title: Antifeedant activity and high mortality in the pea aphid Acyrthosiphon pisum (Hemiptera: Aphidae) induced by biostable insect kinin analogs.
abstract: The insect kinins are multifunctional neuropeptides found in a variety of arthropod species, including the pea aphid Acyrthosiphon pisum (Hemiptera: Aphidae). A series of biostable insect kinin analogs based on the shared C-terminal pentapeptide core region were fed in solutions of artificial diet to the pea aphid over a period of 3 days and evaluated for antifeedant and aphicidal activity. The analogs contained either alpha,alpha-disubstituted or beta-amino acids in key positions to enhance resistance to tissue-bound peptidases and retain activity in a number of insect kinin bioassays and/or on expressed receptors. Three of the biostable analogs demonstrated antifeedant activity, with a marked reduction in honeydew formation observed after 1 day, and very high mortality. In contrast, an unmodified, parent insect kinin and two other analogs containing some of the same structural components that promote biostability are inactive. The most active analog, double Aib analog K-Aib-1 ([Aib]FF[Aib]WGa), featured aphicidal activity calculated at an LC(50) of 0.063 nmol/microl (0.048 microg/microl) and an LT(50) of 1.68 days, matching the potency of some commercially available aphicides. The mechanism of this activity has yet to be established. The aphicidal activity of the biostable insect kinin analogs may result from different potential mechanisms as disruption of digestive processes by interfering with gut motility patterns, digestive enzyme release, and/or with fluid cycling in the gut, and also nutrient transport across the gut itself; all processes shown to be regulated by the insect kinins in other insects. However the mechanism(s) is(are) not yet known. The active insect kinin analogs represent potential leads in the development of selective, environmentally friendly pest aphid control agents.
authors: Laboratory of Agrozoology, Department of Crop Protection, Faculty of Bioscience Engineering, Ghent University, Coupure Links 653, B-9000 Ghent, Belgium. guy.smagghe@ugent.be
authors: Guy
authors: G
authors: Smagghe
authors: Kamran
authors: K
authors: Mahdian
authors: Pawel
authors: P
authors: Zubrzak
authors: Ronald J
authors: RJ
authors: Nachman
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001042:Aphids / Q000187:drug effects* / Q000502:physiology; D005247:Feeding Behavior / Q000187:drug effects*; D019476:Insect Proteins / Q000737:chemistry / Q000494:pharmacology*; D007705:Kinins / Q000737:chemistry / Q000494:pharmacology*; D008969:Molecular Sequence Data; D009479:Neuropeptides / Q000737:chemistry / Q000494:pharmacology*; D017386:Sequence Homology, Amino Acid
chemical_list: D019476:Insect Proteins; D007705:Kinins; D009479:Neuropeptides