The mosquito <i>Aedes aegypti</i> (L.) leucokinin receptor is a multiligand receptor for the three <i>Aedes</i> kinins

Pietrantonio, Patricia V.; Jagge, Christopher; Taneja-Bageshwar, Suparna; Nachman, Ronald J.; Barhoumi, Roula

doi:10.1111/j.1365-2583.2004.00531.x

Cited by 62 publications

(63 citation statements)

References 46 publications

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“…S7). The Aedae-KR predicted amino acid sequences obtained were similar to the receptor cloned from the Malpighian tubule (AAT95982) (9), and the region selected for antibody production (residues 328-345; NEKFKREFHKRYPFRGRN) (Fig. S7) also was identical.…”

Section: Resultsmentioning

confidence: 69%

“…In A. aegypti, three endogenous kinins (aedeskinin I-III) act as diuretic hormones on Malpighian tubule stellate cells (5,6) by stimulating chloride transport and fluid secretion (6)(7)(8). We verified that the aedeskinins activate the single Aedes kinin receptor (Aedae-KR), a G protein-coupled receptor (GPCR) that signals through intracellular calcium (9). We designed kinin analogs to be resistant to degrading peptidases and therefore exhibit sustained high potency (10,11).…”

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confidence: 92%

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Leucokinin mimetic elicits aversive behavior in mosquito Aedes aegypti (L.) and inhibits the sugar taste neuron

Kwon

Agha

Smith

et al. 2016

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

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Insect kinins (leucokinins) are multifunctional peptides acting as neurohormones and neurotransmitters. In females of the mosquito vector Aedes aegypti (L.), aedeskinins are known to stimulate fluid secretion from the renal organs (Malpighian tubules) and hindgut contractions by activating a G protein-coupled kinin receptor designated "Aedae-KR." We used protease-resistant kinin analogs 1728, 1729, and 1460 to evaluate their effects on sucrose perception and feeding behavior. In no-choice feeding bioassays (capillary feeder and plate assays), the analog 1728, which contains α-amino isobutyric acid, inhibited females from feeding on sucrose. It further induced quick fly-away or walk-away behavior following contact with the tarsi and the mouthparts. Electrophysiological recordings from single long labellar sensilla of the proboscis demonstrated that mixing the analog 1728 at 1 mM with sucrose almost completely inhibited the detection of sucrose. Aedae-KR was immunolocalized in contact chemosensory neurons in prothoracic tarsi and in sensory neurons and accessory cells of long labellar sensilla in the distal labellum. Silencing Aedae-KR by RNAi significantly reduced gene expression and eliminated the feeding-aversion behavior resulting from contact with the analog 1728, thus directly implicating the Aedae-KR in the aversion response. To our knowledge, this is the first report that kinin analogs modulate sucrose perception in any insect. The aversion to feeding elicited by analog 1728 suggests that synthetic molecules targeting the mosquito Aedae-KR in the labellum and tarsi should be investigated for the potential to discover novel feeding deterrents of mosquito vectors.neuropeptide GPCR | sucrose taste | sensory neuron | chemical target validation | feeding deterrent

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Section: Resultsmentioning

confidence: 69%

mentioning

confidence: 92%

Leucokinin mimetic elicits aversive behavior in mosquito Aedes aegypti (L.) and inhibits the sugar taste neuron

Kwon

Agha

Smith

et al. 2016

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

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“…The first insect kinin receptor was identified from D. melanogaster and was shown to be a GPCR that is related to tachykinin receptors . The subsequently characterized A. gambiae kinin receptor proved to be a multiligand receptor, responding to all three mosquito kinins (Pietrantonio et al 2005). In these dipteran species, the receptor is expressed in the CNS, as well as in Malpighian tubules and in the hindgut (Radford et al , 2004.…”

Section: Insect Kininsmentioning

confidence: 99%

Peptidergic control of food intake and digestion in insects¹This review is part of a virtual symposium on recent advances in understanding a variety of complex regulatory processes in insect physiology and endocrinology, including development, metabolism, cold hardiness, food intake and digestion, and diuresis, through the use of omics technologies in the postgenomic era.

et al. 2012

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Like all heterotrophic organisms, insects require a strict control of food intake and efficient digestion of food into nutrients to maintain homeostasis and to fulfill physiological tasks. Feeding and digestion are steered by both external and internal signals that are transduced by a multitude of regulatory factors, delivered either by neurons innervating the gut or mouthparts, or by midgut endocrine cells. The present review gives an overview of peptide regulators known to control feeding and digestion in insects. We describe the discovery and functional role in these processes for insect allatoregulatory peptides, diuretic hormones, FMRFamide-related peptides, (short) neuropeptide F, proctolin, saliva production stimulating peptides, kinins, and tachykinins. These peptides control either gut myoactivity, food intake, and (or) release of digestive enzymes. Some peptides exert their action at multiple levels, possibly having a biological function that depends on their site of delivery. Many regulatory peptides have been physically extracted from different insect species. However, multiple peptidomics, proteomics, transcriptomics, and genome sequencing projects have led to increased discovery and prediction of peptide (precursor) and receptor sequences. In combination with physiological experiments, these large-scale projects have already led to important steps forward in unraveling the physiology of feeding and digestion in insects.Key words: insect, midgut, digestion, neuropeptides, stomatogastric nervous system. Résumé : Comme tous les organismes hétérotrophes, les insectes requièrent un contrôle strict de leur ingestion de nourriture et la digestion de leur nourriture en nutriments afin de maintenir leur homéostasie et de compléter leurs tâches physiologiques. L'alimentation et la digestion sont gouvernées par des signaux tant externes qu'internes qui sont transmis par un multitude de facteurs régulateurs, livrés ou bien par les neurones qui innervent le tube digestif ou les pièces buccales ou alors par les cellules endocrines du tube digestif moyen. Notre revue fournit une synthèse des régulateurs peptidiques connus pour contrôler l'alimentation et la digestion chez les insectes. Nous décrivons la découverte et le rôle fonctionnel de ces processus dans le cas des peptides allatorégulateurs, des hormones diurétiques, des peptides apparentés aux amides FMRF, du neuropeptide F (court), de la proctoline, des peptides stimulateurs de la production de salive, des kinines et des tachykinines des insectes. Ces peptides contrôlent la myoactivité du tube digestif, l'ingestion de nourriture et(ou) la libération des enzymes digestives. Certains peptides agissent à de multiples niveaux, possédant une fonction biologique qui dépend de leur site d'action. Plusieurs peptides régulateurs ont été extraits physiquement de différentes espèces d'insectes. Cependant, plusieurs projets de peptidomique, de protéomique, de transcriptomique et de génomique ont mené à de nombreuses découvertes supplémentaires et des prédict...

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“…Myokinin receptors from the southern cattle tick, Boophilus microplus (Holmes et al, 2000(Holmes et al, , 2003, and the dengue vector, the mosquito Aedes aegypti (Pietrantonio et al, 2005), were previously stably and functionally expressed in CHO-K1 cells.…”

Section: Introductionmentioning

confidence: 99%

Comparative structure‐activity analysis of insect kinin core analogs on recombinant kinin receptors from Southern cattle tick Boophilus microplus (Acari: Ixodidae) and mosquito Aedes aegypti (Diptera: Culicidae)

Taneja-Bageshwar¹,

Strey²,

Zubrzak³

et al. 2006

Arch Insect Biochem Physiol

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The systematic analysis of structure-activity relationships of insect kinins on two heterologous receptor-expressing systems is described. Previously, kinin receptors from the southern cattle tick, Boophilus microplus (Canestrini), and the dengue vector, the mosquito Aedes aegypti (L.), were functionally and stably expressed in CHO-K1 cells. In order to determine which kinin residues are critical for the peptide-receptor interaction, kinin core analogs were synthesized as an Ala-replacement series of the peptide FFSWGa and tested by a calcium bioluminescence plate assay. The amino acids Phe(1) and Trp(4) were essential for activity of the insect kinins in both receptors. It was confirmed that the pentapeptide kinin core is the minimum sequence required for activity and that the C-terminal amide is also essential. In contrast to the tick receptor, a large increase in efficacy is observed in the mosquito receptor when the C-terminal pentapeptide is N-terminally extended to a hexapeptide. The aminoisobutyric acid (Aib)-containing analog, FF[Aib]WGa, was as active as superagonist FFFSWGa on the mosquito receptor in contrast to the tick receptor where it was statistically more active than FFFSWGa by an order of magnitude. This restricted conformation Aib analog provides information on the conformation associated with the interaction of the insect kinins with these two receptors. Furthermore, the analog FF[Aib]WGa has been previously shown to resist degradation by the peptidases ACE and nephrilysin and represents an important lead in the development of biostable insect kinin analogs that ticks and mosquitoes cannot readily deactivate.

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The mosquito Aedes aegypti (L.) leucokinin receptor is a multiligand receptor for the three Aedes kinins

Cited by 62 publications

References 46 publications

Leucokinin mimetic elicits aversive behavior in mosquito Aedes aegypti (L.) and inhibits the sugar taste neuron

Leucokinin mimetic elicits aversive behavior in mosquito Aedes aegypti (L.) and inhibits the sugar taste neuron

Comparative structure‐activity analysis of insect kinin core analogs on recombinant kinin receptors from Southern cattle tick Boophilus microplus (Acari: Ixodidae) and mosquito Aedes aegypti (Diptera: Culicidae)

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