Cloning and Characterization of the Pheromone Biosynthesis Activating Neuropeptide Receptor from the Silkmoth, Bombyx mori

Hull, J. Joe; Ohnishi, Atsushi; Moto, Ken'ichi; Kawasaki, Yu; Kurata, Ryuichiro; Suzuki, Masataka; Matsumoto, Shogo

doi:10.1074/jbc.m408142200

Cited by 112 publications

(122 citation statements)

References 47 publications

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“…1). Comparisons of C-terminal intracellular regions of GPCRs indicate that PBANRs reported previously from Helicoverpa zea [3] and Bombyx mori [9] were highly similar to HevPBANR-A and HevPBANR-C, respectively (Fig. 1B). …”

Section: Molecular Identification Of Three Hevpbanr Subtypessupporting

confidence: 53%

“…In the distance tree, three moth PBANRs (HevPBANR, HezPBANR and BomPBANR) are grouped with Drosophila GPCRs CG8784 and CG8795 to produce the monophyletic 'PBANR clade' with a 97% bootstrap value. The PBANRclade is further supported by pharmacological profiles shared by its members: All receptors in this clade show marked sensitivity to pyrokinins/PBAN, which feature the FXPRLa Cterminal amino acid motif [3,9,21,26]. The PBANR clade is grouped with CG9918, mainly sensitive to CAP2b-3 and a diapause hormone (DH) analog that contains a Cterminal WFGPRLa motif [2,21].…”

Section: Phylogenetic Relationships Of Hevpbanr and Other Related Gpcrsmentioning

confidence: 90%

“…Recombinant DNA techniques used for cloning of GPCRs were described previously [9,22]. Briefly, the partial sequence of HevPBANR (Heliothis virescens PBAN receptor) was obtained from the larval CNS cDNA by performing PCRs using a set of degenerate primers.…”

Section: Cloning Of Hevpban Receptormentioning

confidence: 99%

“…In this assay, ligand-mediated activation of the GPCR mobilizes calcium from intracellular stores, resulting in a luminescent flash through oxidation of an aequorin-coelantrazine complex [9,15,22]. Expressed in CHO-WTA11, HevPBANR-C generated robust luminescence responses to PBAN and related peptides (Fig.…”

Section: Functional Expression and Pharmacological Characterization Omentioning

confidence: 99%

“…These findings suggested that the moth counterpart of CG8795 would likely encode a functional PBAN receptor. Indeed, moth orthologs of CG8795 have been identified as functional PBAN receptors in the moth Helicoverpa zea [3] and Bombyx mori [9].…”

Section: Introductionmentioning

confidence: 99%

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The pheromone biosynthesis activating neuropeptide (PBAN) receptor of Heliothis virescens: Identification, functional expression, and structure–activity relationships of ligand analogs

et al. 2008

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Pheromone biosynthesis activating neuropeptide (PBAN) promotes synthesis and release of sex pheromones in moths. We have identified and functionally expressed a PBAN receptor from Heliothis virescens (HevPBANR) and elucidated structure-activity relationships of PBAN analogs. Screening of a larval CNS cDNA library revealed three putative receptor subtypes and nucleotide sequence comparisons suggest they are produced through alternative splicing at the 3'-end. RT-PCR amplified preferentially HevPBANR-C from female pheromone glands. CHO cells expressing HevPBANR-C are highly sensitive to PBAN and related analogs, especially those sharing the C-terminal pentapeptide core, FXPRLamide (X = T, S or V). Alanine replacements in the C-terminal hexapeptide (YFTPRLamide) revealed the relative importance of each residue in the active core as follows, R 5 >L 6 >F 2 ≫P 4 >T 3 ≫Y 1 . This study provides a framework for the rational design of PBANR-specific agonists and/or antagonists that could be exploited for disruption of reproductive function in agriculturally important insect pests.

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Section: Molecular Identification Of Three Hevpbanr Subtypessupporting

confidence: 53%

Section: Phylogenetic Relationships Of Hevpbanr and Other Related Gpcrsmentioning

confidence: 90%

Section: Cloning Of Hevpban Receptormentioning

confidence: 99%

Section: Functional Expression and Pharmacological Characterization Omentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

The pheromone biosynthesis activating neuropeptide (PBAN) receptor of Heliothis virescens: Identification, functional expression, and structure–activity relationships of ligand analogs

et al. 2008

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Expression of pheromone biosynthesis activating neuropeptide and its receptor (PBANR) mRNA in adult female Spodoptera exigua (Lepidoptera: Noctuidae)

Cheng

LiZhi

Jiang

et al. 2010

Arch Insect Biochem Physiol

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The full-length cDNA of pheromone biosynthesis activating neuropeptide receptor (PBANR) was cloned from the beet armyworm, Spodoptera exigua (Hübner) (Lepidoptera: Noctuidae); it included an open reading frame of 1,053 bp encoding 350 amino acids. The PBANR of S. exigua (SePBANR) was structurally characteristic of G protein-coupled receptor and its amino acid sequence shared 98% identity with the PBANR of Spodoptera littoralis. Both pheromone biosynthesis activating neuropeptide (PBAN) and PBANR mRNA abundance were measured in the brain-subesophageal ganglion complex, pheromone gland, ventral nerve cord, and ovary of S. exigua female moths by real-time RT-PCR. The abundance of PBAN mRNA in brain-subesophageal ganglion complex and PBANR mRNA in pheromone gland was significantly greater compared to other tissues, suggesting that the ligand-receptor relationship of PBAN and PBANR exists quantitatively in S. exigua. Both PBAN and PBANR expression displayed a remarkable diurnal rhythm, for they were low and stable during the photophase (07:00-21:00) and increased markedly during the scotophase (with a maximum abundance at 23:30) in 3-day-old female moths. The abundance of PBAN and PBANR increased steadily from the 1st day to the 5th day of the adult female life. The pattern of both diurnal and daily expression of PBAN and PBANR mRNA were coincident with enhanced capacity of sex pheromone release and mating of S. exigua moths during the same period. We infer from these results that pheromone biosynthesis and release in S. exigua is regulated by PBAN via up-regulating synthesis.

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Suppression of PBAN receptor expression reduces fecundity in the fall armyworm, Spodoptera frugiperda

Park

Vatanparast

2022

Arch Insect Biochem Physiol

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The fall armyworm, Spodoptera frugiperda, native to the tropical and subtropical areas of the American continent is one of the world's most destructive insect pests. In most insects, sex pheromone production is initiated following the activation of a pheromone‐biosynthesis‐activating neuropeptide (PBAN) receptor, which belongs to G protein‐coupled receptor. We explored expression level of S. frugiperda PBAN receptor (Sf‐PBANr) gene and validated the physiological function by assessing the fecundity of adult females subjected to its specific RNA interference (RNAi). Sf‐PBANr was predicted from a transcriptome of S. frugiperda. Reverse‐transcription polymerase chain reaction assay showed its expression in all developmental stages of S. frugiperda. Specific suppression of Sf‐PBANr by RNAi in either sex significantly reduced the total number of laid eggs per adult female. Matings between both RNAi‐treated males and female resulted in 63.3% reduction in fecundity. In contrast, the RNAi effect was less 47.5%–49.5% at the matings from single‐parent RNAi treatment. These results suggest that the Sf‐PBANr is associated with female of S. frugiperda.

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Cloning and Characterization of the Pheromone Biosynthesis Activating Neuropeptide Receptor from the Silkmoth, Bombyx mori

Cited by 112 publications

References 47 publications

The pheromone biosynthesis activating neuropeptide (PBAN) receptor of Heliothis virescens: Identification, functional expression, and structure–activity relationships of ligand analogs

The pheromone biosynthesis activating neuropeptide (PBAN) receptor of Heliothis virescens: Identification, functional expression, and structure–activity relationships of ligand analogs

Expression of pheromone biosynthesis activating neuropeptide and its receptor (PBANR) mRNA in adult female Spodoptera exigua (Lepidoptera: Noctuidae)

Suppression of PBAN receptor expression reduces fecundity in the fall armyworm, Spodoptera frugiperda

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