Identification of a New Pheromone-Binding Protein in the Antennae of a Geometrid Species and Preparation of Its Antibody to Analyze the Antennal Proteins of Moths Secreting Type II Sex Pheromone Components

Watanabe, Hayaki; Tabunoki, Hiroko; Miura, Nami; Matsui, Aya; Satō, Ryōichi; Ando, Tetsu

doi:10.1271/bbb.90029

Cited by 10 publications

(6 citation statements)

References 16 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…These results suggested a strong interaction between HcunPBPs and the pheromone components. In addition, the binding models showed that some crucial hydrophobic residues might play a beneficial role in the binding of HcunPBPs to their sex pheromone components, including 12…”

Section: ■ Resultsmentioning

confidence: 96%

“…Recently, Löfstedt et al (2016) revised and extended the known classifications of lepidopteran pheromones by defining another two pheromone types, type 0 and type III pheromones . To date, however, the characterized PBPs reported in moths are mainly responsible for detection of type I sex pheromones. ,, In contrast, PBPs for type II sex pheromones have only been reported from a few species, including Ascotis selenaria cretacea, Operophtera brumata, and Ectropis obliqua. − …”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Functional Disparity of Three Pheromone-Binding Proteins to Different Sex Pheromone Components in Hyphantria cunea (Drury)

Zhang

Mang

Liao

et al. 2020

J. Agric. Food Chem.

View full text Add to dashboard Cite

Hyphantria cunea (Drury) is a destructive invasive pest species in China that uses type II sex pheromone components. To date, however, the binding mechanisms of its sex pheromone components to their respective pheromone-binding proteins (HcunPBPs 1/2/3) have not been explored. In the current study, all three HcunPBPs were expressed in the antennae of both sexes. The prokaryotic expression and ligand binding assays were employed to study the binding of the moth’s four sex pheromone components, including two aldehydes and two epoxides, and 24 plant volatiles to the HcunPBPs. Our results showed that the abilities of these HcunPBPs to bind to the aldehydes were significantly different from binding to the epoxides. These three HcunPBPs also selectively bind to some of the plant volatiles tested. Our molecular docking results indicated that some crucial hydrophobic residues might play a role in the binding of HcunPBPs to their sex pheromone components. Three HcunPBPs have different selectivities for pheromone components with both major and minor structural differences. Our study provides a fundamental insight into the olfactory mechanism of moths at the molecular level, especially for moth species that use various type II pheromone components.

show abstract

Section: ■ Resultsmentioning

confidence: 96%

Section: Introductionmentioning

confidence: 99%

Functional Disparity of Three Pheromone-Binding Proteins to Different Sex Pheromone Components in Hyphantria cunea (Drury)

Zhang

Mang

Liao

et al. 2020

J. Agric. Food Chem.

View full text Add to dashboard Cite

show abstract

“…Type II pheromones have mainly been found in the moth superfamilies Geometroidea and Noctuoidea [ 17 ], but olfactory genes for type II pheromones were only identified in the geometrids A . selenaria cretacea [ 68 , 69 ] and O . brumata [ 56 ] and the erebids L .…”

Section: Discussionmentioning

confidence: 99%

Antennal transcriptome analysis of the piercing moth Oraesia emarginata (Lepidoptera: Noctuidae)

et al. 2017

View full text Add to dashboard Cite

The piercing fruit moth Oraesia emarginata is an economically significant pest; however, our understanding of its olfactory mechanisms in infestation is limited. The present study conducted antennal transcriptome analysis of olfactory genes using real-time quantitative reverse transcription PCR analysis (RT-qPCR). We identified a total of 104 candidate chemosensory genes from several gene families, including 35 olfactory receptors (ORs), 41 odorant-binding proteins, 20 chemosensory proteins, 6 ionotropic receptors, and 2 sensory neuron membrane proteins. Seven candidate pheromone receptors (PRs) and 3 candidate pheromone-binding proteins (PBPs) for sex pheromone recognition were found. OemaOR29 and OemaPBP1 had the highest fragments per kb per million fragments (FPKM) values in all ORs and OBPs, respectively. Eighteen olfactory genes were upregulated in females, including 5 candidate PRs, and 20 olfactory genes were upregulated in males, including 2 candidate PRs (OemaOR29 and 4) and 2 PBPs (OemaPBP1 and 3). These genes may have roles in mediating sex-specific behaviors. Most candidate olfactory genes of sex pheromone recognition (except OemaOR29 and OemaPBP3) in O. emarginata were not clustered with those of studied noctuid species (type I pheromone). In addition, OemaOR29 was belonged to cluster PRIII, which comprise proteins that recognize type II pheromones instead of type I pheromones. The structure and function of olfactory genes that encode sex pheromones in O. emarginata might thus differ from those of other studied noctuids. The findings of the present study may help explain the molecular mechanism underlying olfaction and the evolution of olfactory genes encoding sex pheromones in O. emarginata.

show abstract

“…The female sex pheromone blend of G. molesta comprises of four components 18 : ( Z )-8-dodecenyl acetate, ( E )-8-dodecenyl acetate, ( Z )-8-dodecenyl alcohol and 1-dodecanol. The accumulated studies suggest that multiple PBPs were found in a single species, which strongly implies functional differentiation of these PBPs, possibly in discrimination among pheromone components 9 , 19 – 21 . In moth, whose PBPs were identified usually contain three PBP genes 22 – 26 .…”

Section: Introductionmentioning

confidence: 96%

Molecular and Functional Characterization of pheromone binding protein 1 from the Oriental Fruit Moth, Grapholita molesta (Busck)

Zhang

Chen

et al. 2018

Sci Rep

View full text Add to dashboard Cite

Pheromone binding protein (PBP) is thought primarily to bind and transport the sex pheromone in moths. The accumulated studies suggest that three PBPs were identified in moth species. In Grapholita molesta, the functions of GmolPBP2 and GmolPBP3 have been previously studied. However, the function of GmolPBP1 is still unclear. Furthermore, the Cydia pomonella sex pheromone Codlemone can act as a sex pheromone synergist of G. molesta. In C. pomonella, CpomPBP1 specifically bind the Codlemone. CpomPBP1 displays high identity with GmolPBP1 (70%), indicating that the two PBPs may share a similar 3D structure thus can bind the similar or same ligands. In this study, we explored the molecular and functional characterization of GmolPBP1. GmolPBP1, bearing the typical characteristics of Lepidopteran odorant binding proteins, was closest phylogenetically to CpomPBP1. Binding studies demonstrated that GmolPBP1 exhibited strong binding affinities with (Z)-8-dodecenyl alcohol, 1-dodecanol and Codlemone. Molecular docking showed that GmolPBP1 has different ligand recognition mechanism for the three ligands. Our results suggest that GmolPBP1 functions as recognizer of (Z)-8-dodecenyl alcohol and 1-dodecanol of the female sex pheromone blend, and may be the potential transporter of Codlemone, which contributes to the synergism of the pheromone response of G. molesta by Codlemone.

show abstract

Identification of a New Pheromone-Binding Protein in the Antennae of a Geometrid Species and Preparation of Its Antibody to Analyze the Antennal Proteins of Moths Secreting Type II Sex Pheromone Components

Cited by 10 publications

References 16 publications

Functional Disparity of Three Pheromone-Binding Proteins to Different Sex Pheromone Components in Hyphantria cunea (Drury)

Functional Disparity of Three Pheromone-Binding Proteins to Different Sex Pheromone Components in Hyphantria cunea (Drury)

Antennal transcriptome analysis of the piercing moth Oraesia emarginata (Lepidoptera: Noctuidae)

Molecular and Functional Characterization of pheromone binding protein 1 from the Oriental Fruit Moth, Grapholita molesta (Busck)

Contact Info

Product

Resources

About