Binding affinity of five PBPs to Ostrinia sex pheromones

BMC Molecular Biology

Research Article

Kevin W. Wanner¹  Zhenying Wang²  Tiantao Zhang²  Kanglai He²  Yaqi Sun³  Brad S. Coates⁴ 

[1] Department of Plant Sciences and Plant Pathology, Montana State University, 59717, Bozemon, MT, USA;State Key Laboratory for the Biology of the Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, No. 2 West Yuanmingyuan Road, 100193, Beijing, China;State Key Laboratory for the Biology of the Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, No. 2 West Yuanmingyuan Road, 100193, Beijing, China;College of Bioscience Technology, Shenyang Agriculture University, Shenyang, China;United States Department of Agriculture, Agricultural Research Service, Corn Insects and Crop Genetics Research Unit, Iowa State University, 50011, Ames, IA, USA;

关键词: Pheromone binding protein;    Binding;    Sex pheromone;    Docking;    Mutant;   

DOI  :  10.1186/s12867-017-0079-y

 received in 2016-05-25, accepted in 2017-01-16,  发布年份 2017

来源: Springer

【 摘 要 】

BackgroundPheromone binding proteins (PBPs) of male Lepidoptera function in chemical communication, mate attraction and recognition. Directional selection was previously predicted between PBP3 orthologs of Ostrinia furnacalis and Ostrinia nubilalis were interpreted as being involved in sexual isolation.ResultsIn vitro assays show that recombinant male OfurPBP3 bound O. furnacalis sex pheromones, Z-12-tetradecenyl acetate (Z12-14:OAc) and E-12-tetradecenyl acetate (E12-14:OAc), as well as to ECB pheromones Z11- and E11-14:OAc. Recombinant OfurPBP4 and OfurPBP5 bound E11- and Z11-14:OAc with greater affinity compared to Z12- and E12-14:OAc, and OfurPBP4 incapable of binding with E12-14:OAc. In silico molecular docking predicted OfurPBP3 residues Phe12, Ile52, Leu94, Ile113 within a hydrophobic ligand-binding pocket and may participate in E12- and Z12-14:OAc binding. Independent site-directed mutagenesis experiments demonstrated that Ser12, Asn52, Arg94, and Asn113 residues variants caused an approximately 1.7- to 4.6-fold reduction in OfurPBP3 affinity for Z12- and E12-14:OAc, and a 2.7- to 8.4-fold decrease in affinity towards E11- and Z11-14:OAc.ConclusionsFive PBPs of O. furnacalis play important functions in Ostrinia pheromones binding. These four amino acids may play a role in binding of sex pheromone, but this study does not address questions regarding specific response between males of O. furnacalis and O. nubilalis. Additional studies are required determine the role, if any, PBPs play in the evolution of sex pheromone communication.

【 授权许可】

CC BY   
© The Author(s) 2017