scholarly journals Characterization of the Expression and Functions of Two Odorant-Binding Proteins of Sitophilus zeamais Motschulsky (Coleoptera: Curculionoidea)

Insects ◽  
2019 ◽  
Vol 10 (11) ◽  
pp. 409 ◽  
Author(s):  
Zhang ◽  
Shen ◽  
Xia ◽  
Wang ◽  
Tang
Keyword(s):  
Binding Affinity ◽  
Binding Proteins ◽  
Competitive Binding ◽  
Sitophilus Zeamais ◽  
Host Volatiles ◽  
Binding Assays ◽  
Odorant Binding Proteins ◽  
Qrt Pcr ◽  
Odorant Binding ◽  
Competitive Binding Assays

Odorant-binding proteins (OBPs) are important in insect chemical communication. The objective of this research was to identify the functions of two OBPs in Sitophilus zeamais. qRT-PCR and western blot (WB) were performed to investigate the expression profiles at the transcript and protein levels, respectively. Fluorescence competitive binding assays were used to measure the ability of the OBPs to bind to host volatiles, and a Y-tube olfactometer was used to verify the results (attraction/no response) via behavioral experiments. The RNAi was used to verify the function by knocking down the ability of proteins to bind odorants. qRT-PCR showed the highest expression SzeaOBP1 and SzeaOBP28 at the low-instar larva (LL) and eclosion adult (EA) stages, respectively. WB showed that both SzeaOBP1 and SzeaOBP28 were highly expressed in the EA stage. Fluorescence competitive binding assays indicated that SzeaOBP1 exhibited extremely high binding affinity with cetanol. SzeaOBP28 exhibited a pronounced binding affinity for 4-hydroxy-3-methoxybenzaldehyde. The behavioral experiment showed that the adult S. zeamais responded strongly to 4-hydroxy-3-methoxybenzaldehyde and valeraldehyde from Sorghum bicolor. The RNAi knockdown individuals displayed behavioral differences between normal insects and dsRNA (SzeaOBP1)-treated insects. We infer that they both have functions in perception and recognition of host volatiles, whereas SzeaOBP28 may also have other functions.

New Analogues of (E)-β-Farnesene with Insecticidal Activity and Binding Affinity to Aphid Odorant-Binding Proteins

2011 ◽  
Vol 59 (6) ◽  
pp. 2456-2461 ◽  
Author(s):  
Yufeng Sun ◽  
Huili Qiao ◽  
Yun Ling ◽  
Shaoxiang Yang ◽  
Changhui Rui ◽  
...  
Keyword(s):  
Binding Affinity ◽  
Insecticidal Activity ◽  
Binding Proteins ◽  
Odorant Binding Proteins ◽  
Odorant Binding

scholarly journals Sex- and tissue-specific expression of odorant-binding proteins and chemosensory proteins in adults of the scarab beetle Hylamorpha elegans (Burmeister) (Coleoptera: Scarabaeidae)

PeerJ ◽  
2019 ◽  
Vol 7 ◽  
pp. e7054 ◽  
Author(s):  
Angélica González-González ◽  
María E. Rubio-Meléndez ◽  
Gabriel I. Ballesteros ◽  
Claudio C. Ramírez ◽  
Rubén Palma-Millanao
Keyword(s):  
Binding Proteins ◽  
Expression Patterns ◽  
Scarab Beetle ◽  
Control Methods ◽  
Specific Expression ◽  
Odorant Binding Proteins ◽  
Chemosensory Proteins ◽  
Qrt Pcr ◽  
Odorant Binding ◽  
Pest Control Methods

In this study, we addressed the sex- and tissue-specific expression patterns of odorant-binding proteins (OBPs) and chemosensory proteins (CSPs) in Hylamorpha elegans (Burmeister), an important native scarab beetle pest species from Chile. Similar to other members of its family, this scarab beetle exhibit habits that make difficult to control the pest by conventional methods. Hence, alternative ways to manage the pest populations based on chemical communication and signaling (such as disrupting mating or host finding process) are highly desirable. However, developing pest-control methods based on chemical communication requires to understand the molecular basis for pheromone recognition/chemical perception in this species. Thus, with the aim of discovering olfaction-related genes, we obtained the first reference transcriptome assembly of H. elegans. We used different tissues of adult beetles from males and females: antennae and maxillary palps, which are well known for embedded sensory organs. Then, the expression of predicted odorant-binding proteins (OBPs) and chemosensory proteins (CSPs) was analyzed by qRT-PCR. In total, 165 transcripts related to chemoperception were predicted. Of these, 16 OBPs, including one pheromone-binding protein (PBP), and four CSPs were successfully amplified by qRT-PCR. All of these genes were differentially expressed in the sensory tissues with respect to the tibial tissue that was used as a control. The single predicted PBP found was highly expressed in the antennal tissues, particularly in males, while several OBPs and one CSP showed male-biased expression patterns, suggesting that these proteins may participate in sexual recognition process. In addition, a single CSP was expressed at higher levels in female palps than in any other studied condition, suggesting that this CSP would participate in oviposition process. Finally, all four CSPs exhibited palp-biased expression while mixed results were obtained for the expression of the OBPs, which were more abundant in the palps than in the antennae. These results suggest that these chemoperception proteins would be interesting novel targets for control of H. elegans, thus providing a theoretical basis for further studies involving new pest control methods.

scholarly journals GOBP1 Plays a Key Role in Sex Pheromones and Plant Volatiles Recognition in Yellow Peach Moth, Conogethes punctiferalis (Lepidoptera: Crambidae)

Insects ◽  
2019 ◽  
Vol 10 (9) ◽  
pp. 302
Author(s):  
Jing ◽  
Zhang ◽  
Bai ◽  
Prabu ◽  
He ◽  
...  
Keyword(s):  
Host Plant ◽  
Binding Affinity ◽  
Plant Volatiles ◽  
Sex Pheromones ◽  
Binding Proteins ◽  
Prunus Persica ◽  
Olfactory Sensilla ◽  
Odorant Binding Proteins ◽  
Yellow Peach Moth ◽  
Odorant Binding

Insects recognize odorous compounds using sensory neurons organized in olfactory sensilla. The process odor detection in insects requires an ensemble of proteins, including odorant binding proteins, olfactory receptors, and odor degrading enzymes; each of them are encoded by multigene families. Most functional proteins seem to be broadly tuned, responding to multiple chemical compounds with different, but mostly quite similar structures. Based on the hypothesis that insects recognize host volatiles by means of general odorant binding proteins (GOBPs), the current study aimed to characterize GOBPs of the yellow peach moth, Conogethes punctiferalis (Guenée). In oviposition preference tests, it was found that the yellow peach moth preferred volatiles from Prunus persica (peach) in finding their host plant. Exposure of the moth to volatiles from peaches affected the expression level of GOBP genes. Binding affinity of GOBPs from yellow peach moth was assessed for 16 host plant volatiles and 2 sex pheromones. The fluorescence ligand-binding assays revealed highest affinities for hexadecanal, farnesol, and limonene with KD values of 0.55 ± 0.08, 0.35 ± 0.04, and 1.54 ± 0.39, respectively. The binding sites of GOBPs from yellow peach moth were predicted using homology modeling and characterized using molecular docking approaches. The results indicated the best binding affinity of both GOBP1 and GOBP2 for farnesol, with scores of −7.4 and −8.5 kcal/mol. Thus, GOBPs may play an important role in the process of finding host plants.

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