Functional disparity of four pheromone-binding proteins from the plum fruit moth Grapholita funebrana Treitscheke in detection of sex pheromone components

Li, Linlin; Xu, Bo; Li, Chunqin; Li, Boliao; Luo, Kun; Li, Guangwei; Xiu-lin, Chen

doi:10.1016/j.ijbiomac.2022.11.186

Cited by 5 publications

(5 citation statements)

References 72 publications

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“…The competitive binding results are exhibited in Table 2 and Figure 6. SvelOBP1 was found to be able to bind to 24 compounds (K i values < 16 µM) [41,44] among the 43 tested odorants. SvelOBP1 exhibited high binding affinities to ten esters (K i values from 6.66 ± 0.03 to 12.90 ± 0.75 µM) and seven alcohols (K i values from 7.98 ± 0.08 to 12.83 ± 0.12 µM) (Figure 6A,B), and it could bind as well to five terpenoids (K i values from 8.73 ± 0.09 to 12.10 ± 0.06 µM) (Figure 6C).…”

Section: Fluorescence Competitive Binding Analyses Of Svelobp1mentioning

confidence: 97%

“…To measure the protein binding affinities, each ligand solution (1 mM) was added as aliquots into the 2 µM SvelOBP1/1-NPN mixture to obtain final concentrations ranging from 0 to 16 µM to replace 1-NPN, and then, the competitive binding curves were plotted based on the fluorescence intensity values of the three replicates. The dissociation constants K 1-NPN of 1-NPN to SvelOBP1 were calculated by GraphPad Prism 8.0 software with non-linear regression for the one site-specific binding method [41]. The inhibitory constant (K i ) of each ligand binding to SvelOBP1 was calculated with Equation (1) [22].…”

Section: Competitive Fluorescence Binding Assaymentioning

confidence: 99%

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The Sequence Characteristics and Binding Properties of the Odorant-Binding Protein SvelOBP1 from Sympiezomias velatus (Coleoptera: Curculionidae) to Jujube Volatiles

Zhai,

Zhang,

Tian

et al. 2024

Life

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Sympiezomias velatus (Chevrolat) (Coleoptera: Curculionidae) has caused serious damage on jujube trees (Ziziphus jujuba Mill) in northern China. Semiochemicals emerging from the host are essential in the process of insects identifying and localizing the host. The highly expressed odorant-binding protein 1 of S. velatus (SvelOBP1) was assumed to play a possible role in the recognition of host volatiles. In this study, SvelOBP1 was cloned based on the antennal transcriptome of S. velatus. The recombinant SvelOBP1 protein was expressed in Escherichia coli and purified by Ni-NTA resin. The predicted protein SvelOBP1 belonged to a classic OBP subfamily. The expression patterns revealed that SvelOBP1 was mainly expressed in the antennae of both males and females, whereas the expression of SvelOBP1 in other body parts could be neglected. The fluorescence binding assay indicated that SvelOBP1 displayed very strong binding affinities to dibutyl benzene-1,2-dicarboxylate and (Z)-hex-3-en-1-ol (Ki = 6.66 ± 0.03 and 7.98 ± 0.06 μM). The molecular docking results showed that residues Trp114, Phe115 and Asp110 may be involved in binding to both dibutyl benzene-1,2-dicarboxylate and (Z)-hex-3-en-1-ol and may have a great impact on odorant recognition of S. velatus. Our results provide evidence that SvelOBP1 might participate in the olfactory molecular perception of S. velatus and would promote the development of pest attractants for S. velatus control.

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Section: Fluorescence Competitive Binding Analyses Of Svelobp1mentioning

confidence: 97%

Section: Competitive Fluorescence Binding Assaymentioning

confidence: 99%

The Sequence Characteristics and Binding Properties of the Odorant-Binding Protein SvelOBP1 from Sympiezomias velatus (Coleoptera: Curculionidae) to Jujube Volatiles

Zhai,

Zhang,

Tian

et al. 2024

Life

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“…The plum fruit moth Grapholita funebrana is an important fruit borer from the family Tortricidae of Lepidoptera 1 , 2 . Larvae of G. funebrana cause damage by boring the fruits of many wild and cultivated stone fruits and other plants in the family Rosaceae, such as apricot, cherry, peach, and plum 3 .…”

Section: Background and Summarymentioning

confidence: 99%

Nuclear and mitochondrial genomes of the plum fruit moth Grapholita funebrana

Cao,

Yang,

Chen

et al. 2024

Sci Data

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The plum fruit moth Grapholita funebrana (Tortricidae, Lepidoptera) is an important pest of many wild and cultivated stone fruits and other plants in the family Rosaceae. Here, we assembled its nuclear and mitochondrial genomes using Illumina, Nanopore, and Hi-C sequencing technologies. The nuclear genome size is 570.9 Mb, with a repeat rate of 51.28%, and a BUCSO completeness of 97.7%. The karyotype for males is 2n = 56. We identified 17,979 protein-coding genes, 5,643 tRNAs, and 94 rRNAs. We also determined the mitochondrial genome of this species and annotated 13 protein-coding genes, 22 tRNAs, and 2 rRNA. These genomes provide resources to understand the genetics, ecology, and genome evolution of the tortricid moths.

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“…In the FCBA of PBPs of Lymantria dispar to the sex pheromone components Z9-14:Ac, Z7-12:Ac, and Z11-16, it was shown that MlorPBP1 had high affinity for all three components, while MlorPBP2 and MlorPBP3 only bound to one component each [ 14 ]. The experimental results of the combination of Grapholitha funebrana PBPs and sex pheromone ligands show that although all four recombinant GfunPBPs (rGfunPBPs) had binding activity with the tested sex pheromone compounds, their preferred ligands were significantly different [ 15 ]. Two types of SlitPBPs ( SlitPBP1 and SlitPBP2 ) of Spodoptera litura were genetically knocked out using the CRISPR/Cas9 system.…”

Section: Introductionmentioning

confidence: 99%

EsigPBP3 Was the Important Pheromone-Binding Protein to Recognize Male Pheromones and Key Eucalyptus Volatiles

Fu,

Xiao,

Yang

et al. 2024

IJMS

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Pheromone-binding proteins (PBPs) are specific odorant-binding proteins that can specifically recognize insect pheromones. Through transcriptional analysis of the antennae of adult Endoclita signifer, EsigPBP3 was discovered and identified, and EsigPBP3 was found to be highly expressed in the antennae of male moths. Based on the binding characteristics and ability of EsigPBP3, we can find the key ligands and binding site to consider as a target to control the key wood bore E. signifier. In this study, the fluorescence competitive binding assays (FCBA) showed that EsigPBP3 had a high binding affinity for seven key eucalyptus volatiles. Molecular docking analysis revealed that EsigPBP3 had the strongest binding affinity for the sexual pheromone component, (3E,7E)-4,7,11-trimethyl-1,3,7,10-dodecatetraene. Furthermore, same as the result of FCBA, the EsigPBP3 exhibited high binding affinities to key eucalyptus volatiles, eucalyptol, α-terpinene, (E)-beta-ocimene, (−)-β-pinene, and (−)-α-pinene, and PHE35, MET7, VAL10, PHE38, ILE52, and PHE118 are key sites. In summary, EsigPBP3 exhibits high binding affinity to male pheromones and key volatile compounds and the crucial binding sites PHE35, MET7, VAL10, PHE38, ILE52, and PHE118 can act as targets in the recognition of E. signifier pheromones.

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Functional disparity of four pheromone-binding proteins from the plum fruit moth Grapholita funebrana Treitscheke in detection of sex pheromone components

Cited by 5 publications

References 72 publications

The Sequence Characteristics and Binding Properties of the Odorant-Binding Protein SvelOBP1 from Sympiezomias velatus (Coleoptera: Curculionidae) to Jujube Volatiles

The Sequence Characteristics and Binding Properties of the Odorant-Binding Protein SvelOBP1 from Sympiezomias velatus (Coleoptera: Curculionidae) to Jujube Volatiles

Nuclear and mitochondrial genomes of the plum fruit moth Grapholita funebrana

EsigPBP3 Was the Important Pheromone-Binding Protein to Recognize Male Pheromones and Key Eucalyptus Volatiles

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