Article (Scientific journals)
Pheromone-Binding Protein 1 Performs a Dual Function for Intra- and Intersexual Signaling in a Moth
Zhan, Yidi; Zhang, Jiahui; Xu, Mengxian et al.
2024In International Journal of Molecular Sciences, 25 (23)
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Keywords :
intraspecies communication; mating behavioral manipulation; pheromone recognition mechanism; Animals; Carrier Proteins; Female; Insect Proteins; Male; Molecular Docking Simulation; Moths; Phylogeny; Receptors, Odorant; Sex Attractants; Signal Transduction; 9 hexadecenyl acetate; complementary DNA; hydrogen; odorant binding protein; odorant binding protein 13; odorant binding protein 18; odorant binding protein 2; odorant binding protein 22; odorant binding protein 28a; odorant binding protein 29; odorant binding protein 4; odorant binding protein 40; odorant binding protein 9; pheromone; pheromone binding protein 1; sex pheromone; transcriptome; unclassified drug; carrier protein; insect protein; odorant-binding protein; pheromone binding protein, insect; Agriphila aeneociliella; Article; binding affinity; Cnaphalocrocis medinalis; competitive binding assay; controlled study; DNA synthesis; fluorescence; hydrogen bond; Lepidoptera; molecular docking; molecular interaction; moth; nonhuman; phylogeny; protein expression; protein function; protein localization; reproductive isolation; animal; female; genetics; male; metabolism; olfactory receptor; signal transduction
Abstract :
[en] Moths use pheromones to ensure intraspecific communication. Nevertheless, few studies are focused on both intra- and intersexual communication based on pheromone recognition. Pheromone-binding proteins (PBPs) are generally believed pivotal for male moths in recognizing female pheromones. Our research revealed that PBP1 of Agriphila aeneociliella (AaenPBP1) serves a dual function in both intra- and intersexual pheromone recognition. Here, a total of 20 odorant-binding protein (OBP) family genes from A. aeneociliella were identified and subjected to transcriptional analysis. Among these, AaenPBP1 was primarily highly expressed in the antennae. Competitive fluorescence binding assays and molecular docking analyses demonstrated that AaenPBP1 exhibits a strong binding affinity for the female sex pheromone (Z)-9-Hexadecenyl acetate and the male pheromone 1-Nonanal. Notably, hydrogen bonds were observed between Ser56 and the ligands. The analysis of pheromone components and PBPs in lepidopteran lineage suggested that their strong and precise interactions, shaped by coevolution, may play a crucial role in facilitating reproductive isolation in moths. Our findings provide valuable insight into the functional significance of PBPs in invertebrates and support the development of behavioral regulation tools as part of an integrated pest management strategy targeting crambid pests. © 2024 by the authors.
Disciplines :
Entomology & pest control
Author, co-author :
Zhan, Yidi;  State Key Laboratory of Wheat Improvement, Shandong Agricultural University, No. 61, Daizong Road, Taian, 271018, China ; College of Plant Protection, Shandong Agricultural University, No. 61, Daizong Road, Taian, 271018, China
Zhang, Jiahui  ;  Université de Liège - ULiège > TERRA Research Centre ; College of Plant Protection, Shandong Agricultural University, No. 61, Daizong Road, Taian, 271018, China
Xu, Mengxian;  College of Plant Protection, Shandong Agricultural University, No. 61, Daizong Road, Taian, 271018, China
Francis, Frédéric  ;  Université de Liège - ULiège > TERRA Research Centre > Gestion durable des bio-agresseurs ; College of Plant Protection, Shandong Agricultural University, No. 61, Daizong Road, Taian, 271018, China
Liu, Yong;  State Key Laboratory of Wheat Improvement, Shandong Agricultural University, No. 61, Daizong Road, Taian, 271018, China ; College of Plant Protection, Shandong Agricultural University, No. 61, Daizong Road, Taian, 271018, China
Language :
English
Title :
Pheromone-Binding Protein 1 Performs a Dual Function for Intra- and Intersexual Signaling in a Moth
Publication date :
06 December 2024
Journal title :
International Journal of Molecular Sciences
ISSN :
1661-6596
eISSN :
1422-0067
Publisher :
MDPI
Volume :
25
Issue :
23
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 23 July 2025

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