The scarab beetle Holotrichia oblita Faldermann (Coleoptera: Scarabaeidae) is a predominant underground pest in the northern parts of China, and its larvae (grubs) cause great economic losses because of its wide range of host plants and covert habitats. Environmentally friendly strategies for controlling adults would have novel and broad potential applications. One potential pest management measure is the regulation of olfactory chemoreception to control target insect pests. In the process of olfactory recognition, odorant-binding proteins (OBPs) are believed to carry hydrophobic odorants from the environment to the surface of olfactory receptor neurons. To obtain a better understanding of the relationship between OBP structures and their ligands, homology modelling and molecular docking have been conducted on the interaction between HoblOBP1 and hexyl benzoate in the present study. Based on the results, site-directed mutagenesis and binding experiments were combined to describe the binding sites of HoblOBP1 and to explore its ligand-binding mechanism. After homology modelling of HoblOBP1, it was found that the three-dimensional structure of HoblOBP1 consists of six α-helices and three disulphide bridges that connect the helices, and the hydrophobic pockets are both composed of five helices. Based on the docking study, we found that van der Waals interactions and hydrophobic interactions are both important in the bonding between HoblOBP1 and hexyl benzoate. Intramolecular residues formed the hydrogen bonds in the C terminus of the protein and the bonds are crucial for the ligand-binding specificity. Finally, MET48, ILE80 and TYR111 are binding sites predicted for HoblOBP1. Using site-directed mutagenesis and fluorescence assays, it was found that ligands could not be recognized by mutant of Tyr111. A possible explanation is that the compound could not be recognized by the mutant, and remains in the binding cavity because of the loss of the intramolecular hydrogen bonding that acts as a holder. So we believe that Tyr111 of HoblOBP1 is a key binding site. We also believe that Ile80A is a very important binding site, especially to some ligands.
66Bumblebees are a diverse group of globally important pollinators in natural 67 ecosystems and for agricultural food production. With both eusocial and solitary life-68 cycle phases, and some social parasite species, they are especially interesting models 69to understand social evolution, behavior, and ecology. Reports of many species in 70 decline point to pathogen transmission, habitat loss, pesticide usage, and global 71 climate change, as interconnected causes. These threats to bumblebee diversity make 72 our reliance on a handful of well-studied species for agricultural pollination 73 particularly precarious. To broadly sample bumblebee genomic and phenotypic 74 diversity, we de novo sequenced and assembled the genomes of 17 species, 75representing all 15 subgenera, producing the first genus-wide quantification of genetic 76and genomic variation potentially underlying key ecological and behavioral traits. The 77 species phylogeny resolves subgenera relationships while incomplete lineage sorting 78 likely drives high levels of gene tree discordance. Five chromosome-level assemblies 79show a stable 18-chromosome karyotype, with major rearrangements creating 25 80 chromosomes in social parasites. Differential transposable element activity drives 81 changes in genome sizes, with putative domestications of repetitive sequences 82influencing gene coding and regulatory potential. Dynamically evolving gene families 83and signatures of positive selection point to genus-wide variation in processes linked 84to foraging, diet and metabolism, immunity and detoxification, as well as adaptations 85for life at high altitudes. These high-quality genomic resources capture natural genetic 86and phenotypic variation across bumblebees, offering new opportunities to advance 87 our understanding of their remarkable ecological success and to identify and manage 88 current and future threats. 89 90 91 92
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
hi@scite.ai
10624 S. Eastern Ave., Ste. A-614
Henderson, NV 89052, USA
Copyright © 2024 scite LLC. All rights reserved.
Made with 💙 for researchers
Part of the Research Solutions Family.