Rational Design of Insect Control Agents: The PK/PBAN Family as a Study Case

Altstein, Miriam; Hariton, Aliza

doi:10.1007/978-90-481-2316-2_3

Cited by 8 publications

(7 citation statements)

References 145 publications

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“…Such partial inhibition could have resulted from low dosage of the peptide, or, alternatively, from the existence of more than one natural elicitor or receptor that mediate(s) sex pheromone biosynthesis, with only one of the various possible elicitor/receptor interactions inhibited by the peptide. The involvement of several receptor sub‐types in pheromone biosynthesis in H. peltigera females has been proposed previously, in light of the ability of various BBC peptides to inhibit sex pheromone biosynthesis elicited by synthetic PBAN but not by synthetic pheromonotropin, leucopyrokinin or myotropin [2,14]. This hypothesis, however, was based on ‘artificial’ stimulation of sex pheromone biosynthesis.…”

Section: Discussionmentioning

confidence: 99%

“…The first member of the family, leucopyrokinin, was discovered in the cockroach Leucophaea maderae in 1986 [1], and over 30 members have been identified since then. They include pyrokinins, myotropins, PBAN, melanization and reddish coloration hormone, diapause hormone, pheromonotropin, and peptides derived from the PBAN gene or cDNA of various moths (termed pheromonotropic β and γ peptides), all of which share the common C‐terminal pentapeptide, FXPRL amide (where X = S, T, G or V) (for detailed review of PK/PBAN peptides and their functions, see [2]). Functions of the PK/PBAN family include stimulation of sex pheromone biosynthesis in moths [3,4], mediation of key functions associated with feeding (gut muscle contractions) [5,6], development (embryonic diapause, pupal diapause and pupariation) [7–11] and defense (melanin biosynthesis) [12,13] in a variety of insects (moths, cockroaches, locusts and flies).…”

Section: Introductionmentioning

confidence: 99%

“…Particular emphasis was placed on whether elicitation of a given function by several different peptides and elicitation of several different functions by a given peptide is inhibited by the same or by different BBC peptides. All of the above experiments were carried out by co‐injection of the BBC with a given elicitor [2].…”

Section: Introductionmentioning

confidence: 99%

“…cDNA of various moths (termed pheromonotropic b and c peptides), all of which share the common C-terminal pentapeptide, FXPRL amide (where X = S, T, G or V) (for detailed review of PK ⁄ PBAN peptides and their functions, see [2]). Functions of the PK ⁄ PBAN family include stimulation of sex pheromone biosynthesis in moths [3,4], mediation of key functions associated with feeding (gut muscle contractions) [5,6], development (embryonic diapause, pupal diapause and pupariation) [7][8][9][10][11] and defense (melanin biosynthesis) [12,13] in a variety of insects (moths, cockroaches, locusts and flies).…”

Section: Introductionmentioning

confidence: 99%

“…Since the PK/PBAN neuropeptides play a major role in many physiological and behavioral processes during development, reproduction, feeding and defense, their antagonists may be good candidates for insecticides/insect control agents, as they may compete with the natural elicitors and disrupt or interfere with their normal function. The high potential of such antagonists has stimulated active interest in the mode of action of this family of neuropeptides in general, and in approaches to obtain PK ⁄ PBAN antagonists in particular (for review, see [2]).…”

Section: Introductionmentioning

confidence: 99%

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Bioavailability of backbone cyclic PK/PBAN neuropeptide antagonists – inhibition of sex pheromone biosynthesis elicited by the natural mechanism in Heliothis peltigera females

et al. 2010

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The bioavailability (i.e. ability to penetrate the insect cuticle, to reach the target organ and to exert bioactivity) of two backbone cyclic (BBC) pyrokinin/pheromone biosynthesis‐activating neuropeptide (PK/PBAN) antagonistic peptides was tested by applying them topically to Heliothis peltigera females and monitoring the resulting inhibition of sex pheromone production elicited by the natural (endogenous) mechanism during scotophase. Peptides were applied at various time points before the onset of scotophase, in aqueous or organic solvents, and pheromone content was examined at the 5th or 6th hour of scotophase. Both peptides penetrated the cuticle very efficiently and inhibited sex pheromone biosynthesis elicited by the natural mechanism for up to 8 or 9 h after application. The degree of inhibition differed between solvents: those applied in double‐distilled water (DDW) were more active than those applied in dimethylsulfoxide (inhibition by 53–73% and 15–38%, respectively, for BBC‐25, and 46–67% and 36–40%, respectively for BBC‐28). Peptides applied in dimethylsulfoxide and hexane exhibited slightly more persistent inhibitory activity than those applied in DDW. The solvents themselves did not affect sex pheromone production. Multiple applications (at −2, 0, +2 and +4 h) resulted in almost complete (87%) inhibition of sex pheromone biosynthesis, compared with 52% inhibition following a single application. The present study is the first demonstration of the ability of topically applied PK/PBAN antagonists to inhibit sex pheromone biosynthesis elicited by the natural mechanism in female moths, and provides important information on the bioavailability of BBC peptides and the mechanism responsible for sex pheromone production in these insects.

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Section: Discussionmentioning

confidence: 99%