Odorant-binding proteins display high affinities for behavioral attractants and repellents in the natural predator Chrysopa pallens

• Published in: Comparative biochemistry and physiology. Part A, Molecular & integrative physiology Molecular & integrative physiology, 2015-07, Vol.185, p.51-57
• Main Authors: Li, Zhao-Qun, Zhang, Shuai, Luo, Jun-Yu, Wang, Si-Bao, Dong, Shuang-Lin, Cui, Jin-Jie
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animals; Arthropod Antennae - metabolism; Behavioral trial; Chemotactic Factors - pharmacology; Chrysopa pallens; Conserved Sequence; Farnesol - pharmacology; Fluorescence binding assay; Gene Expression; Insect Proteins - chemistry; Insect Proteins - genetics; Insect Proteins - metabolism; Insect Repellents - pharmacology; Insecta - drug effects; Insecta - genetics; Insecta - physiology; Molecular Sequence Data; Odorant-binding protein; Organ Specificity; Phylogeny; Protein Binding; Receptors, Odorant - chemistry; Receptors, Odorant - genetics; Receptors, Odorant - metabolism; Sequence Homology, Amino Acid; Smell
• ISSN: 1095-6433; 1531-4332
• DOI: 10.1016/j.cbpa.2015.03.011

Chrysopa pallens is an important natural predator of various pests in many different cropping systems. Understanding the sophisticated olfactory system of insect antennae is crucial for studying the physiological bases of olfaction and could also help enhance the effectiveness of C. pallens in biological control. However, functional studies of the olfactory genes in C. pallens are still lacking. In this study, we cloned five odorant-binding protein (OBP) genes from C. pallens (CpalOBPs). Quantitative RT-PCR results indicated that the five CpalOBPs had different tissue expression profiles. Ligand-binding assays showed that farnesol, farnesene, cis-3-hexenyl hexanoate, geranylacetone, beta-ionone, octyl aldehyde, decanal, nerolidol (Ki