Binding Properties of Odorant-Binding Protein 4 of Tirathaba rufivena to Areca catechu Volatiles

Odorant-binding proteins (OBPs) play a key role in the olfactory system and are essential for mating and oviposition host selection. Tirathaba rufivena, a serious lepidopterous insect pest of the palm area in recent years, has threatened cultivations of Areca catechu in Hainan. Female-biased odorant-binding protein 4 of T. rufivena (TrufOBP4) expression was hypothesized to participate in the process of oviposition host recognition and localization. In this study, we cloned and analyzed the cDNA sequence of TrufOBP4. The predicted mature protein TrufOBP4 is a small, soluble, secretory protein and belongs to a classic OBP subfamily. Fluorescence binding assay results showed that TrufOBP4 had high binding abilities with the host plant volatiles, octyl methoxycinnamate, dibutyl phthalate, myristic acid and palmitic acid. These four components tend to dock in the same binding pocket based on the molecular docking result. The interactions and contributions of key amino acid residues were also characterized. This research provides evidence that TrufOBP4 might participate in the chemoreception of volatile compounds from inflorescences of A. catechu and can contribute to the integrated management of T. rufivena.

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Molecular and Functional Characterization of One Odorant-Binding Protein Gene OBP3 in Bemisia tabaci (Hemiptera: Aleyrodidae)

Journal of Economic Entomology ◽

10.1093/jee/toz248 ◽

2019 ◽

Cited By ~ 1

Author(s):

Ran Wang ◽

Yuan Hu ◽

Peiling Wei ◽

Cheng Qu ◽

Chen Luo

Keyword(s):

Host Plant ◽

Bemisia Tabaci ◽

Binding Protein ◽

Insect Pest ◽

Critical Role ◽

Functional Characterization ◽

Odorant Binding Protein ◽

Binding Characteristics ◽

And Function ◽

Odorant Binding

Abstract Odorant binding proteins (OBPs) of insects play a critical role in chemical perceptions and choice of insect host plant. Bemisia tabaci is a notorious insect pest which can damage more than 600 plant species. In order to explore functions of OBPs in B. tabaci, here we investigated binding characteristics and function of odorant-binding protein 3 in B. tabaci (BtabOBP3). The results indicated that BtabOBP3 shows highly similar sequence with OBPs of other insects, including the typical signature motif of six cysteines. The recombinant BtabOBP3 protein was obtained, and the evaluation of binding affinities to tested volatiles of host plant was conducted, then the results indicated that β-ionone had significantly higher binding to BtabOBP3 among other tested plant volatiles. Furthermore, silencing of BtabOBP3 significantly altered choice behavior of B. tabaci to β-ionone. In conclusion, it has been demonstrated that BtabOBP3 exerts function as one carrier of β-ionone and the results could be contributed to reveal the mechanisms of choosing host plant in B. tabaci.

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Structure of an Odorant-Binding Protein from the Mosquito Aedes aegypti Suggests a Binding Pocket Covered by a pH-Sensitive “Lid”

PLoS ONE ◽

10.1371/journal.pone.0008006 ◽

2009 ◽

Vol 4 (11) ◽

pp. e8006 ◽

Cited By ~ 78

Author(s):

Ney Ribeiro Leite ◽

Renata Krogh ◽

Wei Xu ◽

Yuko Ishida ◽

Jorge Iulek ◽

...

Keyword(s):

Aedes Aegypti ◽

Binding Protein ◽

Binding Pocket ◽

Ph Sensitive ◽

Odorant Binding Protein ◽

Odorant Binding

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Identification and Expression Profiles of 14 Odorant-Binding Protein Genes From Pieris rapae (Lepidoptera: Pieridae)

Journal of Insect Science ◽

10.1093/jisesa/ieaa087 ◽

2020 ◽

Vol 20 (5) ◽

Author(s):

Mao-Ye Li ◽

Xiu-Yun Jiang ◽

Yu-Zhe Qi ◽

Yuan-Jie Huang ◽

Shi-Guang Li ◽

...

Keyword(s):

Pieris Rapae ◽

Binding Protein ◽

Expression Profiles ◽

Insect Pest ◽

Amino Acid Identity ◽

Odorant Binding Protein ◽

Olfactory Communication ◽

High Amino Acid ◽

Solid Foundation ◽

Odorant Binding

Abstract The small white butterfly, Pieris rapae (L.), is an important insect pest of Brassica crops. This species utilize olfactory cues to find their hosts and mates. However, the molecular mechanism underlying the olfactory perception in this species remains unclear. Here, we identified 14 odorant-binding proteins (OBP) genes—essential for insect olfaction—in P. rapae by exploring a previously published transcriptome dataset. Proteins encoded by all of these genes contain N-terminal signal peptides and six positionally conserved cysteine residues, which are characteristic of insect OBPs. These OBPs displayed high amino acid identity with their respective orthologs in other lepidopterans, and several conserved motifs were identified within these OBPs. Phylogenetic analysis showed that these OBPs were well segregated from each other and clustered into different branches. PrapOBP1 and PrapOBP2 were clustered into the ‘general odorant-binding protein’ clade, and PrapOBP3 and PrapOBP4 fall into the ‘pheromone-binding protein’ clade. The 14 OBP genes were located on seven genomic scaffolds. Of these, PrapOBP1, 2, 3, and 4 were located on scaffold332, whereas PrapOBP5, 6, 7, 8, and 9 were located on scaffold116. Ten of the 14 genes had antenna-biased expression. Of these, PrapOBP1, 2, 4, and 13 were enriched in male antennae, whereas PrapOBP7 and PrapOBP10 were female-biased. Our findings suggest that these OBPs may be involved in olfactory communication. To the best of our knowledge, this is the first report on the identification and characterization of OBPs in P. rapae, and our findings provide a solid foundation for studying the functions of these genes.

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