{"title":"香味结合蛋白基因FoccOBP9的分子特征和表达谱","authors":"Zhike Zhang","doi":"10.1017/S0007485324000683","DOIUrl":null,"url":null,"abstract":"<p><p>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. <i>Frankliniella occidentalis</i> 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 <i>F. occidentalis</i>. To identify the OBP gene of <i>F. occidentalis</i> 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 <i>FoccOBP9</i> 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 <i>F</i>. <i>occidentalis</i>.</p>","PeriodicalId":9370,"journal":{"name":"Bulletin of Entomological Research","volume":" ","pages":"74-83"},"PeriodicalIF":1.6000,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Molecular characterisation and expression profiles of an odorant-binding proteins gene (FoccOBP9) from <i>Frankliniella occidentalis</i>.\",\"authors\":\"Zhike Zhang\",\"doi\":\"10.1017/S0007485324000683\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>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. <i>Frankliniella occidentalis</i> 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 <i>F. occidentalis</i>. To identify the OBP gene of <i>F. occidentalis</i> 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 <i>FoccOBP9</i> 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 <i>F</i>. <i>occidentalis</i>.</p>\",\"PeriodicalId\":9370,\"journal\":{\"name\":\"Bulletin of Entomological Research\",\"volume\":\" \",\"pages\":\"74-83\"},\"PeriodicalIF\":1.6000,\"publicationDate\":\"2025-02-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Bulletin of Entomological Research\",\"FirstCategoryId\":\"97\",\"ListUrlMain\":\"https://doi.org/10.1017/S0007485324000683\",\"RegionNum\":3,\"RegionCategory\":\"农林科学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"ENTOMOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Bulletin of Entomological Research","FirstCategoryId":"97","ListUrlMain":"https://doi.org/10.1017/S0007485324000683","RegionNum":3,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"ENTOMOLOGY","Score":null,"Total":0}
Molecular characterisation and expression profiles of an odorant-binding proteins gene (FoccOBP9) from Frankliniella occidentalis.
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.
期刊介绍:
Established in 1910, the internationally recognised Bulletin of Entomological Research aims to further global knowledge of entomology through the generalisation of research findings rather than providing more entomological exceptions. The Bulletin publishes high quality and original research papers, ''critiques'' and review articles concerning insects or other arthropods of economic importance in agriculture, forestry, stored products, biological control, medicine, animal health and natural resource management. The scope of papers addresses the biology, ecology, behaviour, physiology and systematics of individuals and populations, with a particular emphasis upon the major current and emerging pests of agriculture, horticulture and forestry, and vectors of human and animal diseases. This includes the interactions between species (plants, hosts for parasites, natural enemies and whole communities), novel methodological developments, including molecular biology, in an applied context. The Bulletin does not publish the results of pesticide testing or traditional taxonomic revisions.