Functional characterization of alkaline phosphatases involved alarm pheromone in the vetch aphid Megoura viciae

• Published in: iScience Vol. 26; no. 11; p. 108115
• Main Authors: Song, Xuan, Qin, Yao-Guo, Zhang, Yi-Han, Zhou, Yu-Bei, Chen, Dan, Xie, Dong-Hai, Li, Zheng-Xi
• Format: Journal Article
• Language: English
• Published: Elsevier Inc 17.11.2023; Elsevier
• Subjects: Entomology; Molecular biology; Phylogeny; Molecular biology; Entomology; Phylogeny
• ISSN: 2589-0042; 2589-0042
• DOI: 10.1016/j.isci.2023.108115

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. [Display omitted] •Four ALP genes are identified in the vetch aphid•The binding residues of (E, E)-FPP are varied in the MvALP1-4•The expression patterns of MvALP1-4 indicated promiscuous functions•One alkaline phosphatase has terpene synthase activity Entomology; Molecular biology; Phylogeny