Binding interaction between a queen pheromone component HOB and pheromone binding protein ASP1 of Apis cerana

Weng, Chen; Fu, Yu-Xia; Jiang, Hongtao; Zhuang, Shulin; Li, Hongliang

doi:10.1016/j.ijbiomac.2014.08.046

Cited by 27 publications

(14 citation statements)

References 20 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…H > 0 and S > 0 alludes a hydrophobic interaction [37]; H < 0 and S < 0 suggests the van der Waals force or hydrogen bond formation [38]; and H < 0 and S > 0 reflects an electrostatic force [39]. Besides, the negative values of G reveals that the binding process was spontaneous [22,40].…”

Section: Determination Of Binding Parameter and Binding Forcementioning

confidence: 99%

Binding interaction between rice glutelin and amylose: Hydrophobic interaction and conformational changes

Liu

Zhong

et al. 2015

International Journal of Biological Macromolecules

View full text Add to dashboard Cite

Section: Determination Of Binding Parameter and Binding Forcementioning

confidence: 99%

Binding interaction between rice glutelin and amylose: Hydrophobic interaction and conformational changes

Liu

Zhong

et al. 2015

International Journal of Biological Macromolecules

View full text Add to dashboard Cite

“…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 ). OBP11 have the highest expression in the stage of foragers, which display the highest olfactory sensitity in the A. cerana (Zhao et al, 2013a ).…”

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.

View full text Add to dashboard Cite

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.

show abstract

“…The insect antenna is a highly specific sensor and can discriminate exquisitely different odorant molecules including sex pheromones that stimulate insect behavioral responses 1 . The olfactory system of Lepidoptera is very sensitive to detect and differentiate similar sex pheromone compounds between the proximal species of insects, involving in the evolution of insect mating isolation and speciation 2 – 4 .…”

Section: Introductionmentioning

confidence: 99%

Molecular characterization and functional differentiation of three pheromone-binding proteins from Tryporyza intacta

Fang

Hu²,

Mao

et al. 2018

Sci Rep

View full text Add to dashboard Cite

Insect pheromone-binding proteins (PBPs) have been proposed to capture and transport hydrophobic sex pheromone components emitted by con-specific insects to pheromone receptors in the hemolymph of male antennal sensilla. In this study, field trapping results indicate that a mixture of E11–16: Ald and Z11–16: Ald can effectively attract a great number of male Tryporyza intacta. Real-time PCR results suggest that the transcript levels of three TintPBP1-3 genes are mainly expressed in the adult antennae. Fluorescence competitive binding experiments show that TintPBP1-3 proteins have great binding affinities to their major sex pheromones. Moreover, TintPBPs clearly cannot bind to other four kinds of sex pheromone components released by another sugarcane borer, Chilo venosatus and Chilo infuscatellu, which have the same host plant and live in similar habitats like T. intacta. The molecular docking results demonstrate that six amino acid residues of the three TintPBPs are crucial for the specific perception of the sex pheromone components. These results will provide a foundation for the development of novel sex pheromone analogues and blocking agents for biological control of sugarcane pests, improving their efficient monitoring and integrated management strategies in the sugarcane field.

show abstract

Binding interaction between a queen pheromone component HOB and pheromone binding protein ASP1 of Apis cerana

Cited by 27 publications

References 20 publications

Binding interaction between rice glutelin and amylose: Hydrophobic interaction and conformational changes

Binding interaction between rice glutelin and amylose: Hydrophobic interaction and conformational changes

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

Molecular characterization and functional differentiation of three pheromone-binding proteins from Tryporyza intacta

Contact Info

Product

Resources

About