Expression, affinity, and binding mode analysis of antennal-binding protein X in the variegated cutworm Peridroma saucia (Hübner)

The variegated cutworm Peridroma saucia (Hübner) is a worldwide pest that causes serious damage to many crops. Odorant-binding proteins (OBPs) are small soluble proteins involved in the first step of odorant reception. In moths, antennal-binding protein Xs (ABPXs) represent a main subfamily of class...

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Bibliographic Details
Published in:International journal of biological macromolecules 2023-07, Vol.242 (Pt 1), p.124671-124671, Article 124671
Main Authors: Dong, Jun-Feng, Sun, Ya-Lan, Wang, Ke, Guo, Hao, Wang, Shao-Li
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Antennal binding protein X
Binding properties
Carrier Proteins - chemistry
Female
Insect Proteins - metabolism
Male
Molecular Docking Simulation
Moths - genetics
Peridroma saucia
Receptors, Odorant - chemistry
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Summary:The variegated cutworm Peridroma saucia (Hübner) is a worldwide pest that causes serious damage to many crops. Odorant-binding proteins (OBPs) are small soluble proteins involved in the first step of odorant reception. In moths, antennal-binding protein Xs (ABPXs) represent a main subfamily of classic OBPs. However, their functions remain unclear. Here, we cloned the ABPX gene from the antennae of P. saucia. RT-qPCR and western-blot analyses showed that PsauABPX is antenna-predominant and male-biased. Further temporal expression investigation indicated that the expression of PsauABPX started 1 day before eclosion and reached the highest 3 days after eclosion. Next, fluorescence binding assays revealed that recombinant PsauABPX had high binding affinities with P. saucia female sex pheromone components Z11–16: Ac and Z9–14: Ac. Then, molecular docking, molecular dynamics simulation, and site-directed mutagenesis were employed to identify key amino acid residues involved in the binding of PsauABPX to Z11–16: Ac and Z9–14: Ac. The results demonstrated that Val-32, Gln-107 and Tyr-114 are essential for the binding to both sex pheromones. This study not only give us insight into the function and binding mechanism of ABPXs in moths, but could also be used to explore novel strategies to control P. saucia.
ISSN:0141-8130
1879-0003
DOI:10.1016/j.ijbiomac.2023.124671