Transcriptomic Analysis of Neocaridina denticulata sinensis Gills Following FPPS Knockdown Reveals Its Regulatory Role in Immune Response

Farnesyl pyrophosphate synthase (FPPS) is a key enzyme in the terpenoid biosynthesis pathway, responsible for converting isopentenyl pyrophosphate (IPP) and dimethylallyl pyrophosphate (DMAPP) into farnesyl pyrophosphate (FPP). In crustaceans, FPPS plays an important role in various physiological processes, particularly in synthesizing the crustacean-specific hormone methyl farnesoate (MF). This study analyzed the evolutionary differences in the physicochemical properties, subcellular localization, gene structure, and motif composition of FPPS in <i>Neocaridina denticulata sinensis</i> (named NdFPPS) compared to other species. The significant evolutionary divergence of FPPS was observed in crustaceans, likely linked to its role in MF synthesis. After the RNA interference (RNAi)-mediated knockdown of <i>NdFPPS</i>, transcriptomic analysis of gills revealed the significant enrichment of differentially expressed genes (DEGs) in pathways related to metabolism and immunity. Gene set enrichment analysis (GSEA) showed that most of these immune-related pathways were significantly suppressed, suggesting that <i>NdFPPS</i> may indirectly regulate the immune response by modulating metabolic levels. During the early stages of <i>Vibrio parahaemolyticus</i> infection, the expression of <i>NdFPPS</i> in the gills was significantly downregulated and subsequently returned to its original levels. Overall, our results provide new perspectives on the role of FPPS in immune regulation and enrich the functional information of FPPS.

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Publication Details

Journal
International Journal of Molecular Sciences
Published
2024-12-25
DOI
https://doi.org/10.3390/ijms26010065
Citations
1
Primary Topic
Invertebrate Immune Response Mechanisms
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article
Field-Weighted Citation Impact
0.24

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article

Transcriptomic Analysis of Neocaridina denticulata sinensis Gills Following FPPS Knockdown Reveals Its Regulatory Role in Immune Response

Dandan Feng, Hongrui Li, Chunyu Zhang, Jiquan Zhang et al.
1 citations
International Journal of Molecular Sciences
Invertebrate Immune Response Mechanisms
0.24
article

Transcriptomic Analysis of Neocaridina denticulata sinensis Gills Following FPPS Knockdown Reveals Its Regulatory Role in Immune Response

Dandan Feng, Hongrui Li, Chunyu Zhang, Jiquan Zhang, Zixuan Wu, Yuke Bu, Mengfei Liu, Yuying Sun
article en
1 citations

Abstract

Farnesyl pyrophosphate synthase (FPPS) is a key enzyme in the terpenoid biosynthesis pathway, responsible for converting isopentenyl pyrophosphate (IPP) and dimethylallyl pyrophosphate (DMAPP) into farnesyl pyrophosphate (FPP). In crustaceans, FPPS plays an important role in various physiological processes, particularly in synthesizing the crustacean-specific hormone methyl farnesoate (MF). This study analyzed the evolutionary differences in the physicochemical properties, subcellular localization, gene structure, and motif composition of FPPS in <i>Neocaridina denticulata sinensis</i> (named NdFPPS) compared to other species. The significant evolutionary divergence of FPPS was observed in crustaceans, likely linked to its role in MF synthesis. After the RNA interference (RNAi)-mediated knockdown of <i>NdFPPS</i>, transcriptomic analysis of gills revealed the significant enrichment of differentially expressed genes (DEGs) in pathways related to metabolism and immunity. Gene set enrichment analysis (GSEA) showed that most of these immune-related pathways were significantly suppressed, suggesting that <i>NdFPPS</i> may indirectly regulate the immune response by modulating metabolic levels. During the early stages of <i>Vibrio parahaemolyticus</i> infection, the expression of <i>NdFPPS</i> in the gills was significantly downregulated and subsequently returned to its original levels. Overall, our results provide new perspectives on the role of FPPS in immune regulation and enrich the functional information of FPPS.

International Journal of Molecular SciencesVol. 26(1)
Hebei University (CN)
National Natural Science Foundation of China
Life below water
Openalex Percentile: Top 39%
Invertebrate Immune Response Mechanisms
0.24
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