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Published on: December 21, 2019
Eight TRIM32 isoforms from oriental river prawn Macrobrachium nipponense are involved in innate immunity during white
Wei-Yu Chen1, Yi-Qing Gong2, Xu-Ri Zhou3
1College of Water Conservancy and Hydropower Engineering, Hohai University, 1 Xikang Road, Nanjing, Jiangsu, 210098, China.
Abstract:
Tripartite motif (TRIM) proteins comprise a large family of RING-type ubiquitin E3 ligases that regulate important biological processes. In this study, full-length MnTRIM32 cDNA was obtained from oriental river prawn Macrobrachium nipponense, and eight MnTRIM32 isoforms generated by alternative splicing were identified. The open reading frames of the eight MnTRIM32 isoforms were predicted to be separately composed of 402, 346, 347, 346, 414, 358, 359, and 358 amino acid residues. Protein structural analysis revealed that all MnTRIM32 isoforms contained a RING domain and a coiled coil region. MnTRIM32 was ubiquitously expressed in all tissues tested, with the highest expression in the hepatopancreas. The mRNA levels of MnTRIM32 in the gills, stomach, and intestine of prawns were found to undergo time-dependent enhancement following white spot syndrome virus (WSSV) stimulation. Double-stranded RNA interference studies revealed that MnTRIM32 silencing significantly downregulated the expression levels of interferon (IFN) regulatory factor MnIRF, IFN-like factor MnVago4, and tumor necrosis factor MnTNF. Furthermore, knockdown of MnTRIM32 in WSSV-challenged prawns increased the expression of VP28 and the number of WSSV copies, suggesting that MnTRIM32 plays a positive role in limiting WSSV infection. These findings provided strong evidence for the important role of MnTRIM32 in the antiviral innate immunity of M. nipponense.
Insights
Macrobrachium nipponense TRIM32 (MnTRIM32) plays a crucial role in antiviral immunity. This study identified eight MnTRIM32 isoforms that help limit white spot syndrome virus (WSSV) infection in prawns.
Area of Science:
- * Molecular Biology
- * Immunology
- * Aquaculture
Background:
- * Tripartite motif (TRIM) proteins are RING-type ubiquitin E3 ligases involved in diverse biological processes.
- * MnTRIM32 is a member of this family found in the oriental river prawn, Macrobrachium nipponense.
- * Understanding MnTRIM32's function is vital for prawn antiviral defense.
Purpose of the Study:
- * To identify and characterize MnTRIM32 isoforms in Macrobrachium nipponense.
- * To investigate the role of MnTRIM32 in antiviral innate immunity against white spot syndrome virus (WSSV).
- * To elucidate the molecular mechanisms underlying MnTRIM32's antiviral activity.
Main Methods:
- * cDNA cloning and sequencing to identify MnTRIM32 isoforms.
- * Bioinformatic analysis for protein structure prediction.
- * Quantitative real-time PCR (qRT-PCR) for gene expression analysis.
- * Double-stranded RNA interference (dsRNAi) for gene silencing.
- * WSSV challenge assays to assess viral load and gene expression.
Main Results:
- * Eight MnTRIM32 isoforms were identified, all possessing a RING domain and coiled coil region.
- * MnTRIM32 exhibited ubiquitous expression, with highest levels in the hepatopancreas.
- * MnTRIM32 mRNA levels increased in response to WSSV infection in gills, stomach, and intestine.
- * Silencing MnTRIM32 led to downregulation of key antiviral genes (MnIRF, MnVago4, MnTNF).
- * MnTRIM32 knockdown enhanced WSSV replication, indicated by increased VP28 expression and viral copy numbers.
Conclusions:
- * MnTRIM32 is a critical component of the antiviral innate immune response in Macrobrachium nipponense.
- * MnTRIM32 positively regulates antiviral immunity, likely by influencing the expression of interferon regulatory factors and related pathways.
- * These findings highlight MnTRIM32 as a potential target for enhancing antiviral strategies in prawn aquaculture.
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