TRIM103 activates the RLRs pathway to enhance antiviral response by targeting VP5 and VP7.

Autor: Qin B; College of Animal Science and Technology, Hunan Agricultural University, Changsha, 410128, China., Lv Z; Fisheries College, Hunan Agricultural University, Changsha, 410128, China; Hunan Engineering Technology Research Center of Featured Aquatic Resources Utilization, Hunan Agricultural University, Changsha, 410128, China., Yang H; Fisheries College, Hunan Agricultural University, Changsha, 410128, China., Xiao T; Fisheries College, Hunan Agricultural University, Changsha, 410128, China; Hunan Engineering Technology Research Center of Featured Aquatic Resources Utilization, Hunan Agricultural University, Changsha, 410128, China., Su J; Department of Basic Veterinary Medicine, College of Veterinary Medicine, Hunan Agricultural University, Changsha, Hunan, China. Electronic address: sjmauhn@hunau.edu.cn.
Jazyk: angličtina
Zdroj: Developmental and comparative immunology [Dev Comp Immunol] 2024 Dec; Vol. 161, pp. 105254. Date of Electronic Publication: 2024 Aug 28.
DOI: 10.1016/j.dci.2024.105254
Abstrakt: Grass carp (Ctenopharyngodon idella), crucial to global inland aquaculture with a production of 5.8 million tones in 2020, faces significant challenges from hemorrhagic disease caused by grass carp reovirus (GCRV). Rapid mutations compromise current vaccines, underscoring the need for a deeper understanding of antiviral mechanisms to enhance molecular marker-assisted selection. This study investigates the role of Tripartite Motif (TRIM) family in the innate immune response of grass carp, focusing on TRIM103 from Ctenopharyngodon Idella (CiTRIM103), a member of the TRIM-B30.2 family, which includes proteins with the B30.2 domain at the N-terminus, known for antiviral properties in teleosts. CiTRIM103 bind to the outer coat proteins VP5 and VP7 of GCRV. This binding is theorized to strengthen the function of the RIG-I-like Receptor (RLR) signaling pathway, crucial for antiviral responses. Demonstrations using overexpression and RNA interference (RNAi) techniques have shown that CiTRIM103 effectively inhibits GCRV replication. Moreover, molecular docking and pulldown assays suggest potential binding interactions of CiTRIM103's B30.2 domain with GCRV outer coat proteins VP5 and VP7. These interactions impede viral replication, enhance RLR receptor expression, and activate key transcription factors to induce type I interferons (IFNs). These findings elucidate the antiviral mechanisms of CiTRIM103, provide a foundation for future Molecular genetic breeding in grass carp.
(Copyright © 2024 Elsevier Ltd. All rights reserved.)
Databáze: MEDLINE
Externí odkaz: