Discrimination of Oviposition Deterrent Volatile β-Ionone by Odorant-Binding Proteins 1 and 4 in the Whitefly Bemisia tabaci

Biomolecules

Jiahui Tian¹  Cheng Qu¹  Du Li¹  Fengqi Li¹  Chen Luo¹  Youssef Dewer²  Zhen Yang³ 

[1]Beijing Key Laboratory of Environment Friendly Management on Fruit Diseases and Pests in North China, Institute of Plant and Environment Protection, Beijing Academy of Agriculture and Forestry Sciences, Beijing 100097, China

[2]Bioassay Research Department, Central Agricultural Pesticide Laboratory, Sabahia Plant Protection Research Station, Agricultural Research Center, Alexandria 21616, Egypt

[3]Tianjin University of Traditional Chinese Medicine, Tianjin 300000, China

关键词: bemisia tabaci;    odorant-binding protein;    competitive binding;    β-ionone;   

DOI  :  10.3390/biom9100563

来源: DOAJ

【 摘 要 】

: The whitefly, Bemisia tabaci, is an important invasive economic pest of agricultural crops worldwide. β-ionone has a significant oviposition repellent effect against B. tabaci, but the olfactory molecular mechanism of this insect for recognizing β-ionone is unclear. To clarify the binding properties of odorant-binding proteins (OBPs) with β-ionone, we performed gene cloning, evolution analysis, bacterial expression, fluorescence competitive binding assay, and molecular docking to study the binding function of OBP1 and OBP4 on β-ionone. The results showed that after the OBP1 and OBP4 proteins were recombined, the compound β-ionone exhibited a reduction in the fluorescence binding affinity to <50%, with a dissociation constant of 5.15 and 3.62 μM for OBP1 and OBP4, respectively. Our data indicate that β-ionone has high affinity for OBP1 and OBP4, which play a crucial role in the identification of oviposition sites in B. tabaci. The findings of this study suggest that whiteflies employ β-ionone compound in the selection of the suitable egg-laying sites on host plants during the oviposition behavior.

【 授权许可】

Unknown