| Title: | "Expression, Affinity, and Functional Characterization of the Specific Binding of Two Putative Pheromone-Binding Proteins in the Omnivorous German Cockroach Blattella germanica" |
| Author(s): | Wang H; Ma YF; Wang MM; Chen GL; Dewer Y; He M; Zhang F; Yang YF; Liu JF; He P; |
| Address: | "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. Key Laboratory of Animal Resistance Research, College of Life Science, Shandong Normal University, 88 East Wenhua Road, Jinan 250014, People's Republic of China. Zunyi Medical University Zhuhai Campus, Zhuhai, Guangdong 519040, People's Republic of China. Institute of Entomology, Provincial Key Laboratory for Agricultural Pest Management in Mountainous Region, Guizhou University, Huaxi District, Guiyang, Guizhou 550025, People's Republic of China" |
| ISSN/ISBN: | 1520-5118 (Electronic) 0021-8561 (Linking) |
| Abstract: | "The German cockroach Blattella germanica (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 (BgerOBP26 and BgerOBP40) 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 Escherichia coli expression system and affinity purification. In vitro 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 B. germanica, which could lay the groundwork for improved understanding of many aspects of the chemical ecology of B. germanica. Moreover, this information complements the understanding of the olfactory molecular mechanism in cockroaches and provides potential gene targets for B. germanica control" |
| Keywords: | "Animals Arthropod Antennae/metabolism *Blattellidae/genetics/metabolism Carrier Proteins Female *Insect Proteins/genetics/metabolism Insecta/metabolism Male Pheromones *Receptors, Odorant/genetics/metabolism *Sex Attractants German cockroach binding affin;" |
| Notes: | "MedlineWang, Hong Ma, Yun-Feng Wang, Mei-Mei Chen, Guang-Lei Dewer, Youssef He, Ming Zhang, Fan Yang, Yu-Feng Liu, Jian-Feng He, Peng eng 2020/09/22 J Agric Food Chem. 2020 Nov 25; 68(47):13573-13583. doi: 10.1021/acs.jafc.0c02456. Epub 2020 Nov 6" |
