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« Previous Abstract"Indoor exposure levels and risk assessment of volatile organic compounds in residences, schools, and offices in China from 2000 to 2021: A systematic review"    Next AbstractFunctional differentiation of pheromone-binding proteins in the common cutworm Spodoptera litura »

Comp Biochem Physiol B Biochem Mol Biol


Title:Binding properties of pheromone-binding protein 1 from the common cutworm Spodoptera litura
Author(s):Liu NY; He P; Dong SL;
Address:"Education Ministry Key Laboratory of Integrated Management of Crop Diseases and Pests, College of Plant Protection, Nanjing Agricultural University, Nanjing 210095, China"
Journal Title:Comp Biochem Physiol B Biochem Mol Biol
Year:2012
Volume:20111130
Issue:4
Page Number:295 - 302
DOI: 10.1016/j.cbpb.2011.11.007
ISSN/ISBN:1879-1107 (Electronic) 1096-4959 (Linking)
Abstract:"Pheromone-binding proteins (PBPs) were formerly thought to act as passive pheromone carriers. However, recent studies, particularly in Drosophila melanogaster, suggest that PBPs are involved in the recognition of semiochemicals, thus making ligand-binding studies more meaningful. Previously, we cloned three PBPs from Spodoptera litura (Slit), and showed that SlitPBP1 is much more abundant than the other two, particularly in male antennae. To investigate the ligand specificity of SlitPBP1, we expressed the protein in a bacterial system and performed binding experiments with the three components of the specific sex pheromones (Z9-14:Ac, Z9,E11-14:Ac and Z9,E12-14:Ac), as well as with 26 volatile ligands. The results indicated that SlitPBP1 bound all three sex pheromone components with dissociation constants between 0.6 and 1.1 muM. The same protein also bound with comparable affinities several pheromone analogs, but not plant volatiles. The presence of a double bond was the most important element for a strong binding, while its position and configuration also affected the affinity. Finally, the binding of pheromone components is strongly affected by pH, showing a critical pH value corresponding to isoelectric point of the protein. This suggests that a pH-dependent conformational mechanism might exist in SlitPBP1 for pheromone binding and release"
Keywords:"Animals Carrier Proteins/*metabolism Chromatography, Affinity Cloning, Molecular Computational Biology DNA Primers/genetics DNA, Complementary/genetics Escherichia coli Hydrogen-Ion Concentration Insect Proteins/*metabolism Isoelectric Point *Models, Mole;"
Notes:"MedlineLiu, Nai-Yong He, Peng Dong, Shuang-Lin eng Research Support, Non-U.S. Gov't England 2011/12/07 Comp Biochem Physiol B Biochem Mol Biol. 2012 Apr; 161(4):295-302. doi: 10.1016/j.cbpb.2011.11.007. Epub 2011 Nov 30"

 
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