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两种假定信息素结合蛋白在杂食性德国蟑螂中的特异性结合的表达、亲和力和功能特征。

Expression, Affinity, and Functional Characterization of the Specific Binding of Two Putative Pheromone-Binding Proteins in the Omnivorous German Cockroach .

机构信息

State Key Laboratory Breeding Base of Green Pesticide and Agricultural Bioengineering, Key Laboratory of Green Pesticide and Agricultural Bioengineering, Ministry of Education, Guizhou University, Huaxi District, Guiyang 550025, People's Republic of China.

Bioassay Research Department, Central Agricultural Pesticide Laboratory, Agricultural Research Center, 7 Nadi El-Seid Street, Dokki 12618, Giza, Egypt.

出版信息

J Agric Food Chem. 2020 Nov 25;68(47):13573-13583. doi: 10.1021/acs.jafc.0c02456. Epub 2020 Nov 6.

DOI:10.1021/acs.jafc.0c02456
PMID:32955873
Abstract

The German cockroach (L.) is an important pest in medical, veterinary, and public health. Studies on the olfaction mechanism of hemimetabolous insects have rarely been reported, especially in cockroaches. Pheromone-binding proteins (PBPs) play a vital role in insect sex pheromone recognition, which solubilize and carry the hydrophobic pheromonal compounds through the antennal lymph to receptors. In this study, two potential PBPs ( and ) were identified on the basis of their biased expression in male antennae using tissue transcriptome data and verified by the quantitative real-time polymerase chain reaction approach. We then expressed and purified the two identified odorant-binding proteins (OBPs) using the expression system and affinity purification. binding studies showed that the two OBPs display stronger binding affinities to the female volatile sex pheromone blattellaquinone than to its analogues and contact sex pheromone components. Finally, three-dimensional modeling of the two OBPs and dock conformation with sex pheromone molecules showed BgerOBP26 has a larger odorant cavity and more conservative active amino acid residues than BgerOBP40. These results illuminated the binding characteristics of potential PBPs of , which could lay the groundwork for improved understanding of many aspects of the chemical ecology of . Moreover, this information complements the understanding of the olfactory molecular mechanism in cockroaches and provides potential gene targets for control.

摘要

德国小蠊(L.)是医学、兽医和公共卫生领域的重要害虫。关于半变态昆虫嗅觉机制的研究很少有报道,尤其是在蟑螂中。信息素结合蛋白(PBPs)在昆虫性信息素识别中起着至关重要的作用,它通过触角淋巴将疏水性信息素化合物溶解并携带到受体上。在本研究中,根据组织转录组数据,雄性触角中偏表达的情况,鉴定了两个潜在的 PBP(和),并通过定量实时聚合酶链反应方法进行了验证。然后,我们使用表达系统和亲和纯化表达和纯化了这两个鉴定的气味结合蛋白(OBPs)。结合研究表明,这两个 OBPs 对雌性挥发性性信息素巴西麻醌的结合亲和力强于其类似物和接触性信息素成分。最后,对两个 OBPs 的三维建模和与性信息素分子的对接构象表明,BgerOBP26 比 BgerOBP40 具有更大的气味腔和更保守的活性氨基酸残基。这些结果阐明了潜在的 PBPs 的结合特性,这可能为更好地理解的化学生态学的许多方面奠定基础。此外,这些信息补充了对蟑螂嗅觉分子机制的理解,并为提供了潜在的基因靶标用于控制。

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