scholarly journals Contribution of odorant binding proteins to olfactory detection of (Z)-11-hexadecenal in Helicoverpa armigera

2020 ◽  
Author(s):  
Hao Guo ◽  
Ping-Ping Guo ◽  
Ya-Lan Sun ◽  
Ling-Qiao Huang ◽  
Chen-Zhu Wang
Keyword(s):  
Helicoverpa Armigera ◽  
Binding Proteins ◽  
Supporting Cells ◽  
Odorant Binding Proteins ◽  
Sensilla Trichodea ◽  
Helicoverpa Armígera ◽  
Olfactory Detection ◽  
Receptor Neurons ◽  
Pheromone Binding Proteins ◽  
Odorant Binding

AbstractHelicoverpa armigera utilizes (Z)-11-hexadecenal (Z11-16:Ald) as its major sex pheromone component. Three pheromone binding proteins (PBPs) and two general odorant binding proteins (GOBPs) are abundantly expressed in male antennae of H. armigera. However, their precise roles in the olfactory detection of Z11-16:Ald remain enigmatic. To answer this question, we first synthesized the antibody against HarmOR13, a pheromone receptor (PR) primarily responding to Z11-16:Ald and mapped the local associations between PBPs / GOBPs and HarmOR13. Immunostaining showed that HarmPBPs and HarmGOBPs were localized in the supporting cells of sensilla trichodea and sensilla basiconica respectively. In particular, HarmPBP1 and HarmPBP2 were colocalized in the cells surrounding the olfactory receptor neurons (ORNs) expressing HarmOR13. Next, using two noninterfering binary expression tools, we heterologously expressed HarmPBP1, HarmPBP2 and HarmOR13 in Drosophila T1 sensilla to validate the functional interplay between PBPs and HarmOR13. We found that the addition of HarmPBP1 or HarmPBP2 significantly increased the sensitivity of HarmOR13 to Z11-16:Ald. However, the presence of either HarmPBP1 or HarmPBP2 was ineffective to change the tuning breadth of HarmOR13. Taken together, our results support the idea that PBPs are contributors to the peripheral olfactory sensitivity but do not affect the selectivity. Lastly, we discovered that HarmOR13 and the Drosophila OR67d employed a similar coding mechanism to detect pheromones, suggesting that pheromone detection across different insect orders appears to co-opt a conserved molecular principle to recognize pheromone ligands.

scholarly journals Odorant binding proteins promote flight activity in the migratory insect, Helicoverpa armigera

2020 ◽  
Vol 29 (19) ◽  
pp. 3795-3808
Author(s):  
Shang Wang ◽  
Melissa Minter ◽  
Rafael A. Homem ◽  
Louise V. Michaelson ◽  
Herbert Venthur ◽  
...  
Keyword(s):  
Helicoverpa Armigera ◽  
Binding Proteins ◽  
Flight Activity ◽  
Odorant Binding Proteins ◽  
Helicoverpa Armígera ◽  
Odorant Binding

scholarly journals A pheromone-binding protein from the cockroach Leucophaea maderae: cloning, expression and pheromone binding

2003 ◽  
Vol 371 (2) ◽  
pp. 573-579 ◽  
Author(s):  
Stéphane RIVIÈRE ◽  
Audrey LARTIGUE ◽  
Brigitte QUENNEDEY ◽  
Valérie CAMPANACCI ◽  
Jean-Pierre FARINE ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Volatile Compounds ◽  
Binding Proteins ◽  
Sexual Pheromone ◽  
Female Adult ◽  
Odorant Binding Proteins ◽  
Leucophaea Maderae ◽  
Pheromone Components ◽  
Pheromone Binding Proteins ◽  
Odorant Binding

Odorant-binding proteins (OBPs) are thought to transport volatile compounds from air to their receptors through the sensillary lymph. In this protein family, the subgroup of pheromone-binding proteins (PBPs) is specifically tuned to the perception of the sexual pheromone. To date, the description of OBPs has been restricted to Endopterygota and Paraneoptera. Their expression in Orthopteroid has been hypothesized, but no evidence of OBP has been produced in this assemblage to date. In the present study, we describe the first OBP from a Dictyopteran insect that belongs to the cockroach Leucophaea maderae. The PBP of L. maderae (PBPLma) shares all the hallmarks of the OBP family and is expressed specifically in the female adult antennae, the sex that perceives the sexual pheromone. The affinity of the recombinant PBPLma produced in the Escherichia coli periplasm for the pheromonal compounds has been tested by displacement of a fluorophore, 8-anilino-1-naphtalenesulphonic acid (ANS). Our results suggest that two chemically close compounds of the pheromonal blend (3-hydroxy-butan-2-one and butane-2,3-diol) are capable of displacing ANS, whereas two other pheromone components (E-2-octenoic acid and senecioic acid) and other alkyl volatile compounds are not capable of displacing ANS, indicating a certain filtering of binding, which can be correlated with the putative function.

scholarly journals Comparative Genomics Provide Insights Into Function and Evolution of Odorant Binding Proteins in Cydia pomonella

2021 ◽  
Vol 12 ◽  
Author(s):  
Cong Huang ◽  
Xue Zhang ◽  
Dongfeng He ◽  
Qiang Wu ◽  
Rui Tang ◽  
...  
Keyword(s):  
Binding Proteins ◽  
Cydia Pomonella ◽  
Purifying Selection ◽  
Codling Moth ◽  
Economic Losses ◽  
Odorant Binding Proteins ◽  
Host Seeking ◽  
Receptor Neurons ◽  
Gains And Losses ◽  
Odorant Binding

Insect olfaction is vital for foraging, mating, host-seeking, and avoidance of predators/pathogens. In insects, odorant binding proteins (OBPs) are involved in transporting hydrophobic odor molecules from the external environment to receptor neurons. The codling moth, Cydia pomonella, one of the most destructive insect fruit pests, causes enormous economic losses. However, little is known about the number, variety, gains and losses, and evolution of OBP genes in C. pomonella. Here we report the identification of 40 OBPs in C. pomonella, most (75%) of which are classic OBPs, using genomic and transcriptomic analyses. Two OBP genes were lost in C. pomonella relative to possible distant ancestor in Lepidoptera lineage based on an analysis of gene gains and losses. The phylogenetic tree and chromosome location showed that the expansion of OBP genes mainly resulted from tandem duplications, as the CpomGOBP2 gene was duplicated twice along with loss of CpomPBPB. Two positive selection sites of the CpomGOBP1 gene were identified while other OBP genes evolved under purifying selection. Our results provide fundamental knowledge of OBP genes allowing further study of their function in C. pomonella.

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