Effect of synthetic pban and derived peptides on sex pheromone biosynthesis in Heliothis peltigera (Lepidoptera: Noctuidae)

Gazit, Yoav; Dunkelblum, E.; Benichis, Marina; Altstein, Miriam

doi:10.1016/0020-1790(90)90104-3

Cited by 52 publications

(64 citation statements)

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“…4B). This result clearly demonstrates the C-terminal pentapeptide is the active core domain of PBAN, critical for interaction with the HevPBANR, in agreement with pheromonotropic bioassays in Heliothine insects [6,11,25].…”

Section: Structure-activity Relationships Of Pban-related Agonists Onsupporting

confidence: 81%

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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: Structure-activity Relationships Of Pban-related Agonists Onsupporting

confidence: 81%

“…The C-terminal pentapeptide fragment of PBAN-related peptides is critical for myotropic activity [18] and subsequently for their pheromonotropic function [6,25]. This is shown in the current study to be equally true for the PBANR receptor from H. virescens.…”

Section: Pharmacological Profile Supports a Role As The Physiologicalsupporting

confidence: 60%

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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“…These peptides have been synthesized and the synthetic peptides retain biological activity, with cross-reactivity occurring in other species of moths (3,4,6,7). These reports and others indicate that a variety of moths utilize PBAN or PBAN-like peptides in controlling pheromone biosynthesis.…”

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confidence: 99%

Stimulation of pheromone biosynthesis in the moth Helicoverpa zea: action of a brain hormone on pheromone glands involves Ca2+ and cAMP as second messengers.

Jurenka

Jacquin

Roelofs

1991

Proc. Natl. Acad. Sci. U.S.A.

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Isolated abdomen and pheromone gland bioassays were utilized to determine the physiological action of the pheromone-biosynthesis-activating neuropeptide (PBAN) in the corn earworm moth Helicoverpa (= Heliothis) zea. An isolated pheromone gland bioassay showed that synthetic PBAN was active at 0.02 pmol, with maximal activity occurring at 0.5 pmol and 60 min of incubation. Second-messenger studies demonstrated that extracellular Ca2+ is necessary for PBAN activity on isolated pheromone glands. The Ca2+ ionophore A23187 stimulated pheromone biosynthesis alone, whereas the Ca2+ channel blockers La3' and Mn2+ inhibited PBAN activity. However, the organic Ca2+ channel blockers verapamil and nifedipine did not inhibit PBAN activity. Both forskolin and two cAMP analogues stimulated pheromone biosynthesis in the absence of extracellular Ca2+, indicating that Ca2+ may activate an adenylate cyclase. The biogenic amine octopamine did not elicit pheromone production in isolated gland or abdomen bioassays or when in ected into intact female moths. Removal of the ventral nerve chord, including the terminal abdominal ganglia in isolated abdomens, did not affect PBAN stimulation of pheromone production. Similar levels of stimulation were found when isolated abdomens were treated with PBAN in scotophase or photophase.Sex pheromone titers in most moths, including the corn earworm moth Helicoverpa (= Heliothis) zea, fluctuate diurnally with little or no pheromone present during the day and with peak pheromone titers occurring during midscotophase (1). This fluctuation is caused by the release and/or degradation of existing pheromone and the biosynthesis of new pheromone at precise times of the photoperiod. The biosynthesis of pheromone in H. zea is regulated by a peptide produced in the subesophageal ganglion (SEG) portion of the brain complex of female moths (2). This peptide, termed pheromone-biosynthesis-activating neuropeptide (PBAN), has been isolated and sequenced from brains of H. zea (3).Two other pheromonotropic peptides, each with about 80%o sequence identity with H. zea PBAN, have been isolated from the brains of the silkworm, Bombyx mori (4, 5). These peptides have been synthesized and the synthetic peptides retain biological activity, with cross-reactivity occurring in other species of moths (3, 4, 6, 7). These reports and others indicate that a variety of moths utilize PBAN or PBAN-like peptides in controlling pheromone biosynthesis.Although PBAN or PBAN-like activity has been identified in several different moth species, the physiological mode of action of PBAN has not been determined conclusively for any one species. In fact, there are two apparently conflicting hypotheses on how PBAN activates pheromone biosynthesis, and both are based on studies utilizing Heliothis moths as experimental animals. One hypothesis suggests that PBAN is synthesized in the SEG, transported to the corpora cardiaca, and then released into the hemolymph, where it can act on the pheromone gland to induce pheromone biosynthesis (8)....

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“…Backbone cyclization also acquires peptides with higher potency, enhanced metabolic stability, and improved bioavailability. The advantages introduced by backbone cyclization and cycloscan as well as the availability of bioassays for the pyrokinin/PBAN family of peptides (23,39,43,44) (which are required to obtain the essential information for the design of BBC peptides and specificity for the desired biological effects), led us to combine both approaches for the generation of receptor-selective agonists and antagonists.…”

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confidence: 99%

“…The members of this family have been found to be responsible for a variety of physiological and behavioral functions such as: contraction of the locust oviduct (32), myotropic activity of the cockroach and locust hindgut (32,42), egg diapause in the silkworm (41), and acceleration of pupariation in the fleshfly larvae (43), in addition to stimulation of sex pheromone biosynthesis in female moths (12)(13)(14)44) and melanization and reddish coloration in moth larvae (23,45).…”

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confidence: 99%

Backbone Cyclic Peptide Antagonists, Derived from the Insect Pheromone Biosynthesis Activating Neuropeptide, Inhibit Sex Pheromone Biosynthesis in Moths

Altstein¹,

Ben-Aziz²,

Daniel³

et al. 1999

Journal of Biological Chemistry

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We describe an application of the backbone cyclization and cycloscan concept for the design and synthesis of pheromone biosynthesis activating neuropeptide (PBAN) antagonists capable of inhibiting sex pheromone biosynthesis in Heliothis peltigera female moths. Two backbone cyclic (BBC) sub-libraries were designed and synthesized. The structure of the first sub-library ([Arg 27 ]PBAN27-33NH 2 , termed the Ser sub-library) was based on the active C-terminal hexapeptide sequence (Tyr-Phe-Ser-Pro-Arg-Leu-NH 2 ) of PBAN1-33NH 2 , which was found to comprise its active core. It is well established that the activation of multiple receptors by the same peptide arises from the ability of a given peptide to exist in different interchangeable bioactive conformations (1). To attain receptor selectivity it is, therefore, essential to restrict the conformational space of a peptide so it can attain one bioactive conformation.Cyclization is an important and attractive way to restrict the conformational space of peptidic structures (1). Conformationally restricted peptides containing medium and long range cyclizations have been mainly prepared following the same modes of cyclization of naturally occurring peptides. These include end-to-end, side-chain-to-side-chain, and side-chain-toend (2). These modes of cyclization involve modifications of side chains and ends which in many cases are essential for bioactivity, and therefore their modification causes loss of activity. Also, these modes of cyclization are not sufficient to screen effectively the conformational space available for a linear peptide with a given sequence. To overcome these limitations, we have introduced two methods called backbone cyclization (2) and cycloscan (3).Backbone cyclization is a general method by which a conformational constraint is imposed on peptides through the connection of the N ␣ and/or C ␣ atoms in the peptide backbone to each other or to side chains or to the carboxyl and amino ends (2). Thus, the cyclization can be performed while retaining the functionality and the activity of the side chains. Backbone cyclization allows nine new modes of cyclization in addition to the four modes in naturally occurring peptides. Preparation of backbone cyclic (BBC) 1 peptides involves the use of a large variety of orthogonally protected N ␣ and C ␣ (-amino-, -carboxy-, and -thio-alkyl) amino acids building units (4 -6). Synthetic procedures have been developed to incorporate these building units into peptides using the solid phase methodology (7,8).The advantages of backbone cyclization over the naturally occurring modes of cyclization are because of the immense variability of spatial orientation of the constitute residues which result from the multiple anchoring points within a chain or between chains. This allows us to screen the conformational space of a given peptide in an extremely efficient manner. Furthermore, most of the modes of backbone cyclization do not involve chemical modifications of side chains which are essential for biological activity. Ba...

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Effect of synthetic pban and derived peptides on sex pheromone biosynthesis in Heliothis peltigera (Lepidoptera: Noctuidae)

Cited by 52 publications

References 17 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

Stimulation of pheromone biosynthesis in the moth Helicoverpa zea: action of a brain hormone on pheromone glands involves Ca2+ and cAMP as second messengers.

Backbone Cyclic Peptide Antagonists, Derived from the Insect Pheromone Biosynthesis Activating Neuropeptide, Inhibit Sex Pheromone Biosynthesis in Moths

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