Molecular recognition of floral volatile with two olfactory related proteins in the Eastern honeybee (Apis cerana)

Li, Hongliang; Zhang, Linya; Ni, Cuixia; Shang, Hanwu; Zhuang, Shulin; Li, Jianke

doi:10.1016/j.ijbiomac.2013.01.032

Cited by 34 publications

(14 citation statements)

References 29 publications

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“…As for (−)‐limonene, it showed static quenching at pH 7.4 but dynamic quenching at pH 5.0. Surprisingly, the K q value was also greater than 2.0 × 10 10 (l/mol/s), which might be caused by the ionic salts in the solution (Li et al ., ).…”

Section: Resultsmentioning

confidence: 97%

Optimization of reverse chemical ecology method: false positive binding of Aenasius bambawalei odorant binding protein 1 caused by uncertain binding mechanism

et al. 2018

Insect Molecular Biology

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Odorant binding proteins (OBPs) are considered as the core molecular targets in reverse chemical ecology, which is a convenient and efficient method by which to screen potential semiochemicals. Herein, we identified a classic OBP, AbamOBP1 from Aenasius bambawalei, which showed high mRNA expression in male antennae. Fluorescence competitive binding assay (FCBA) results demonstrated that AbamOBP1 has higher binding affinity with ligands at acid pH, suggesting the physiologically inconsistent binding affinity of this protein. Amongst the four compounds with the highest binding affinities at acid pH, 2, 4, 4-trimethyl-2-pentene and 1-octen-3-one were shown to have attractant activity for male adults, whereas (-)-limonene and an analogue of 1-octen-3-ol exhibited nonbehavioural activity. Further homology modelling and fluorescence quenching experiments demonstrated that the stoichiometry of the binding of this protein to these ligands was not 1: 1, suggesting that the results of FCBA were false. In contrast, the apparent association constants (Ka) of fluorescence quenching experiments seemed to be more reliable, because 2, 4, 4-trimethyl-2-pentene and 1-octen-3-one had observably higher Ka than (-)-limonene and 1-octen-3-ol at neutral pH. Based on the characteristics of different OBPs, various approaches should be applied to study their binding affinities with ligands, which could modify and complement the results of FCBA and contribute to the application of reverse chemical ecology.

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Section: Resultsmentioning

confidence: 97%

Optimization of reverse chemical ecology method: false positive binding of Aenasius bambawalei odorant binding protein 1 caused by uncertain binding mechanism

et al. 2018

Insect Molecular Biology

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“…Up to now, 17 OBPs have been found in A. cerana (Zhao et al, 2016 ). So far, three typical OBPs of them has been reported in-depth, ASP2 (OBP2) was specially distributed in worker bee antennae (Li et al, 2008 ), and bind the floral volatile with the dynamic binding mode (Li et al, 2013 ). ASP1 (OBP1) was expressed abundantly on the sensilla placoidea in drone antennae (Zhao et al, 2013b ), and it can bind queen pheromone component with the static binding mode (Weng et al, 2015 ).…”

Section: Introductionmentioning

confidence: 99%

Various Bee Pheromones Binding Affinity, Exclusive Chemosensillar Localization, and Key Amino Acid Sites Reveal the Distinctive Characteristics of Odorant-Binding Protein 11 in the Eastern Honey Bee, Apis cerana

Song

Zhang

et al. 2018

Front. Physiol.

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Odorant-binding proteins (OBPs) are the critical elements responsible for binding and transporting odors and pheromones in the sensitive olfactory system in insects. Honey bees are representative social insects that have complex odorants and pheromone communication systems relative to solitary insects. Here, we first cloned and characterized OBP11 (AcerOBP11), from the worker bees antennae of Eastern honey bee, Apis cerana. Based on sequence and phylogenetic analysis, most sequences homologous to AcerOBP11 belong to the typical OBPs family. The transcriptional expression profiles showed that AcerOBP11 was expressed throughout the developmental stages and highly specifically expressed in adult antennae. Using immunofluorescence localization, AcerOBP11 in worker bee's antennae was only localized in the sensilla basiconica (SB) near the fringe of each segment. Fluorescence ligand-binding assay showed that AcerOBP11 protein had strong binding affinity with the tested various bee pheromones components, including the main queen mandibular pheromones (QMPs), methyl p-hydroxybenzoate (HOB), and (E)-9-oxo-2-decanoic acid (9-ODA), alarm pheromone (n-hexanol), and worker pheromone components. AcerOBP11 also had strong binding affinity to plant volatiles, such as 4-Allylveratrole. Based on the docking and site-directed mutagenesis, two key amino acid residues (Ile97 and Ile140) were involved in the binding of AcerOBP11 to various bee pheromones. Taken together, we identified that AcerOBP11 was localized in a single type of antennal chemosensilla and had complex ligand-binding properties, which confer the dual-role with the primary characteristics of sensing various bee pheromones and secondary characteristics of sensing general odorants. This study not only prompts the theoretical basis of OBPs-mediated bee pheromones recognition of honey bee, but also extends the understanding of differences in pheromone communication between social and solitary insects.

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“…Moreover, the biosensor had reserved the biofunction of OBPs, and it can be used to detect odorants selectively and quantitatively. The broad substrate odorant specificity to floral odors, semiochemicals, and pheromones was in accord with properties of OBPs [37,47].…”

Section: Odorant Detection and Analysismentioning

confidence: 55%

“…Acer-ASP2 was cloned from the full-length cDNA of adult worker bees, Apisceranacerana [37]. Briefly, using reverse transcription-polymerase chain reaction (RT-PCR) and pET-30a (+)/BL21 (DE3) prokaryotic expression system, Acer-ASP2 can be cloned and expressed by being transformed into Escherichia coli BL21 competent cells.…”

Section: Production and Fixation Of Odorant Binding Proteinsmentioning

confidence: 99%

Smell Sensors Based on Odorant Binding Proteins

Yao

Liu

2015

Bioinspired Smell and Taste Sensors

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Molecular recognition of floral volatile with two olfactory related proteins in the Eastern honeybee (Apis cerana)

Cited by 34 publications

References 29 publications

Optimization of reverse chemical ecology method: false positive binding of Aenasius bambawalei odorant binding protein 1 caused by uncertain binding mechanism

Optimization of reverse chemical ecology method: false positive binding of Aenasius bambawalei odorant binding protein 1 caused by uncertain binding mechanism

Various Bee Pheromones Binding Affinity, Exclusive Chemosensillar Localization, and Key Amino Acid Sites Reveal the Distinctive Characteristics of Odorant-Binding Protein 11 in the Eastern Honey Bee, Apis cerana

Smell Sensors Based on Odorant Binding Proteins

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