title: Binding interaction between a queen pheromone component HOB and pheromone binding protein ASP1 of Apis cerana.
abstract: The honeybee's social behavior is closely related to the critical response to pheromone, while pheromone binding proteins (PBPs) play an important role in binding and transferring those pheromones. Here we report one known PBP, antennal special protein 1(ASP1), which has high affinity with a queen mandibular pheromone component, methyl-p-hydroxybenzoate (HOB). In this study, multiple fluorescent spectra, UV absorption spectra, circular dichroism (CD) spectra and molecular docking analysis were combined to clarify the binding process. Basically, fluorescence intensity of ASP1 could be considerably quenched by HOB with an appropriate interaction distance (3.1 nm), indicating that a complex, which is more stable in lower temperature, was formed. The fact ΔH < 0, ΔS < 0, by thermodynamic analysis, indicated the van der Waals and hydrogen bond as main driving force. Moreover, synchronous fluorescence spectra and CD spectra analysis showed the change of partial hydrophilicity of ASP1 and the increase of α-helix after HOB addition. In conclusion, ASP1 can strongly and spontaneously interact with HOB. But the binding ability decreases with the rise of temperature, which may be necessary for sufficient social stability of hives. This study provides elucidation of the detailed binding mechanism and potential physicochemical basis of thermal stability to the social behavior of honeybee.
authors.affiliation: Zhejiang Provincial Key Laboratory of Biometrology and Inspection & Quarantine, College of Life Sciences, China Jiliang University, Hangzhou 310018, China.
authors.forename: Chen
authors.initials: C
authors.lastname: Weng
authors.affiliation: Zhejiang Provincial Key Laboratory of Biometrology and Inspection & Quarantine, College of Life Sciences, China Jiliang University, Hangzhou 310018, China.
authors.forename: Yuxia
authors.initials: Y
authors.lastname: Fu
authors.affiliation: College of Chemical Engineering, Zhejiang University of Technology, Hangzhou 310014, China.
authors.forename: Hongtao
authors.initials: H
authors.lastname: Jiang
authors.affiliation: College of Environmental and Resource Sciences, Zhejiang University, Hangzhou 310058, China.
authors.forename: Shulin
authors.initials: S
authors.lastname: Zhuang
authors.affiliation: Zhejiang Provincial Key Laboratory of Biometrology and Inspection & Quarantine, College of Life Sciences, China Jiliang University, Hangzhou 310018, China. Electronic address: hlli@cjlu.edu.cn.
authors.forename: Hongliang
authors.initials: H
authors.lastname: Li
mesh_terms: D000818:Animals; D001516:Bees; D002352:Carrier Proteins / Q000737:chemistry / Q000378:metabolism*; D002942:Circular Dichroism; D057927:Hydrophobic and Hydrophilic Interactions; D062385:Hydroxybenzoates / Q000737:chemistry* / Q000378:metabolism; D019476:Insect Proteins / Q000737:chemistry / Q000378:metabolism*; D062105:Molecular Docking Simulation; D010675:Pheromones / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D017433:Protein Structure, Secondary; D013816:Thermodynamics
chemical_list: D002352:Carrier Proteins; D062385:Hydroxybenzoates; D019476:Insect Proteins; D010675:Pheromones; C121271:antennal-specific protein 1, Apis mellifera
keywords: Circular dichroism (CD) spectra; Fluorescence spectroscopy; Methyl-p-hydroxybenzoate (HOB); Molecular docking; Pheromone binding protein; Queen mandibular pheromone component