PBAN selective antagonists: inhibition of PBAN induced cuticular melanization and sex pheromone biosynthesis in moths

Ben-Aziz, Orna; Zeltser, Irina; Altstein, Miriam

doi:10.1016/j.jinsphys.2004.11.017

Cited by 21 publications

(3 citation statements)

References 65 publications

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“…Here we report, for the first time, the expression and characterization of another PBAN-R, which is expressed in the larval stage and which most likely, is the receptor involved in other PK/PBAN functions during the insect larval stage, such as cuticular melanization (Ben-Aziz et al, 2005) or potential regulation of pupal diapause (Sun et al, 2005;Xu and Denlinger, 2003). Diapause is an adaptive stage in which the insects temporarily stagnate, in order to survive an unfavorable environmental condition.…”

Section: Discussionmentioning

confidence: 96%

Cloning and characterization of the pheromone biosynthesis activating neuropeptide receptor gene in Spodoptera littoralis larvae

Zheng

Lytle

Njauw

et al. 2007

Gene

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Section: Discussionmentioning

confidence: 96%

Cloning and characterization of the pheromone biosynthesis activating neuropeptide receptor gene in Spodoptera littoralis larvae

Zheng

Lytle

Njauw

et al. 2007

Gene

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“…The PK/PBAN family of neuropeptides elicits a broad array of physiological activities in insect bioassays, including pheromonotropic (1-5), cuticular melanization (15,16), pupariation (26), and hindgut myotropic (1,28) in a variety of insects. In each of these assays, the active core, the minimum sequence capable of eliciting significant activity, has been identified as the C-terminal pentapeptide FXPRLa (X = S,T,G or V) that defines the PK/PBAN family (29)(30)(31)(32)(33)(34).…”

Section: Discussionmentioning

confidence: 99%

A novel dihydroimidazoline trans-Pro mimetic analog is a selective PK PBAN agonist

Nachman

O²,

Davidovitch³

et al. 2010

Front Biosci

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The pyrokinin/pheromone biosynthesis activating neuropeptide (PK/PBAN) family plays a significant role in the regulation of reproductive and developmental processes in a variety of insects. A transPro, type I beta-turn has been previously identified as important for the activity of PK/PBAN peptides. A PK/PBAN analog (PPK-Jo) incorporating a novel dihydroimidazole transPro mimetic motif was evaluated in four PK/PBAN bioassays (pheromonotropic, melanotropic, pupariation and hindgut myotropic). PPK-Jo proved to be a pure, selective melanotropic agonist in S. littoralis. The melanotropic receptor in S. littoralis demonstrates more tolerance to deviations from the ideal transPro structure than those of other PK/PBAN assays. The selective PK/PBAN agonist represents a new tool to better understand the endogenous mechanisms of these peptides and serves as a probe of the plasticity of PK/PBAN regulated systems and receptors. The dihydroimidazoline moiety is shown to function as a surrogate for a transPro in certain circumstances, and provides a novel scaffold with which to construct mimetic PK/PBAN analogs with enhanced selectivity and the potential to disrupt critical physiological processes in insect pests.

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“…These results showed that BomPBANR recognizes the amino acid residue at C6 position and type I β-turn secondary structure (Nachman et al, 1993). We also synthesized and examined a peptide substituted with d -Phe at C4 position [RYFdFPRLamide, LA-4] which had been reported as a linear antagonist (Zeltser et al, 2000; Ben-Aziz et al, 2005) and demonstrated that LA-4 was a partial agonist to BomPBANR (Kawai et al, 2009). …”

Section: Introductionmentioning

confidence: 99%

The Arginine Residue within the C-Terminal Active Core of Bombyx mori Pheromone Biosynthesis-Activating Neuropeptide is Essential for Receptor Binding and Activation

Kawai¹,

Lee²,

Nagata³

et al. 2012

Front. Endocrin.

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In most lepidopteran insects, the biosynthesis of sex pheromones is regulated by pheromone biosynthesis-activating neuropeptide (PBAN). Bombyx mori PBAN (BomPBAN) consists of 33 amino acid residues and contains a C-terminus FSPRLamide motif as the active core. Among neuropeptides containing the FXPRLamide motif, the arginine (Arg, R) residue at the second position from the C-terminus is highly conserved across several neuropeptides, which can be designated as RXamide peptides. The purpose of this study was to clarify the role of the Arg residue in the BomPBAN active core. We synthesized 10-residue peptides corresponding to the C-terminal part of BomPBAN with a series of replacements at the second position from the C-terminus, termed the C2 position, and measured their efficacy in stimulating Ca2+ influx in insect cells expressing a fluorescent PBAN receptor chimera (PBANR–EGFP) using the fluorescent Ca2+ indicator, Fura Red–AM. The PBAN analogs with the C2 position replaced with alanine (Ala, A), aspartic acid (Asp, D), serine (Ser, S), or l-2-aminooctanoic acid (Aoc) decreased PBAN-like activity. RC2A (SKTRYFSPALamide) and RC2D (SKTRYFSPDLamide) had the lowest activity and could not inhibit the activity of PBAN C10 (SKTRYFSPRLamide). We also prepared Rhodamine Red-labeled peptides of the PBAN analogs and examined their ability to bind PBANR. In contrast to Rhodamine Red-PBAN C10 at 100 nM, none of the synthetic analogs exhibited PBANR binding at the same concentration. Taken together, our results demonstrate that the C2 Arg residue in BomPBAN is essential for PBANR binding and activation.

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PBAN selective antagonists: inhibition of PBAN induced cuticular melanization and sex pheromone biosynthesis in moths

Cited by 21 publications

References 65 publications

Cloning and characterization of the pheromone biosynthesis activating neuropeptide receptor gene in Spodoptera littoralis larvae

Cloning and characterization of the pheromone biosynthesis activating neuropeptide receptor gene in Spodoptera littoralis larvae

A novel dihydroimidazoline trans-Pro mimetic analog is a selective PK PBAN agonist

The Arginine Residue within the C-Terminal Active Core of Bombyx mori Pheromone Biosynthesis-Activating Neuropeptide is Essential for Receptor Binding and Activation

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