrial E3 ubiquitin ligase playing a key role in the regulation of mitochondrial dynamics. In mammals, MARCH5 negatively regulates mitochondrial antiviral signaling (MAVS) protein aggregation during viral infection and hampers downstream type I interferon signaling to prevent excessive immune activation. However, its precise functional role in the teleost immune system remains unclear.