scholarly journals Molecular and functional characterization of buffalo nasal epithelial odorant binding proteins and their structural insights by in-silico and biochemical approach

2020 ◽  
Author(s):  
Chidhambaram Manikkaraja ◽  
Bhavika Mam ◽  
Randhir Singh ◽  
Balasubramanian Nagarathnam ◽  
Geen George ◽  
...  
Keyword(s):  
Oleic Acid ◽  
In Silico ◽  
Binding Proteins ◽  
Functional Characterization ◽  
Site Directed Mutagenesis ◽  
Nasal Epithelium ◽  
Binding Affinities ◽  
Odorant Binding Proteins ◽  
Strong Binding ◽  
Odorant Binding

AbstractThe olfactory system is capable of detecting and distinguishing thousands of environmental odorants that play a key role in reproduction, social behaviours including pheromones influenced classical events. Membrane secretary odorant binding proteins (OBPs) are soluble lipocalins, localized in the nasal membrane of mammals. They bind and carry odorants within the nasal epithelium to putative olfactory transmembrane receptors (ORs). While the existence of OBPs and their significant functions are very well known in insects and laboratory mammals, there is little information about the species-specific OBPs in buffaloes. In fact, the OBP of nasal epithelium has not yet been exploited to develop a suitable technique to detect estrus which is being reported as a difficult task in buffalo. In the present study, using molecular biology and protein engineering approaches, we have cloned six novel OBP isoforms from buffalo nasal epithelium (bnOBPs). Furthermore, 3D model was developed and molecular-docking, dynamics experiments were performed by In-silico approach. In particular, we found four residues (Phe104, Phe134, Phe69 and Asn118) from OBP1a, which had strong binding affinities towards two sex pheromones, specifically oleic acid and p-cresol. We expressed this protein in Escherichia coli to examine its involvement in the sex pheromone perception from female buffalo urine and validated through fluorescence quenching studies. Interestingly, fluorescence binding experiments also showed similar strong binding affinities of OBP1a to oleic acid and p-cresol. By using structural data, the binding specificity is also verified by site-directed mutagenesis of the four residues followed by in-vitro binding assays. Our results enable to better understand the functions of different nasal epithelium OBPs in buffaloes. They also lead to improved understanding of the interaction between olfactory proteins and odorants to develop highly selective biosensing devices for non-invasive detection of estrus in buffaloes.

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

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.

Site-directed mutagenesis of odorant-binding proteins

2020 ◽  
pp. 301-324
Author(s):  
Jiao Zhu ◽  
Valeriia Zaremska ◽  
Chiara D'Onofrio ◽  
Wolfgang Knoll ◽  
Paolo Pelosi
Keyword(s):  
Binding Proteins ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Odorant Binding Proteins ◽  
Odorant Binding

scholarly journals Three odorant-binding proteins are involved in the behavioral response of Sogatella furcifera to rice plant volatiles

PeerJ ◽  
2019 ◽  
Vol 7 ◽  
pp. e6576 ◽  
Author(s):  
Kui Hu ◽  
Sheng Liu ◽  
Lin Qiu ◽  
Youzhi Li
Keyword(s):  
Rice Plant ◽  
Plant Volatiles ◽  
Binding Proteins ◽  
Signal Transduction Pathway ◽  
Insect Behavior ◽  
Binding Affinities ◽  
Sogatella Furcifera ◽  
Odorant Binding Proteins ◽  
Weak Binding ◽  
Odorant Binding

Plant volatiles play an important role in regulating insect behavior. Odorant binding proteins (OBPs) are involved in the first step of the olfactory signal transduction pathway and plant volatiles recognition. Sogatella furcifera is one of the most destructive pests of rice crops. Understanding the functions of S. furcifera OBPs (SfurOBPs) in the host plant location and the behavioral responses of S. furcifera to rice plant volatiles could lead to improved, more environmentally-friendly, methods for controlling this pest. We found that SfurOBP1 displayed only weak binding with all the tested volatiles. SfurOBP2, SfurOBP3 and SfurOBP11 had different binding affinities to β-ionone. SfurOBP2 and SfurOBP11 had strong binding affinities to β-caryophyllene (Ki = 2.23 µM) and plant alcohol (Ki = 2.98 µM), respectively. The results of Y-olfactometer experiments indicate that S. furcifera was significantly repelled by octanal and n-octane but strongly attracted by (+)-limonene, acetophenone, 2-heptanone, n-hendecane, α-farnesene and β-ionone. Furthermore, the dsRNA-mediated gene silencing of SfurOBP2, SfurOBP3 and SfurOBP11 shifted the olfactory behavior of S. furcifera for β-ionone, α-farnesene and plant alcohol, respectively. These results suggest that the SfurOBPs are involved in the recognition of rice plant volatiles, and several potential repellants and lures for controlling this pest.

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