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Trim23 promotes WSSV replication though negative regulation of antimicrobial peptides expression in Macrobrachium
Ruidong Zhang1, Xiaoling Dai1, Xueying Cao1
1Jiangsu Province Engineering Research Center for Aquatic Animals Breeding and Green Efficient Aquacultural Technology, College of Marine Science and Engineering, Nanjing Normal University, 1 Wenyuan Road, Nanjing, Jiangsu 210023, China.
Abstract:
The family of TRIM proteins with E3 ubiquitin ligase activity plays important roles in virus infection in vertebrates and invertebrates. In this study, a novel Trim gene shows high similarity to Trim23 (designated as MnTrim23) was identified from Macrobrachium nipponense. The MnTrim23 protein contains three conserved domains (one RING finger domain, two B-box, and one Coiled-coil region) at its N-terminal and one ARF domain at its C-terminal. The ARF domain characterizes the members of the Trim23 family. MnTrim23 belongs to C-IX family. Phylogenetic analysis shows that MnTrim23 has a closer genetic distance with other Trim23 proteins from invertebrates than that from vertebrates. MnTrim23 has higher expression level in the intestine and hepatopancreas than in the other immune tissues. The expression levels of MnTrim23 in the gills, stomach, and intestines are significantly up-regulated after white spot syndrome virus (WSSV) infection. Moreover, knockdown of MnTrim23 inhibits WSSV replication and VP28 expression, suggesting that MnTrim23 plays a positive role in WSSV infection. Further studies revealed that MnTrim23 negatively regulates the Relish transcription factor-mediated expression of antimicrobial peptides (AMPs). Synthetic AMPs inhibit VP28 expression and WSSV replication. These findings indicate that Trim23 promotes WSSV replication by inhibiting the expression of AMPs that are positively regulated by the host NF-κB signal pathway.
Insights
Macrobrachium nipponense Trim23 (MnTrim23) aids white spot syndrome virus (WSSV) infection by suppressing antimicrobial peptides. Inhibiting MnTrim23 reduces WSSV replication, highlighting its role in shrimp immunity.
Area of Science:
- * Molecular Biology
- * Immunology
- * Zoology
Background:
- * The TRIM (E3 ubiquitin ligase) protein family is crucial in vertebrate and invertebrate antiviral responses.
- * White spot syndrome virus (WSSV) is a significant pathogen affecting shrimp aquaculture.
Purpose of the Study:
- * To identify and characterize a novel TRIM protein, MnTrim23, from Macrobrachium nipponense.
- * To investigate the role of MnTrim23 in WSSV infection and shrimp immune response.
Main Methods:
- * Gene identification, protein domain analysis, phylogenetic analysis, and gene expression analysis (RT-qPCR).
- * RNA interference (RNAi) for gene knockdown and analysis of WSSV replication and VP28 expression.
- * Investigation of the regulatory relationship between MnTrim23, Relish, antimicrobial peptides (AMPs), and WSSV.
Main Results:
- * A novel gene, MnTrim23, similar to Trim23, was identified in Macrobrachium nipponense, possessing conserved TRIM domains and an ARF domain.
- * MnTrim23 expression was highest in the intestine and hepatopancreas and significantly upregulated in response to WSSV infection.
- * Knockdown of MnTrim23 inhibited WSSV replication and VP28 expression, while MnTrim23 negatively regulated Relish-mediated AMP expression, and synthetic AMPs inhibited WSSV.
Conclusions:
- * MnTrim23 plays a positive role in WSSV infection by inhibiting the expression of host antimicrobial peptides.
- * The findings elucidate a novel antiviral mechanism involving MnTrim23 and AMPs regulated by the NF-κB pathway in shrimp.
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