Binding specificity of locust odorant binding protein and its key binding site for initial recognition of alcohols

Jiang, Quanyong; Wang, Weixuan; Zhang, Ziding; Zhang, Long

doi:10.1016/j.ibmb.2009.04.004

Cited by 64 publications

(68 citation statements)

References 39 publications

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“…Dilution of primary antibody was 1:5,000 in A, C and 1:10000 in B, D. Secondary antibody was anti-rabbit IgG conjugated with 10 nm colloidal gold granules at a dilution of 1:20. (C16), heptadecanol (C17), were potential competitors that could displace 1-NPN more effectively than that with short-chain (C6-C10) ligands (Jiang et al, 2009). However, in our case, these C11-C17 aliphatic alcohols completely failed to bind to AlinOBP1 or showed very weak binding affinity, even at the concentrations of 50 mM (Table 3).…”

Section: Discussionmentioning

confidence: 99%

“…6B), which could form hydrogen bonds and to enhance the binding to ligands such as b-ionone. Some of the hydrophilic residues locate in the opening of the binding cavity (Jiang et al, 2009) and are likely to be involved in the formation of hydrogen bonds with the functional group of ligands and play a key role in the initial ligand recognition. However, these presumptions need to be confirmed by real 3D structure of AlinOBP1 which can be solved by X-ray diffraction or NMR.…”

Section: Discussionmentioning

confidence: 99%

“…The most widely used fluorescent probe is N-phenyl-1-naphthylamine (1-NPN), which has been employed in the binding of Drosophila LUSH (Zhou et al, 2004), the Locusta migratoris LmigOBP1-3 (Jiang et al, 2009;Yu et al, 2009), the social wasp Polistes dominulus OBP1 (Calvello et al, 2003) and Bombyx mori OBPs (Zhou et al, 2009;He et al, 2010).…”

Section: Introductionmentioning

confidence: 99%

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Functional characterization and immunolocalization of odorant binding protein 1 in the lucerne plant bug, Adelphocoris lineolatus (GOEZE)

Wang

et al. 2011

Arch Insect Biochem Physiol

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In the insect phylum, the relationships between individuals and their environment are often modulated by chemical communication. Odorant binding proteins (OBPs) are widely and robustly expressed in insect olfactory organs and play a key role in chemosensing and transporting hydrophobic odorants across the sensillum lymph to the olfactory receptor neuron. In this study, a novel OBP gene (AlinOBP1) in the lucerne plant bug, Adelphocoris lineolatus was identified, cloned and expressed. Real-time PCR results indicated that the expression level of AlinOBP1 gene differed in each developmental stage (from first instar to adult) and was predominantly expressed in the antennae of adults. The expression level of AlinOBP1 was 1.91 times higher in male antennae than in female antennae. The binding properties of AlinOBP1 with 114 odorants were measured using a fluorescence probe, N-phenyl-1-naphthylamine (1-NPN), with fluorescence competitive binding. The results revealed that AlinOBP1 exhibits high binding abilities with two major putative pheromone components, ethyl butyrate and trans-2-hexenyl butyrate. In addition, it was observed that six volatiles released from cotton, octanal, nonanal, decanal, 2-ethyl-1-hexanol, b-caryophyllene and b-ionone also bind to AlinOBP1. Immunocytochemistry analysis showed that AlinOBP1 was expressed in the sensillum lymph of sensilla trichodica and sensilla basiconca. Our results demonstrate that AlinOBP1 may function as a carrier in the chemoperception of the lucerne plant bug. C 2011 Wiley Periodicals, Inc.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Functional characterization and immunolocalization of odorant binding protein 1 in the lucerne plant bug, Adelphocoris lineolatus (GOEZE)

Wang

et al. 2011

Arch Insect Biochem Physiol

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“…The following are representative examples with 1-NPN as the fluorescent probe. The OBP1 of the migratory locust, Locusta migratoria (Orthoptera: Acrididae) does not bind fecal or green leaf volatiles, but shows high affinity to some linear aliphatic compounds, with pentadecanol and 2-pentadecanone binding with the highest affinity (Jiang et al, 2009). The affinity of 12 compounds to three aphid OBPs were measured in competitive binding experiments.…”

Section: Introductionmentioning

confidence: 99%

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

Zhang

Chen

et al. 2010

J Chem Ecol

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Chemoreception in insects is mediated by small odorant-binding proteins (OBPs) that are believed to carry lipophilic stimuli to the olfactory receptor cells through the aqueous sensillar lymph. Binding experiments and recent structural studies of OBPs have illustrated their versatility and ability to accommodate ligands of different shapes and chemical structures. We expressed and purified seven recombinant OBPs (MmedOBP1-MmedOBP7) from the parasitic wasp, Microplitis mediator (Hymenoptera: Braconidae) in a prokaryotic expression system. With 4,4'-dianilino-1,1'-binaphthyl-5,5'-sulfonic acid (bis-ANS) as a fluorescent probe, the ligand-binding specificities of these seven MmedOBPs with 50 small organic compounds were investigated in vitro. The results revealed that all of the M. mediator OBPs can bind a wide variety of odorant molecules with different binding affinities. The best ligand for all seven MmedOBPs was β-ionone. MmedOBP2 showed affinity for some aromatic compounds, whereas MmedOBP4 and MmedOBP6 bound several terpenoids. MmedOBP5 bound β-ionone, but did not bind any of the other potential ligands that we tested.

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“…Most importantly, the dissociation constants of OBPs with various competitors can be measured [31]. The most widely used fluorescence probe is N-phenyl-1-naphthylamine (1-NPN), which has been employed in binding experiments with insect OBPs, such as Drosophila LUSH [32], the Locusta migratoris OBPs [28,33], Bombyx mori OBPs [29], Chilo suppressalis GOBP2 [30], Acyrthosiphon pisum OBPs [17] and Aedes aegypti OBP [34].…”

mentioning

confidence: 99%

Cloning, expression and binding specificity analysis of odorant binding protein 3 of the lucerne plant bug, Adelphocoris lineolatus (Goeze)

Sun

Ren

et al. 2010

Chin. Sci. Bull.

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Credible evidence shows that odorant binding proteins (OBPs) are required for insect olfaction perception and play a key role in transporting hydrophobic odorants across the sensillum lymph to the olfactory receptors (ORs). In the present study, a novel OBP (AlinOBP3) gene from the lucerne plant bug, Adelphocoris lineolatus, was cloned and expressed. The expression pattern of AlinOBP3 was evaluated by qPCR, which indicated that AlinOBP3 was dominantly expressed in antennae. The binding properties of AlinOBP3 with 9 cotton volatiles and 5 sex pheromone analogs were measured by fluorescence competitive binding assays with the fluorescence probe 1-NPN. The results revealed that of 9 cotton volatiles, Myrcene, β-Ocimene and α-Phellandrene can bind with AlinOBP3. α-Phellandrene especially bound to AlinOBP3 with a high binding affinity, with a dissociation constant of 56.68 μmol/L. Of the 5 sex pheromone analogs, Hexyl butyrate had the strongest binding affinity with AlinOBP3, with a dissociation constant as 59.53 μmol/L. Butyl butyrate, trans-2-Hexenyl butyrate and Ethyl butyrate had medium binding affinities with AlinOBP3, with dissociation constants of 227.39, 108.77 and 143.47 μmol/L, respectively. The results suggest that AlinOBP3 might be a pheromone binding protein (PBP) with a dual-function for the perception of sex pheromones and plant volatiles. Adelphocoris lineolatus (Goeze), odorant binding protein, gene expression, Western blot, expression pattern, fluorescence competitive binding assays Citation: Gu S H, Sun Y, Ren L Y, et al. Cloning, expression and binding specificity analysis of odorant binding protein 3 of the lucerne plant bug, Adelphocoris lineolatus (Goeze).

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Binding specificity of locust odorant binding protein and its key binding site for initial recognition of alcohols

Cited by 64 publications

References 39 publications

Functional characterization and immunolocalization of odorant binding protein 1 in the lucerne plant bug, Adelphocoris lineolatus (GOEZE)

Functional characterization and immunolocalization of odorant binding protein 1 in the lucerne plant bug, Adelphocoris lineolatus (GOEZE)

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

Cloning, expression and binding specificity analysis of odorant binding protein 3 of the lucerne plant bug, Adelphocoris lineolatus (Goeze)

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