Neuropeptide precursor gene discovery in the Chagas disease vector <i>Rhodnius prolixus</i>

Ons, Sheila; Sterkel, Marcos; Diambra, Luis; Urlaub, Henning; Rivera‐Pomar, Rolando

doi:10.1111/j.1365-2583.2010.01050.x

Cited by 105 publications

(154 citation statements)

References 41 publications

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“…Neuropeptide-like precursor 1 (NPLP1) is conserved in various insects and contains multiple mono-and dibasic cleavage sites for the processing of several peptides, either bioactive neuropeptides or spacer peptides [29,30,95,96]. Currently, a functional role for only one NPLP-1 derived peptide has been elucidated.…”

Section: Neuropeptide-like Precursormentioning

confidence: 99%

Peptidomics of Neuropeptidergic Tissues of the Tsetse FlyGlossina morsitans morsitans

Caers

Boonen

Abbeele³

et al. 2015

J. Am. Soc. Mass Spectrom.

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Abstract. Neuropeptides and peptide hormones are essential signaling molecules that regulate nearly all physiological processes. The recent release of the tsetse fly genome allowed the construction of a detailed in silico neuropeptide database (International Glossina Genome Consortium, Science 344, 380-386 (2014)), as well as an in-depth mass spectrometric analysis of the most important neuropeptidergic tissues of this medically and economically important insect species. Mass spectrometric confirmation of predicted peptides is a vital step in the functional characterization of neuropeptides, as in vivo peptides can be modified, cleaved, or even mispredicted. Using a nanoscale reversed phase liquid chromatography coupled to a Q Exactive Orbitrap mass spectrometer, we detected 51 putative bioactive neuropeptides encoded by 19 precursors: adipokinetic hormone (AKH) I and II, allatostatin A and B, capability/ pyrokinin (capa/PK), corazonin, calcitonin-like diuretic hormone (CT/DH), FMRFamide, hugin, leucokinin, myosuppressin, natalisin, neuropeptide-like precursor (NPLP) 1, orcokinin, pigment dispersing factor (PDF), RYamide, SIFamide, short neuropeptide F (sNPF) and tachykinin. In addition, propeptides, truncated and spacer peptides derived from seven additional precursors were found, and include the precursors of allatostatin C, crustacean cardioactive peptide, corticotropin releasing factor-like diuretic hormone (CRF/DH), ecdysis triggering hormone (ETH), ion transport peptide (ITP), neuropeptide F, and proctolin, respectively. The majority of the identified neuropeptides are present in the central nervous system, with only a limited number of peptides in the corpora cardiaca-corpora allata and midgut. Owing to the large number of identified peptides, this study can be used as a reference for comparative studies in other insects.

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Section: Neuropeptide-like Precursormentioning

confidence: 99%

Peptidomics of Neuropeptidergic Tissues of the Tsetse FlyGlossina morsitans morsitans

Caers

Boonen

Abbeele³

et al. 2015

J. Am. Soc. Mass Spectrom.

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“…Insect myosuppressins have the general conserved sequence: X 1 DVX 4 HX 6 FLRFamide where X 1 can be pQ, P, T or A; X 4 can be D, G or V; and X 6 can be V, S or I (Orchard et al, 2001;Orchard and Lange, 2013;Nygaard et al, 2011). The myosuppressin sequence in R. prolixus (Rhopr-MS) isolated by Ons and colleagues (Ons et al 2009;Ons et al, 2011) has two unique features; the sequence pQDIDHVFMRFamide contains isoleucine (I) in the third position as opposed to the usual valine (V) found in other insects, and also a unique FMRFamide C-terminus and not the usual FLRFamide.…”

Section: Introductionmentioning

confidence: 99%

An unusual myosuppressin from the blood-feeding bugRhodnius prolixus

Lee

Taufique

Silva

et al. 2012

Journal of Experimental Biology

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SUMMARYThe myosuppressin (MS) gene was cloned from a central nervous system (CNS) cDNA library of the hematophagous insect Rhodnius prolixus and is predicted to contain two introns and three exons. The mRNA transcribed from the myosuppressin gene encodes an 88 amino acid prepropeptide, which results in a mature decapeptide after post-translational modification. When compared with the myosuppressins isolated from other insects, the R. prolixus myosuppressin has a unique amino acid sequence (pQDIDHVFMRFamide), with isoleucine (I) in position 3 and methionine (M) in position 8. Reverse transcriptase (RT)-PCR shows that Rhopr-MS is expressed in the CNS and posterior midgut in R. prolixus and immunohistochemistry suggests that an RFamide-like peptide is present in endocrine-like cells in the midgut. Physiological assays using Rhopr-MS indicate that, despite the unusual M at position 8, it still retains myoinhibitory activity, inhibiting the frequency and reducing the amplitude of contractions in the anterior midgut and hindgut, and decreasing heart rate.

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“…Nothing is known about function, with the exception that in D. melanogaster, disruption of the ASTCC gene is embryonic lethal (Veenstra 2009b). PISCF/AST was not found in the R. prolixus genome or via peptide purification even though a PISCF/AST receptor was identified (Ons et al 2009(Ons et al , 2011. A R. prolixus ASTCC has been identified (Veenstra 2009b), although it is unclear whether it is a ligand for the PISCF/ AST receptor.…”

Section: Piscf/astsmentioning

confidence: 99%

“…An alternate variation has been detected in the R. prolixus MIP/AST precursor whereby Rhopr-MIP/AST8 terminates in Gly rather than Trp. The six amino acid spacing between the Trp residues is still maintained (Ons et al 2011). The Hymenoptera A. mellifera and N. vitropennis appear to lack MIPs, as peptide sequences could not be detected by isolation or through genome mining (Hummon et al 2006;Boerjan et al 2010;Hauser et al 2010).…”

Section: The Fglamide-related-ast Familymentioning

confidence: 99%

“…These approaches have recently uncovered the FGLa/ASTs from the Hymenoptera, including the honey bee (Apis mellifera L., 1758) (Hummon et al 2006;Boerjan et al 2010), the parasitoid wasp Nasonia vitripennis (Walker, 1836) (Hauser et al 2010), and the Panamanian leafcutter ant (Acromyrmex echinatior (Forel, 1899)) (GenBank accession No. EGI57352); Hemiptera, including the pea aphid (Acrythosiphon pisum Harris, 1776) (Huybrechts et al 2010) and R. prolixus (Ons et al 2009(Ons et al , 2011; and Siphunculata, the human body louse (Pediculus humanus corporis) (cited in Weaver and Audsley 2009). Furthermore, FGL-amide ASTs have been uncovered in the genome of arachnids including the black-legged deer tick (Ixodes scapularis Say, 1821) (Christie 2008;Neupert et al 2009a) and the American dog tick (Dermacentor variabilis (Say, 1821)) (Bissinger et al 2011).…”

Section: The Fglamide-related-ast Familymentioning

confidence: 99%

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Families of allatoregulator sequences: a 2011 perspective¹This 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.

BendenaWilliam

TobeStephen

2012

Can. J. Zool.

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Three different peptide families have been named "allatostatins" (ASTs), based on their initial purifications which were based on their ability to inhibit juvenile hormone (JH) biosynthesis. These include (i) a family of peptides that have a consensus C-terminal sequence Y/FXFGL-NH 2 ; (ii) a family of peptides with a conserved C-terminal sequence W(X) 6 W-NH 2 ; and(iii) a family of peptides with C-terminal sequence PISCF, some of which are C-terminally-amidated. Each allatostatin family has functions distinct and apart from the inhibition of JH biosynthesis. A peptide family known as the "allatotropins" serve to stimulate JH biosynthesis. This family of peptides also has been proven to exert multiple effects dependent on the species in question. Genome and peptidome projects are uncovering new members of these families and it is clear that these structures are not just confined to Insecta but are found in a range of invertebrates. The receptors for these neuropeptides have been identified and tested experimentally for specific ligand binding. The Y/FXFGLa-ASTs exert their action through galanin-like receptors, W(X) 6 Wa-ASTs through a sex peptide-binding receptor, and PISCF-ASTs through somatostatin-like receptors. These receptors are conserved through evolutionary time and are being identified in numerous invertebrates by way of genome projects.Key words: allatostatin, allatotropin, juvenile hormone, muscle contraction, neuropeptides, neuropeptide receptors, insects, crustaceans, arthropods.Résumé : Trois familles différentes de peptides portent le nom d'« allatostatines » (AST) d'après leurs purifications initiales basées sur leur capacité d'inhiber la biosynthèse de l'hormone juvénile (JH). Elles incluent (i) une famille de peptides qui possèdent une séquence consensus C-terminale Y/FXFGL-NH 2 , (ii) une famille de peptides avec une séquence C-terminale conservée W(X) 6 W-NH 2 et (iii) une famille de peptides avec une séquence C-terminale PISCF, dont certains sont amidatées sur l'extrémité C-terminale. Chaque famille d'allatostatines possède des fonctions distinctes et additionnelles à l'inhibition de la synthèse de l'hormone juvénile. Une famille de peptides connus sous le nom d'« allatotropines » sert à stimuler la synthèse de la JH. Cette famille de peptides produit aussi des effets multiples selon l'espèce concernée. Des projets sur le génome et le peptidome découvrent de nouveaux membres de ces familles et il est clair que ces structures ne se retrouvent pas seulement chez les insectes, mais aussi chez une gamme d'invertébrés. Les récepteurs de ces neuropeptides ont été identifiés et ont été testé expérimentalement pour des liaisons spécifiques au ligand. Les AST-Y/FXFGLa exercent leur action par des récepteurs de type galanine, les AST-W(X)6Wa par un récepteur liant un peptide sexuel et les AST-PISCF par des récepteurs de type somatostatine. Ces récepteurs sont conservés au cours de l'évolution et sont présentement retrouvés chez de nombreux invertébrés dans le cadre des projets de génome.

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Neuropeptide precursor gene discovery in the Chagas disease vector Rhodnius prolixus

Cited by 105 publications

References 41 publications

Peptidomics of Neuropeptidergic Tissues of the Tsetse FlyGlossina morsitans morsitans

Peptidomics of Neuropeptidergic Tissues of the Tsetse FlyGlossina morsitans morsitans

An unusual myosuppressin from the blood-feeding bugRhodnius prolixus

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