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Published October 25, 2021 | Version v1
Journal article Open

Docking of non-semiochemical ligands on silkworm Bombyx mori PBP1/GOBP2 binding sites

  • 1. SAAS-Qilu University of Technology
  • 2. Shandong Academy of Agricultural Sciences
  • 3. University of Nantes

Description

This work was mandatory on the basis of the following observations: age variations of PBP/GOBP expression independently of the male pheromone responsiveness, detection of PBP and GOBP proteins in aging female moths, PBP/GOBP expression in multiple metabolic tissues at many various life stages of the insect and induction of PBP/GOBP gene by insecticide abamectin. On the basis of this complete set of data analyzing the abundance of mRNA and the presence of protein for PBPs and GOBPs in an extremely large repertoire of tissues, we set out molecular docking experiments to analyze the binding of a variety of non-semiochemical ligands including alkaloids, insecticides, juvenoids, products of fat degradation and vitamins to BmorPBP1 and BmorGOBP2. These two proteins were extensively described for their ability to interact with odor pheromone semiochemical molecule.

Notes

Supplemental information Frontiers in Physiology https://doi.org/10.3389/fphys.2021.712593 Financial Support: Overseas Talent-Taishan JFP-NO.tshw20091015 Natural Sciences Foundation of Shandong Province ZR2011CM046

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Additional details

Related works

Is supplemented by
Journal article: 10.3389/fphys.2021.712593 (DOI)

References

  • Guo, Xia et al. (2021) An expanded survey of the moth PBP/GOBP clade in Bombyx mori: new insight into expression and functional roles. Front. Physiol. doi:10.3389/fphys.2021.712593

Subjects

Insect Odor Binding Proteins
en.wikipedia.org/wiki/Odorant-binding_protein
Bombyx Pheromone Binding Protein 1
www.uniprot.org/uniprot/55M675
Bombyx General Odorant Binding Protein 2
www.uniprot.org/uniprot/P34170
Vitamin chemical structures
www.compoundchem.com/2015/01/13/vitamins