Three pheromone-binding proteins help segregation between two Helicoverpa species utilizing the same pheromone components

Guo, Hao; Huang, Ling-Qiao; Pelosi, Paolo; Wang, Chen‐Zhu

doi:10.1016/j.ibmb.2012.06.004

Cited by 65 publications

(48 citation statements)

References 43 publications

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“…The protein renaturation and extensive dialysis were performed with a linear gradient of urea. This treatment does not affect the structure of insect OBPs, as previously demonstrated (Ban et al 2003b; Guo et al 2012). The protein production was with an N-terminal His tag, which was cleaved by thrombin (Sigma, USA).…”

Section: Methodssupporting

confidence: 76%

“…Figure S5 reports the expression and purification of them. Then, we performed competitive ligand-binding experiments using well established protocols for other insect OBPs (Ban et al 2002, 2003b; Guo et al 2012; He et al 2010; Zhou et al 2009) to investigate the specificity of the binding pocket in the three D. tabulaeformis OBPs. The probe was excited at 337 nm, and emission spectra were recorded between 380 and 450 nm.…”

Section: Resultsmentioning

confidence: 99%

“…The first OBP, also the first pheromone-binding protein (PBP), that was identified from Antheraea polyphemus (Lepidoptera: Saturniidae) (Vogt and Riddiford 1981). Since then, OBPs have been identified from various insect species (e.g., Garczynski et al 2012; Gu et al 2011; Guo et al 2012; Krieger et al 2004; Picimbon and Gadenne 2002; Vogt 2002; Xiu and Dong 2007; Xiu et al 2008; Zhang et al 2009; Zheng et al 2013; Zhu et al 2013). Among Lepidoptera, there are two important classes of OBPs, PBPs and general odorant binding proteins (GOBPs), with the GOBPs further classified into GOBP1 and GOBP2 subgroups (Gong et al 2009b; Pelosi et al 2006).…”

Section: Introductionmentioning

confidence: 99%

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Molecular Characterization, Expression Pattern, and Ligand-Binding Property of Three Odorant Binding Protein Genes from Dendrolimus tabulaeformis

Zhang

Wang

et al. 2014

J Chem Ecol

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Odorant binding proteins (OBPs) play important roles in insect olfactory processes. The Chinese pine caterpillar moth, Dendrolimus tabulaeformis (Lepidoptera, Lasiocampidae) is a serious economic pest in China, and the pheromones of this species have been identified to monitor their presence. However, the molecular mechanisms by which D. tabulaeformis perceive pheromones and host volatiles remain unknown. In this study, we identified and characterized three new OBPs, including one pheromone binding protein (PBP1) and two general odor binding proteins (GOBPs), from antennal cDNA of D. tabulaeformis. The deduced amino acid sequences of DtabPBP1, DtabGOBP1, and DtabGOBP2 revealed mature proteins of 140, 147, and 140 amino acids, respectively. Each has six cysteine residues in conserved positions relative to other known OBPs. Amino-acid alignments indicated that the two GOBPs are more conserved (DtabGOBP1 is 52.9–67.4 % identical to orthologs from other Lepidoptera, and DtabGOBP2 is 55.2–81.8 % identical) than the PBP (32.5–46.0 %). Real-time PCR indicated tissue- and sex-specific expression patterns of the three genes. DtabPBP1 was mainly expressed in the antennae of males, whereas female antennae had only 1.09 % the expression in male antennae. Both DtabGOBP1 and DtabGOBP2 were more highly expressed in antennae than in other tissues, while DtabGOBP1 was more abundant in male antennae and DtabGOBP2 in female antennae. In addition, the binding specificities of the three proteins were investigated, and all three OBPs exhibited high binding affinities for the pheromone component (5Z,7E)-5,7-dodecadien-1-yl propionate (Z5,E7-12:OPr). This suggests a role in binding pheromone for GOBPs, as well as PBP1, in D. tabulaeformis.Electronic supplementary materialThe online version of this article (doi:10.1007/s10886-014-0412-6) contains supplementary material, which is available to authorized users.

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Section: Methodssupporting

confidence: 76%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Molecular Characterization, Expression Pattern, and Ligand-Binding Property of Three Odorant Binding Protein Genes from Dendrolimus tabulaeformis

Zhang

Wang

et al. 2014

J Chem Ecol

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“…This means that the conformational change reported for the PBP1 of B. mori , where the formation of the seventh α-helix was observed at pH 4–5 [17], [18], does not occur in our protein. Indeed, when examining the sequence of Harm OBP7 we could not expect such conformational change, as the C-terminus in this protein is 15 amino acid shorter than that of BmorPBP1, which is instead of the same length as in the three PBPs of Helicoverpa species [27]. In other OBPs of this sub-group (i.e.…”

Section: Resultsmentioning

confidence: 93%

A Lysine at the C-Terminus of an Odorant-Binding Protein is Involved in Binding Aldehyde Pheromone Components in Two Helicoverpa Species

et al. 2013

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Odorant-binding proteins (OBPs) are soluble proteins, whose role in olfaction of insects is being recognized as more and more important. We have cloned, expressed and purified an OBP (HarmOBP7) from the antennae of the moth Helicoverpa armigera. Western blot experiments indicate specific expression of this protein in the antennae of adults. HarmOBP7 binds both pheromone components Z-11-hexadecenal and Z-9-hexadecenal with good affinity. We have also performed a series of binding experiments with linear aldehydes, alcohols and esters, as well as with other compounds and found a requirement of medium size for best affinity. The affinity of OBP7, as well as that of a mutant lacking the last 6 residues does not substantially decrease in acidic conditions, but increases at basic pH values with no significant differences between wild-type and mutant. Binding to both pheromone components, instead, is negatively affected by the lack of the C-terminus. A second mutant, where one of the three lysine residues in the C-terminus (Lys123) was replaced by methionine showed reduced affinity to both pheromone components, as well as to their analogues, thus indicating that Lys123 is involved in binding these compounds, likely forming hydrogen bonds with the functional groups of the ligands.

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“…Two important classes of OBPs in Lepidoptera, pheromone binding protein and general odorant binding protein, are primarily expressed in antennae of both sexes and are involved in the detection of sex pheromone components and plant volatiles, respectively, in species such as Helicoverpa armigera [27], Plutella xylostella [28] and Spodoptera exigua [29]. Our qPCR data showed that PameOBP1 and 2 were specifically expressed at high levels in antennae, and showed a strong male bias, suggesting that they might be involved in odorant or pheromone discrimination in P .…”

Section: Discussionmentioning

confidence: 99%

Molecular and Functional Characterization of Three Odorant-Binding Protein from Periplaneta americana

Zhang

et al. 2017

PLoS ONE

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The American cockroach, Periplaneta americana, is a vector of many pathogenic organisms associated with human diseases. Olfaction plays a crucial role in guiding cockroach behaviors and contributes to their ability to transmit pathogens. Odorant binding proteins (OBPs), abundant in the insect olfactory sensilla, are important for insect olfaction. In this study, three OBP genes, PameOBP1, 2 and 3, were cloned from P. americana. Sequence alignment and phylogenetic analysis revealed that PameOBP1, 2 and 3 belong to the Minus-C OBP, Classic OBP, and Plus-C OBP subfamilies, respectively. Expression pattern and ligand-binding analysis showed that PameOBP1 and 2 were specifically expressed in antennae, and exhibited high binding affinities (Ki < 2 μM) to farnesene, farnesol, 2-tridecanone, and tetradecane, suggesting roles in volatile perception. Conversely, PameOBP3 was ubiquitously expressed in most of the tissues examined at high levels and displayed very weak binding affinities (Ki > 40 μM) for all 87 ligands tested. Our study provides insights into the functional diversity of PameOBP genes and provides some volatiles that can potentially be used in behavioral interference of P. americana.

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Three pheromone-binding proteins help segregation between two Helicoverpa species utilizing the same pheromone components

Cited by 65 publications

References 43 publications

Molecular Characterization, Expression Pattern, and Ligand-Binding Property of Three Odorant Binding Protein Genes from Dendrolimus tabulaeformis

Molecular Characterization, Expression Pattern, and Ligand-Binding Property of Three Odorant Binding Protein Genes from Dendrolimus tabulaeformis

A Lysine at the C-Terminus of an Odorant-Binding Protein is Involved in Binding Aldehyde Pheromone Components in Two Helicoverpa Species

Molecular and Functional Characterization of Three Odorant-Binding Protein from Periplaneta americana

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