scholarly journals An Odorant Binding Protein (SaveOBP9) Involved in Chemoreception of the Wheat Aphid Sitobion avenae

2020 ◽  
Vol 21 (21) ◽  
pp. 8331
Author(s):  
Rana Muhammad Kaleem Ullah ◽  
Sundas Rana Quershi ◽  
Muhammad Muzammal Adeel ◽  
Hazem Abdelnabby ◽  
Muhammad Irfan Waris ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Rna Interference ◽  
Integrated Management ◽  
Three Dimensional ◽  
Sitobion Avenae ◽  
Odorant Binding Proteins ◽  
Volatile Organic ◽  
Fluorescence Binding ◽  
Fluorescence Binding Assay ◽  
Odorant Binding

Odorant binding proteins play a key role in the olfactory system and are involved in the odor perception and discrimination of insects. To investigate the potential physiological functions of SaveOBP9 in Sitobion avenae, fluorescence ligand binding experiments, molecular docking, RNA interference, and behavioral tests were performed. Fluorescence binding assay results showed that SaveOBP9 had broad and high (Ki < 10 μM) binding abilities with most of the wheat volatiles, but was more obvious at pH 7.4 than pH 5.0. The binding sites of SaveOBP9 to the volatiles were predicted well by three-dimensional docking structure modeling and molecular docking. Moreover, S. avenae showed a strong behavioral response with the four compounds of wheat. The reduction in mRNA transcript levels after the RNA interference significantly reduced the expression level of SaveOBP9 and induced the non-significant response of S. avenae to the tetradecane, octanal, decanal, and hexadecane. This study provides evidence that SaveOBP9 might be involved in the chemoreception of wheat volatile organic compounds and can successfully contribute in the integrated management programs of S. avenae.

scholarly journals Discrimination of Oviposition Deterrent Volatile β-Ionone by Odorant-Binding Proteins 1 and 4 in the Whitefly Bemisia tabaci

Biomolecules ◽  
2019 ◽  
Vol 9 (10) ◽  
pp. 563 ◽  
Author(s):  
Li ◽  
Li ◽  
Dewer ◽  
Qu ◽  
Yang ◽  
...  
Keyword(s):  
Bemisia Tabaci ◽  
Binding Proteins ◽  
Oviposition Behavior ◽  
Egg Laying ◽  
Competitive Binding Assay ◽  
Odorant Binding Proteins ◽  
Evolution Analysis ◽  
Binding Function ◽  
Fluorescence Binding ◽  
Odorant Binding

: The whitefly, Bemisia tabaci, is an important invasive economic pest of agricultural crops worldwide. β-ionone has a significant oviposition repellent effect against B. tabaci, but the olfactory molecular mechanism of this insect for recognizing β-ionone is unclear. To clarify the binding properties of odorant-binding proteins (OBPs) with β-ionone, we performed gene cloning, evolution analysis, bacterial expression, fluorescence competitive binding assay, and molecular docking to study the binding function of OBP1 and OBP4 on β-ionone. The results showed that after the OBP1 and OBP4 proteins were recombined, the compound β-ionone exhibited a reduction in the fluorescence binding affinity to <50%, with a dissociation constant of 5.15 and 3.62 μM for OBP1 and OBP4, respectively. Our data indicate that β-ionone has high affinity for OBP1 and OBP4, which play a crucial role in the identification of oviposition sites in B. tabaci. The findings of this study suggest that whiteflies employ β-ionone compound in the selection of the suitable egg-laying sites on host plants during the oviposition behavior.

scholarly journals On the capacity of putative plant odorant-binding proteins to bind volatile plant isoprenoids

2021 ◽  
Author(s):  
Deborah Giordano ◽  
Angelo Facchiano ◽  
Sabato D’Auria ◽  
Francesco Loreto
Keyword(s):  
Volatile Organic Compounds ◽  
Data Base ◽  
Organic Compounds ◽  
In Silico ◽  
Simulation Experiments ◽  
Odorant Binding Proteins ◽  
Plant Communication ◽  
Volatile Organic ◽  
Odorant Binding ◽  
Data Base Search

AbstractPlants use odors not only to recruit other organisms for symbioses, but to ‘talk’ to each other. Volatile organic compounds (VOCs) from “emitting” plants inform the “receiving” (listening) plants of impending stresses or simply of their presence. However, the receptors that allow receivers to perceive the volatile cue are elusive. Most likely, plants (as animals) have odorant bind proteins (OBPs), and in fact few OBPs are known to bind “stress-induced” plant VOCs. We investigated whether OBPs may bind volatile constitutive and stress-induced isoprenoids, the most emitted plant VOCs, with well-established roles in plant communication. First, we performed a data base search that generated a list of candidate plant OBPs. Second, we investigated in silico the ability of the identified candidate plant OBPs to bind VOCs by molecular simulation experiments. Our results show that monoterpenes can bind the same OBPs that were described to bind other stress-induced VOCs. Whereas, the constitutive hemiterpene isoprene does not bind any investigated OBP and may not have an info-chemical role. We conclude that, as for animal, plant OBPs may bind different VOCs. Despite being generalist and not specialized, plant OBPs may play an important role in allowing plants to eavesdrop messages sent by neighboring plants.

scholarly journals Binding Properties of Odorant-Binding Protein 4 of Tirathaba rufivena to Areca catechu Volatiles

Plants ◽  
2022 ◽  
Vol 11 (2) ◽  
pp. 167
Author(s):  
Xiang Zhou ◽  
Zheng Wang ◽  
Guangchao Cui ◽  
Zimeng Du ◽  
Yunlong Qian ◽  
...  
Keyword(s):  
Binding Protein ◽  
Integrated Management ◽  
Insect Pest ◽  
Binding Pocket ◽  
Secretory Protein ◽  
Odorant Binding Protein ◽  
Host Recognition ◽  
Areca Catechu ◽  
Fluorescence Binding Assay ◽  
Odorant Binding

Odorant-binding proteins (OBPs) play a key role in the olfactory system and are essential for mating and oviposition host selection. Tirathaba rufivena, a serious lepidopterous insect pest of the palm area in recent years, has threatened cultivations of Areca catechu in Hainan. Female-biased odorant-binding protein 4 of T. rufivena (TrufOBP4) expression was hypothesized to participate in the process of oviposition host recognition and localization. In this study, we cloned and analyzed the cDNA sequence of TrufOBP4. The predicted mature protein TrufOBP4 is a small, soluble, secretory protein and belongs to a classic OBP subfamily. Fluorescence binding assay results showed that TrufOBP4 had high binding abilities with the host plant volatiles, octyl methoxycinnamate, dibutyl phthalate, myristic acid and palmitic acid. These four components tend to dock in the same binding pocket based on the molecular docking result. The interactions and contributions of key amino acid residues were also characterized. This research provides evidence that TrufOBP4 might participate in the chemoreception of volatile compounds from inflorescences of A. catechu and can contribute to the integrated management of T. rufivena.

scholarly journals Effective collection of volatile organic compounds in water using rimming flow with odorant-binding proteins

2015 ◽  
Vol 2 (4) ◽  
pp. 15-00244-15-00244 ◽  
Author(s):  
Hitoshi KIDA ◽  
Satoshi TSUKADA ◽  
Yoshiyuki TAGAWA ◽  
Ryoichi SATO ◽  
Masaharu KAMEDA
Keyword(s):  
Volatile Organic Compounds ◽  
Organic Compounds ◽  
Binding Proteins ◽  
Odorant Binding Proteins ◽  
Rimming Flow ◽  
Volatile Organic ◽  
Odorant Binding

scholarly journals The Odorant-Binding Proteins of the Spider Mite Tetranychus urticae

2021 ◽  
Vol 22 (13) ◽  
pp. 6828
Author(s):  
Jiao Zhu ◽  
Giovanni Renzone ◽  
Simona Arena ◽  
Francesca Romana Dani ◽  
Harald Paulsen ◽  
...  
Keyword(s):  
Tetranychus Urticae ◽  
Spider Mite ◽  
Binding Proteins ◽  
Three Dimensional ◽  
Binding Pocket ◽  
Agricultural Pests ◽  
Three Dimensional Model ◽  
Odorant Binding Proteins ◽  
Large Molecules ◽  
Odorant Binding

Spider mites are one of the major agricultural pests, feeding on a large variety of plants. As a contribution to understanding chemical communication in these arthropods, we have characterized a recently discovered class of odorant-binding proteins (OBPs) in Tetranychus urticae. As in other species of Chelicerata, the four OBPs of T. urticae contain six conserved cysteines paired in a pattern (C1–C6, C2–C3, C4–C5) differing from that of insect counterparts (C1–C3, C2–C5, C4–C6). Proteomic analysis uncovered a second family of OBPs, including twelve members that are likely to be unique to T. urticae. A three-dimensional model of TurtOBP1, built on the recent X-ray structure of Varroa destructor OBP1, shows protein folding different from that of insect OBPs, although with some common features. Ligand-binding experiments indicated some affinity to coniferyl aldehyde, but specific ligands may still need to be found among very large molecules, as suggested by the size of the binding pocket.

scholarly journals A hypothesis on the capacity of plant odorant-binding proteins to bind volatile isoprenoids based on in silico evidences

eLife ◽  
2021 ◽  
Vol 10 ◽  
Author(s):  
Deborah Giordano ◽  
Angelo Facchiano ◽  
Sabato D'Auria ◽  
Francesco Loreto
Keyword(s):  
Binding Proteins ◽  
Docking Simulation ◽  
Structural Features ◽  
Plant Proteins ◽  
Molecular Docking Simulation ◽  
Odorant Binding Proteins ◽  
Plant Communication ◽  
Defensive Responses ◽  
Volatile Organic ◽  
Odorant Binding

Volatile organic compounds (VOCs) from ‘emitting’ plants inform the ‘receiving’ (listening) plants of impending stresses or simply of their presence. However, the receptors that allow receivers to detect the volatile cue are elusive. Most likely, plants (as animals) have odorant-binding proteins (OBPs), and in fact, a few OBPs are known to bind ‘stress-induced’ plant VOCs. We investigated whether these and other putative OBPs may bind volatile constitutive and stress-induced isoprenoids, the most emitted plant VOCs, with well-established roles in plant communication and defense. Molecular docking simulation experiments suggest that structural features of a few plant proteins screened in databases could allow VOC binding. In particular, our results show that monoterpenes may bind the same plant proteins that were described to bind other stress-induced VOCs, while the constitutive hemiterpene isoprene is unlikely to bind any investigated putative OBP and may not have an info-chemical role. We conclude that, as for animal, there may be plant OBPs that bind multiple VOCs. Plant OBPs may play an important role in allowing plants to eavesdrop messages by neighboring plants, triggering defensive responses and communication with other organisms.

A Three-Dimensional Tetraphenylethylene-Based Fluorescence Covalent Organic Framework for Molecular Recognition

2020 ◽  
Author(s):  
Junxia Ren ◽  
Yaozu Liu ◽  
Xin Zhu ◽  
Yangyang Pan ◽  
Yujie Wang ◽  
...  
Keyword(s):  
Molecular Recognition ◽  
Fluorescence Probe ◽  
Three Dimensional ◽  
Hazardous Substances ◽  
Covalent Organic Framework ◽  
Highly Sensitive ◽  
Volatile Organic ◽  
Polycyclic Aromatic ◽  
Better Than ◽  
Organic Framework

<p><a></a><a></a><a></a><a></a><a></a><a></a><a></a><a>The development of highly-sensitive recognition of </a><a></a><a></a><a></a><a></a><a>hazardous </a>chemicals, such as volatile organic compounds (VOCs) and polycyclic aromatic hydrocarbons (PAHs), is of significant importance because of their widespread social concerns related to environment and human health. Here, we report a three-dimensional (3D) covalent organic framework (COF, termed JUC-555) bearing tetraphenylethylene (TPE) side chains as an aggregation-induced emission (AIE) fluorescence probe for sensitive molecular recognition.<a></a><a> </a>Due to the rotational restriction of TPE rotors in highly interpenetrated framework after inclusion of dimethylformamide (DMF), JUC-555 shows impressive AIE-based strong fluorescence. Meanwhile, owing to the large pore size (11.4 Å) and suitable intermolecular distance of aligned TPE (7.2 Å) in JUC-555, the obtained material demonstrates an excellent performance in the molecular recognition of hazardous chemicals, e.g., nitroaromatic explosives, PAHs, and even thiophene compounds, via a fluorescent quenching mechanism. The quenching constant (<i>K</i><sub>SV</sub>) is two orders of magnitude better than those of other fluorescence-based porous materials reported to date. This research thus opens 3D functionalized COFs as a promising identification tool for environmentally hazardous substances.</p>

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