Identification and Characterization Analysis of Transient Receptor Potential Mucolipin Protein of Laodelphax striatellus Fallén.
Identification and Characterization Analysis of Transient Receptor Potential Mucolipin Protein of Laodelphax striatellus Fallén.
复制标题
灰飞虱瞬时受体电位粘磷脂蛋白的鉴定及表征分析
DOI：
10.3390/insects12121107
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发表时间：
2021-12-12
期刊：
影响因子：
3
通讯作者：
Xu Q
中科院分区：
文献类型：
--
作者：
Wang H;Dong Y;Wan B;Ji Y;Xu Q
灰飞虱（Laodelphax striatellus）是亚洲水稻、玉米和小麦等作物的毁灭性害虫，通过直接吸食韧皮部汁液和传播植物病毒造成危害，严重影响作物产量。瞬时受体电位粘脂蛋白（TRPML）在Ca 2+释放、细胞膜运输、细胞自噬和离子稳态等方面发挥重要作用，但目前对农业害虫TRPML蛋白的研究还很少。在本研究中，我们首先鉴定了L.纹状体。我们不仅分析了Ls-TRPML的基因进化特征和表达谱，而且阐明了Ls-TRPML的蛋白亚细胞定位和脂质结合特性。我们发现TRPML在农业害虫中是进化保守的。Ls-TRPML主要在L.具条纹的子房此外，我们还发现Ls-TRPML定位于草地贪夜蛾（Spodoptera frugiperda）细胞的核膜以及草地贪夜蛾的肠和卵巢。纹状体。脂质结合实验检测到Ls-TRPML与脂质的结合，表明Ls-TRPML在脂质相互作用中的潜在作用。因此，我们的研究结果首先帮助我们分析Ls-TRPML的基因特征，然后确定Ls-TRPML与脂质的结合;我们的研究结果将拓宽我们对TRPML在农业害虫中的作用的理解。瞬时受体电位粘脂蛋白（TRPML）在果蝇体内的钙离子释放中起着关键作用，导致细胞膜运输、自噬和离子稳态。然而，迄今为止，TRPML在农业害虫中的表征仍然未知。本文首次报道了禾本科作物毁灭性害虫灰飞虱的TRPML。洛杉矶纹状体TRPML（Ls-TRPML）开放阅读框为1818 bp，编码605个氨基酸。TRPML基因在农业害虫中具有进化保守性，Ls-TRPML基因在棉铃虫卵巢中的表达量明显高于其它器官。在转录和蛋白质水平上与纹状体细胞的同源性。Bac-Bac系统分析表明，Ls-TRPML在草地贪夜蛾细胞中定位于质膜、核膜和细胞核，并与溶酶体共定位。免疫荧光显微镜分析表明，Ls-TRPML定位于肠细胞和卵巢滤泡细胞的胞质和核周围。纹状体。从脂质结合试验的结果表明，Ls-TRPML强烈结合磷脂酰肌醇-3，5-二磷酸，与其他磷酸肌醇。总之，我们的研究结果有助于鉴定和表征L. TRPML在农业害虫中的多个细胞过程中的功能。
The small brown planthopper Laodelphax striatellus is a destructive pest of rice, maize and wheat crops in Asia, causing damage by directly sucking phloem sap and transmitting plant viruses, and thus seriously impacting crops yields. Transient receptor potential mucolipin (TRPML) protein plays a vital role in Ca2+ ions release, resulting in membrane trafficking, autophagy and ion homeostasis; however, till now, we have learned little about the TRPML protein of agricultural pests. In this study, we first identified the TRPML of L. striatellus. We analyzed not only the gene evolutionary features and expression profiles but also clarified the protein subcellular localization and lipid-binding characteristics of Ls-TRPML. We found that TRPML is evolutionarily conserved among agricultural pests. Ls-TRPML is predominately expressed in L. striatellus ovary. Moreover, we found that Ls-TRPML localizes in the nuclear membrane in Spodoptera frugiperda cells and the intestine and ovary of L. striatellus. The binding of Ls-TRPML with lipids was detected by lipid-binding assay, indicating the potential role of Ls-TRPML in lipid interaction. Thus, our findings first helped us analyze the gene characterization of Ls-TRPML and then identify the binding of Ls-TRPML with lipids; our findings will broaden our understanding of TRPML’s roles in agricultural pests. Transient receptor potential mucolipin (TRPML) protein in flies plays a pivotal role in Ca2+ ions release, resulting in membrane trafficking, autophagy and ion homeostasis. However, to date, the characterization of TRPML in agricultural pests remains unknown. Here, we firstly reported the TRPML of a destructive pest of gramineous crops, Laodelphax striatellus. The L. striatellus TRPML (Ls-TRPML) has a 1818 bp open reading frame, encoding 605 amino acid. TRPML in agricultural pests is evolutionarily conserved, and the expression of Ls-TRPML is predominately higher in the ovary than in other organs of L. striatellus at the transcript and protein level. The Bac–Bac system showed that Ls-TRPML localized in the plasma membrane, nuclear membrane and nucleus and co-localized with lysosome in Spodoptera frugiperda cells. The immunofluorescence microscopy analysis showed that Ls-TRPML localized in the cytoplasm and around the nuclei of the intestine cells or ovary follicular cells of L. striatellus. The results from the lipid-binding assay revealed that Ls-TRPML strongly bound to phosphatidylinositol-3,5-bisphosphate, as compared with other phosphoinositides. Overall, our results helped is identify and characterize the TRPML protein of L. striatellus, shedding light on the function of TRPML in multiple cellular processes in agricultural pests.
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