scholarly journals Characterization of Antennal Sensilla and Immunolocalization of Odorant-Binding Proteins on Spotted Alfalfa Aphid, Therioaphis trifolii (Monell)

2020 ◽  
Vol 11 ◽  
Author(s):  
Limei Song ◽  
Xuemin Wang ◽  
Yanqi Liu ◽  
Yinpeng Sun ◽  
Liping Ban
Keyword(s):  
Electron Microscopy ◽  
Binding Proteins ◽  
Antennal Segment ◽  
Antennal Sensilla ◽  
Odorant Binding Proteins ◽  
Transmission Electron ◽  
Neuron Group ◽  
Ultrathin Sections ◽  
Odorant Binding

The spotted alfalfa aphid [Therioaphis trifolii (Monell), Homoptera, Drepanosiphidae] is a well-known destructive pest that can significantly reduce alfalfa yields. Herein, the morphology of antennal sensilla of T. trifolii has been examined by using scanning electron microscopy and the ultrastructure of sensilla stellate and placoidea was described by transmission electron microscopy. Stellate sensilla, placoid sensilla, and coeloconic sensilla were found on the 6th segment, and a single sensillum placoidea was located on the 5th segment. Placoid sensilla were also present on the 3rd antennal segment of alate and apterous aphids, and the number was similar between two morphs. Two types of trichoid sensilla and coeloconic sensilla were found on the antennae, respectively. The results of ultrastructure showed that stellate sensilla are innervated by three neurons, while placoid sensilla present three groups of neurons, equipped with 2–3 dendrites in each neuron group. Immunocytochemical localization of odorant-binding proteins (OBPs) was performed on ultrathin sections of sensilla stellate and placoidea, and we observed that the antiserum against OBP6 intensively labeled all placoid sensilla from both primary and secondary rhinaria. OBP7 and OBP8 could also be detected in placoid sensilla, but less strongly than OBP6. In addition, OBP6, OBP7, and OBP8 were densely labeled in stellate sensilla, suggesting OBP6, OBP7, and OBP8 may sense alarm pheromone germacrene A in T. trifolii.

scholarly journals Identification and functional characterization of odorant-binding proteins 69a and 76a of Drosophila suzukii

Heliyon ◽  
2021 ◽  
Vol 7 (3) ◽  
pp. e06427
Author(s):  
Haixia Zhan ◽  
Du Li ◽  
Youssef Dewer ◽  
Changying Niu ◽  
Fengqi Li ◽  
...  
Keyword(s):  
Binding Proteins ◽  
Functional Characterization ◽  
Drosophila Suzukii ◽  
Odorant Binding Proteins ◽  
Odorant Binding

Functional Characterization of a New Class of Odorant-Binding Proteins in the MothMamestra brassicae

1998 ◽  
Vol 253 (2) ◽  
pp. 489-494 ◽  
Author(s):  
Jonathan Bohbot ◽  
Franck Sobrio ◽  
Philippe Lucas ◽  
Patricia Nagnan-Le Meillour
Keyword(s):  
Binding Proteins ◽  
Functional Characterization ◽  
Odorant Binding Proteins ◽  
New Class ◽  
Odorant Binding

Binding Characterization of Recombinant Odorant-binding Proteins from the Parasitic Wasp, Microplitis mediator (Hymenoptera: Braconidae)

2010 ◽  
Vol 37 (2) ◽  
pp. 189-194 ◽  
Author(s):  
Shuai Zhang ◽  
Li-Zhen Chen ◽  
Shao-Hua Gu ◽  
Jin-Jie Cui ◽  
Xi-Wu Gao ◽  
...  
Keyword(s):  
Binding Proteins ◽  
Parasitic Wasp ◽  
Odorant Binding Proteins ◽  
Microplitis Mediator ◽  
Odorant Binding

scholarly journals Transcriptomic Characterization of Odorant Binding Proteins in Cacia cretifera thibetana and Their Association with Different Host Emitted Volatiles

Insects ◽  
2021 ◽  
Vol 12 (9) ◽  
pp. 787
Author(s):  
Ning Zhao ◽  
Xiangzhong Mao ◽  
Naiyong Liu ◽  
Ling Liu ◽  
Zhixiao Zhang ◽  
...  
Keyword(s):  
Binding Proteins ◽  
Average Length ◽  
Rna Extraction ◽  
Binding Affinities ◽  
Specific Expression ◽  
Male And Female ◽  
Odorant Binding Proteins ◽  
Chemokine Signaling ◽  
Odorant Binding

This study characterized the transcriptome of Cacia cretifera thibetana and explored odorant binding proteins (OBPs) and their interaction with host-specific compounds. A total of 36 samples from six different organs including antennae, head, thorax, abdomen, wings, and legs (12 groups with 3 replicates per group) from both male and female insects were collected for RNA extraction. Transcriptomic analysis revealed a total of 89,897 transcripts as unigenes, with an average length of 1036 bp. Between male and female groups, 31,095 transcripts were identified as differentially expressed genes (DEGs). The KEGG pathway analysis revealed 26 DEGs associated with cutin, suberine, and wax biosynthesis and 70, 48, and 62 were linked to glycerophospholipid metabolism, choline metabolism in cancer, and chemokine signaling pathways, respectively. A total of 31 OBP genes were identified. Among them, the relative expression of 11 OBP genes (OBP6, 10, 12, 14, 17, 20, 22, 26, 28, 30, and 31) was confirmed by quantitative RT-PCR in different tissues. Seven OBP genes including CcreOBP6 and CcreOBP10 revealed antennae-specific expression. Further, we selected two OBPs (CcreOBP6 and CcreOBP10) for functional analysis to evaluate their binding affinity with 20 host odorant compounds. The CcreOBP6 and CcreOBP10 exhibited strong binding affinities with terpineol and trans-2-hexenal revealing their potential as an attractant or repellent for controlling C. cretifera thibetana.

Molecular and biochemical characterization of two odorant-binding proteins from dark black chafer, Holotrichia parallela

Genome ◽  
2012 ◽  
Vol 55 (7) ◽  
pp. 537-546 ◽  
Author(s):  
Qian Ju ◽  
Ming-jing Qu ◽  
Ying Wang ◽  
Xiao-jing Jiang ◽  
Xiao Li ◽  
...  
Keyword(s):  
Binding Proteins ◽  
Biochemical Characterization ◽  
Sequence Similarity ◽  
Control Measures ◽  
Odorant Binding Proteins ◽  
Holotrichia Parallela ◽  
Important Pest ◽  
High Degree ◽  
Odorant Binding

The dark black chafer, Holotrichia parallela Motschulsky, is an economically important pest worldwide. Odorant-based lures and traps are being developed as a key kind of alternative control measures for this pest, and studies to reveal the mechanisms for chemotaxis in this pest are necessary. Two full-length cDNAs encoding different odorant-binding proteins (OBPs) were cloned. The predicted proteins were found to have the functional domains characteristic of typical OBPs and share a high degree of sequence similarity with OBP1 and OBP2 from other insects and were therefore designated as H. parallela OBP-1 and H. parallela OBP-2 (HparOBP-1 and HparOBP-2, respectively). These two OBPs were specifically expressed in antennae. The binding affinity of two purified proteins indicated that HparOBP-1 and HparOBP-2 could selectively interact with various volatiles emitted from host plants and pheromone components. Among the 10 chemicals tested, HparOBP-1 could bind to six of the tested compounds with a dissociation concentration (Ki) less than 20, and HparOBP-2 could bind to three of the compounds. The two OBPs are probably involved in chemotaxis of the dark black chafer. This discovery should accelerate research on chemical communications of this pest, which could potentially lead to the improvement of control measures based on lures and traps.

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