Related Experiment Video
Updated: Jul 23, 2025
Dissection of Drosophila melanogaster Flight Muscles for Omics Approaches
Published on: October 17, 2019
Molecular characterization and functional analysis of TRIM37 from black tiger shrimp (Penaeus monodon)
Chao Zhao1, Chao Peng2, Pengfei Wang2
1Key Laboratory of South China Sea Fishery Resources Exploitation and Utilization, Ministry of Agriculture and Rural Affairs, South China Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, 510300, Guangzhou, Guangdong Province, China; Key Laboratory of Aquacultural Biotechnology Ministry of Education, Ningbo University, Ningbo, 315832, China.
Abstract:
The family of TRIM proteins with E3 ubiquitin ligase activity served important roles in the regulation of innate immune processes, in particular antiviral and proinflammatory cytokine responses. In this study, a novel TRIM37 homolog was identified from Penaeus monodon (named PmTRIM37). The PmTRIM37 protein contained three conserved domains (one RING finger domain, a B-box, and one Coiled-coil region) at its N-terminal and one Meprin and MATH domain at its C-terminal. The MATH domain was the characteristic of TRIM37 family. PmTRIM37 has relatively high expression in immune-related tissues such as hepatopancreas, gills, lymphoid organs and hemocytes. The expression levels of PmTRIM37 in hepatopancreas and lymphoid organs were significantly up-regulated after white spot syndrome virus (WSSV) infection. Knock down of PmTRIM37 promoted WSSV replication and VP28 expression, suggesting that PmTRIM37 played a negative role in WSSV infection. Further studies revealed that PmTRIM37 positively regulated the NF-κB pathway and Antimicrobial peptides (AMP) expression during WSSV infection. These findings indicated that PmTRIM37 might restrict WSSV replication by positively regulating NF-κB pathway during WSSV infection in P. monodon.
Insights
A novel TRIM37 protein in shrimp (PmTRIM37) was identified and found to be crucial for innate immunity. It restricts white spot syndrome virus (WSSV) by activating the NF-κB pathway and antimicrobial peptide production.
Area of Science:
- Marine biology
- Immunology
- Molecular biology
Background:
- The TRIM (Tripartite Motif) protein family plays a key role in innate immunity, particularly in antiviral and inflammatory responses.
- Understanding shrimp immune responses is vital for aquaculture and disease management.
Purpose of the Study:
- To identify and characterize a novel TRIM37 homolog in Penaeus monodon (PmTRIM37).
- To investigate the role of PmTRIM37 in the shrimp's response to white spot syndrome virus (WSSV) infection.
Main Methods:
- Identification and domain analysis of PmTRIM37.
- Gene expression analysis in different tissues and post-WSSV infection.
- RNA interference (RNAi) to knock down PmTRIM37 expression.
- Analysis of WSSV replication and VP28 expression.
- Investigation of the NF-κB pathway and antimicrobial peptide (AMP) expression.
Main Results:
- PmTRIM37 possesses conserved TRIM domains (RING, B-box, Coiled-coil) and a characteristic MATH domain.
- PmTRIM37 is highly expressed in immune tissues and significantly upregulated in the hepatopancreas and lymphoid organs after WSSV infection.
- Knockdown of PmTRIM37 enhanced WSSV replication and VP28 expression.
- PmTRIM37 positively regulates the NF-κB pathway and AMP expression during WSSV infection.
Conclusions:
- PmTRIM37 is a crucial component of the shrimp innate immune system.
- PmTRIM37 restricts WSSV replication, likely by activating the NF-κB pathway and promoting AMP production.
