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Title: Unraveling neuropeptidergic signaling systems in the tsetse fly, Glossina morsitans morsitans
Other Titles: Ontrafelen van neuropeptiderge signaalsystemen in de tseetseevlieg, Glossina morsitans morsitans
Authors: Caers, Jelle
Issue Date: 25-Nov-2014
Abstract: Normal 0 21 false false false NL-BE X-NONE X-NONE <span style="font-size:12.0pt;line-height:115%;font-family:&quot;Times New Roman&quot;,&quot;serif&quot;" lang="EN-GB">Unravelingneuropeptidergic signaling systems in the tsetse fly, <i style="mso-bidi-font-style:normal">Glossina morsitans morsitansTsetseflies (Glossina spp.) act as the solevector for trypanosome parasites causing human African trypanosomiasis(sleeping sickness) or African animal trypanosomiasis. In 2004 theInternational Glossina GenomeInitiative (IGGI) was launched, which resulted in the sequencing of the whole Glossina morsitans morsitans genome. Abetter understanding of the unique tsetse biology (e.g. obligate blood-feeding,reproduction by adenotrophic viviparity which implies intrauterine feeding andgiving birth to a living larva, proline-dependent energy metabolism) and itsunderlying physiological processes will arise from the wealth of genomicinformation. This knowledge may lead to new vector control initiatives throughthe development of species-specific and environmentally safe insecticides.Neuropeptidergic signaling systems have already been put forward as potentialtargets because of their central role in most physiological processes likereproduction, feeding behavior, energy metabolism, locomotion, osmotic balance,etc. These systems typically consistof small bioactive peptides synthesized and released by neuroendocrine organsthat operate through fine-tuned interactions with their correspondingreceptors. The neuropeptides can act as neurotransmitters, neuromodulators orneurohormones and their receptors mainly belong to the family of Gprotein-coupled receptors (GPCRs).<p class="MsoNormal" style="margin-bottom:6.0pt;text-align:justify;line-height:150%"><span style="font-size:12.0pt;line-height:150%;font-family:&quot;Times New Roman&quot;,&quot;serif&quot;" lang="EN-GB">The first part of this work consisted of theprediction and identification of the neuropeptidergic signaling systems genesin the tsetse genome based on similarities with corresponding genes of otherinsects. In total 42 neuropeptide and 43 neuropeptide receptor genes weremanually annotated of which 33 receptors could be associated with theirputative neuropeptide ligand(s). A peptidomics study was performed to identifyas many peptides as possible in peptide extracts from tissues of the centraland visceral nervous system. In total 35 expected bioactive neuropeptides weredetected in a total set of 223 peptides originating from 22 differentneuropeptide precursors. The other peptides can be classified as truncatedneuropeptides, incompletely processed neuropeptides and spacer peptides.Threeneuropeptidergic signalingsystems were studied in more detail: theadipokinetic hormone (AKH), the neuropeptide F (NPF), and the shortneuropeptide F (sNPF) signaling system. The AKH system is known for itsregulatory role in the energy/fat metabolism of insects during energy requiringprocesses like flight. The NPF and sNPF systems are mainly known for their rolein feeding behavior of insects, but are involved in a variety of otherphysiological processes as well. For each of the three systems transcriptdistribution profiles were determined for the receptor and neuropeptide geneswhich showed strong similarities with other insects, suggesting a role incomparable processes. Furthermore, the receptors were characterized with areverse pharmacology approach, which confirmed that the predicted peptidescould activate their receptors in a concentration-dependent manner. The pharmacologicalcharacteristics of the AKH ligands were determined with a structure-activitystudy. An additional set of ten other insect AKH neuropeptides was alsoadministered to the tsetse AKH receptors which showed that not all AKH neuropeptidesare equally potent to induce receptor activation. Finally, first attempts weremade to determine the functions of the AKH, NPF, and sNPF system with in vivo studies. <w:LatentStyles DefLockedState="false" DefUnhideWhenUsed="true" DefSemiHidden="true" DefQFormat="false" DefPriority="99" LatentStyleCount="267"> <w:LsdException Locked="false" Priority="0" SemiHidden="false" UnhideWhenUsed="false" QFormat="true" Name="Normal"/> <w:LsdException Locked="false" Priority="9" SemiHidden="false" UnhideWhenUsed="false" QFormat="true" Name="heading 1"/> <w:LsdException Locked="false" Priority="10" SemiHidden="false" UnhideWhenUsed="false" QFormat="true" Name="Title"/> <w:LsdException Locked="false" Priority="11" SemiHidden="false" UnhideWhenUsed="false" QFormat="true" Name="Subtitle"/> <w:LsdException Locked="false" Priority="22" SemiHidden="false" UnhideWhenUsed="false" QFormat="true" Name="Strong"/> <w:LsdException Locked="false" Priority="20" SemiHidden="false" UnhideWhenUsed="false" QFormat="true" Name="Emphasis"/> <w:LsdException 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Publication status: published
KU Leuven publication type: TH
Appears in Collections:Animal Physiology and Neurobiology Section - miscellaneous

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