Prokaryotic Expression and Binding Characteristics of Odor-Binding Protein GqinOBP10 in Gynaephora qinghaiensis

<i>Gynaephora qinghaiensis</i> is a major grassland pest common in the alpine meadows of the western plateau of China, and its biological behavior is affected by the synergy of a variety of chemicals in the environment. OBPs can dissolve and transport odor molecules such as volatile plant compounds through lymphatic fluid, which plays an important olfactory-to-olfactory role. However, the specific function of OBPs in the interaction mechanism between moths and volatile plant compounds is still unknown. The purpose of this study was to analyze the binding characteristics of GqinOBP10 and its volatile plant compounds in moths and to explore its role in the olfactory perception mechanism of moths so as to study the corresponding target ligands and achieve green control. The purified GqinOBP10 was subjected to fluorescence competitive binding to eight ligands. The 3D modeling of GqinOBP10 was carried out by the SWISS-MODEL website, and the molecular docking was carried out by Autodock 4.2.6 software, and the binding of GqinOBP10 to eight ligands was simulated and verified. The results showed that the cloned strain with the full length of GqinOBP10 was cloned. The fluorescence competition binding results showed that GqinOBP10 had strong binding ability to eight volatile plant compounds, among which the binding ability to 2-Amino-1-phenylethanol and 2-Oleoylglycerol was the strongest, and had high binding ability with the other six ligands. The molecular docking results showed that the binding energy of GqinOBP10 and eight odorant molecules was negative, and all of them could form 1~4 hydrogen bond for binding, among which the binding performance with 2-Oleoylglycerol was the best. The findings suggest that <i>dsOBP10</i> injection leads to a notable decrease in both the expression levels of <i>GqinOBP10</i> and the antennal potential response in male and female tissues. This indicates that GqinOBP10 is likely crucial for the localization and recognition of host plants in <i>G. qinghaiensis</i>. By silencing <i>GqinOBP10</i>, the olfactory perception of host volatiles is significantly impaired, highlighting the protein's importance in the caterpillars' ability to detect and respond to their environment. These insights provide a valuable basis for developing targeted attractants, potentially enhancing pest management strategies by manipulating olfactory cues in these caterpillars. Further research could explore the specific mechanisms by which GqinOBP10 influences olfactory perception and host plant selection.

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Journal
International Journal of Molecular Sciences
Published
2025-10-29
DOI
https://doi.org/10.3390/ijms262110502
Primary Topic
Neurobiology and Insect Physiology Research
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article
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article

Prokaryotic Expression and Binding Characteristics of Odor-Binding Protein GqinOBP10 in Gynaephora qinghaiensis

Yuantao Zhou, Youpeng Lai, Zhanling Liu, Haibin Han et al.
International Journal of Molecular Sciences
Neurobiology and Insect Physiology Research
article

Prokaryotic Expression and Binding Characteristics of Odor-Binding Protein GqinOBP10 in Gynaephora qinghaiensis

Yuantao Zhou, Youpeng Lai, Zhanling Liu, Haibin Han, Shujing Gao, Dier Tang
article en

Abstract

<i>Gynaephora qinghaiensis</i> is a major grassland pest common in the alpine meadows of the western plateau of China, and its biological behavior is affected by the synergy of a variety of chemicals in the environment. OBPs can dissolve and transport odor molecules such as volatile plant compounds through lymphatic fluid, which plays an important olfactory-to-olfactory role. However, the specific function of OBPs in the interaction mechanism between moths and volatile plant compounds is still unknown. The purpose of this study was to analyze the binding characteristics of GqinOBP10 and its volatile plant compounds in moths and to explore its role in the olfactory perception mechanism of moths so as to study the corresponding target ligands and achieve green control. The purified GqinOBP10 was subjected to fluorescence competitive binding to eight ligands. The 3D modeling of GqinOBP10 was carried out by the SWISS-MODEL website, and the molecular docking was carried out by Autodock 4.2.6 software, and the binding of GqinOBP10 to eight ligands was simulated and verified. The results showed that the cloned strain with the full length of GqinOBP10 was cloned. The fluorescence competition binding results showed that GqinOBP10 had strong binding ability to eight volatile plant compounds, among which the binding ability to 2-Amino-1-phenylethanol and 2-Oleoylglycerol was the strongest, and had high binding ability with the other six ligands. The molecular docking results showed that the binding energy of GqinOBP10 and eight odorant molecules was negative, and all of them could form 1~4 hydrogen bond for binding, among which the binding performance with 2-Oleoylglycerol was the best. The findings suggest that <i>dsOBP10</i> injection leads to a notable decrease in both the expression levels of <i>GqinOBP10</i> and the antennal potential response in male and female tissues. This indicates that GqinOBP10 is likely crucial for the localization and recognition of host plants in <i>G. qinghaiensis</i>. By silencing <i>GqinOBP10</i>, the olfactory perception of host volatiles is significantly impaired, highlighting the protein's importance in the caterpillars' ability to detect and respond to their environment. These insights provide a valuable basis for developing targeted attractants, potentially enhancing pest management strategies by manipulating olfactory cues in these caterpillars. Further research could explore the specific mechanisms by which GqinOBP10 influences olfactory perception and host plant selection.

International Journal of Molecular SciencesVol. 26(21)
Qinghai University (CN), Institute of Plant Protection (CN), Chinese Academy of Agricultural Sciences (CN), Institute of Grassland Research (CN)
Openalex Percentile: Top 66%
Neurobiology and Insect Physiology Research
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