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Molecular characterisation and expression profiles of an odorant-binding proteins gene (FoccOBP9) from Frankliniella occidentalis

Published online by Cambridge University Press:  09 January 2025

Zhike Zhang Open the ORCID record for Zhike Zhang [Opens in a new window]
Zhike Zhang*
Affiliation:
Ningxia Academy of Agriculture and Forestry Sciences, Institute of Plant Protection, Yinchuan, China
*
Corresponding author: Zhike Zhang; Email: zhangzhike98@163.com
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Abstract

Insect odorant-binding proteins (OBPs) are the key proteins in insect olfactory perception and play an important role in the perception and discrimination of insects. Frankliniella occidentalis is a polyphagous pest and seriously harms the quality and yield of fruits, flowers and crops worldwide. Therefore, the discovery of OBPs has greatly improved the understanding of behavioural response that mediates the chemoreception of F. occidentalis. To identify the OBP gene of F. occidentalis and its sequence and expression, rapid amplification cDNA ends (RACE) and qRT-PCR reaction system were performed. The results showed that the sequence of FoccOBP9 gene was 846 bp and the reading frame was 558 bp, encoding 185 amino acid residues, a 3′ non-coding region of 195 bp and a 5′ non-coding region of 93 bp.The molecular weight of the protein was about 20.08 kDa, and the isoelectric point was 8.89. FoccOBP9 was similar to AtumGOBP and CnipOBP2 (30%), followed by BdorGOBP, DficGOBP, DsuzGOBP, AalbOBP38, CmarOBP6 and SexiOBP. Phylogenetic analysis of the FoccOBP9 demonstrated that the FoccOBP9 had a relatively close evolutionary relationship with SgreOBP1, AtumGOBP, HeleOBP3, CbowOBP17, CnipOBP2 and CpalOBP2. The prediction of secondary structure showed that FoccOBP9 protein contained 135 amino acid residues forming α-helix, 91 amino acid residues forming β-sheets and 24 amino acid residues forming β-turning. However, three-dimensional structure prediction showed that the FoccOBP9 protein skeleton was composed of six α-helices and the loops connecting these helices. Dynamic observation of the three-dimensional structure revealed that five α-helices (α1, α2, α4, α5, α6) were found in the structure. The expression profiles analysis revealed that FoccOBP9 are highly abundant in antenna significantly, followed by the head and belly, and almost no expression in the chest and foot. Therefore, the identification and analysis of OBP may be useful for monitoring and limiting the damage of F. occidentalis.

Keywords

expressionF. occidentalisodorant-binding proteinssequence analysisstructure prediction
Type
Research Paper
Information
Bulletin of Entomological Research , First View , pp. 1 - 10
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Copyright © The Author(s), 2025. Published by Cambridge University Press

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