Functional characterization of alkaline phosphatases involved alarm pheromone in the vetch aphid Megoura viciae
Summary: The alkaline phosphatases (ALPs) are highly promiscuous enzymes and have been extensively investigated in mammals for their medical significance, but their functional promiscuity is relatively poorly understood in insects. Here, we first identified four ALP genes (designated as MvALP1-4) in...
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Elsevier
2023-11-01
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| Series: | iScience |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2589004223021922 |
| _version_ | 1797659925233532928 |
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| author | Xuan Song Yao-Guo Qin Yi-Han Zhang Yu-Bei Zhou Dan Chen Dong-Hai Xie Zheng-Xi Li |
| author_facet | Xuan Song Yao-Guo Qin Yi-Han Zhang Yu-Bei Zhou Dan Chen Dong-Hai Xie Zheng-Xi Li |
| author_sort | Xuan Song |
| collection | DOAJ |
| description | Summary: The alkaline phosphatases (ALPs) are highly promiscuous enzymes and have been extensively investigated in mammals for their medical significance, but their functional promiscuity is relatively poorly understood in insects. Here, we first identified four ALP genes (designated as MvALP1-4) in the vetch aphid Megoura viciae that contained one alkaline phosphatase site, three metal-binding sites, and varied other functional sites. Phylogenetic analysis, molecular docking and the spatiotemporal expression profiling of MvALP1-4 were very different, indicating a promiscuous functionality. We also found that MvALP4 involved the biosynthesis of aphid alarm pheromones (EβF) in vitro and in vivo. Finally, transcriptome analysis in the stimulated and unstimulated aphids supported the involvement of MvALPs in the biosynthesis of aphid alarm pheromones. Our study identified a multifunctional ALP involved terpene synthase enzyme activity in the aphid, which contributes to the understanding of the functional plasticity of ALPs in insects. |
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| format | Article |
| id | doaj.art-9ccf83ec17dd4e3696f5966b5081e789 |
| institution | Directory Open Access Journal |
| issn | 2589-0042 |
| language | English |
| last_indexed | 2024-03-11T18:22:19Z |
| publishDate | 2023-11-01 |
| publisher | Elsevier |
| record_format | Article |
| series | iScience |
| spelling | doaj.art-9ccf83ec17dd4e3696f5966b5081e7892023-10-15T04:38:05ZengElsevieriScience2589-00422023-11-012611108115Functional characterization of alkaline phosphatases involved alarm pheromone in the vetch aphid Megoura viciaeXuan Song0Yao-Guo Qin1Yi-Han Zhang2Yu-Bei Zhou3Dan Chen4Dong-Hai Xie5Zheng-Xi Li6Department of Entomology and MOA Key Laboratory for Monitoring and Environment-Friendly Control of Crop Pests, College of Plant Protection, China Agricultural University, Beijing 100193, ChinaDepartment of Entomology and MOA Key Laboratory for Monitoring and Environment-Friendly Control of Crop Pests, College of Plant Protection, China Agricultural University, Beijing 100193, ChinaDepartment of Entomology and MOA Key Laboratory for Monitoring and Environment-Friendly Control of Crop Pests, College of Plant Protection, China Agricultural University, Beijing 100193, ChinaDepartment of Entomology and MOA Key Laboratory for Monitoring and Environment-Friendly Control of Crop Pests, College of Plant Protection, China Agricultural University, Beijing 100193, ChinaDepartment of Entomology and MOA Key Laboratory for Monitoring and Environment-Friendly Control of Crop Pests, College of Plant Protection, China Agricultural University, Beijing 100193, ChinaDepartment of Entomology and MOA Key Laboratory for Monitoring and Environment-Friendly Control of Crop Pests, College of Plant Protection, China Agricultural University, Beijing 100193, ChinaDepartment of Entomology and MOA Key Laboratory for Monitoring and Environment-Friendly Control of Crop Pests, College of Plant Protection, China Agricultural University, Beijing 100193, China; Corresponding authorSummary: The alkaline phosphatases (ALPs) are highly promiscuous enzymes and have been extensively investigated in mammals for their medical significance, but their functional promiscuity is relatively poorly understood in insects. Here, we first identified four ALP genes (designated as MvALP1-4) in the vetch aphid Megoura viciae that contained one alkaline phosphatase site, three metal-binding sites, and varied other functional sites. Phylogenetic analysis, molecular docking and the spatiotemporal expression profiling of MvALP1-4 were very different, indicating a promiscuous functionality. We also found that MvALP4 involved the biosynthesis of aphid alarm pheromones (EβF) in vitro and in vivo. Finally, transcriptome analysis in the stimulated and unstimulated aphids supported the involvement of MvALPs in the biosynthesis of aphid alarm pheromones. Our study identified a multifunctional ALP involved terpene synthase enzyme activity in the aphid, which contributes to the understanding of the functional plasticity of ALPs in insects.http://www.sciencedirect.com/science/article/pii/S2589004223021922EntomologyMolecular biologyPhylogeny |
| spellingShingle | Xuan Song Yao-Guo Qin Yi-Han Zhang Yu-Bei Zhou Dan Chen Dong-Hai Xie Zheng-Xi Li Functional characterization of alkaline phosphatases involved alarm pheromone in the vetch aphid Megoura viciae iScience Entomology Molecular biology Phylogeny |
| title | Functional characterization of alkaline phosphatases involved alarm pheromone in the vetch aphid Megoura viciae |
| title_full | Functional characterization of alkaline phosphatases involved alarm pheromone in the vetch aphid Megoura viciae |
| title_fullStr | Functional characterization of alkaline phosphatases involved alarm pheromone in the vetch aphid Megoura viciae |
| title_full_unstemmed | Functional characterization of alkaline phosphatases involved alarm pheromone in the vetch aphid Megoura viciae |
| title_short | Functional characterization of alkaline phosphatases involved alarm pheromone in the vetch aphid Megoura viciae |
| title_sort | functional characterization of alkaline phosphatases involved alarm pheromone in the vetch aphid megoura viciae |
| topic | Entomology Molecular biology Phylogeny |
| url | http://www.sciencedirect.com/science/article/pii/S2589004223021922 |
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