title: Peptidomics of Neuropeptidergic Tissues of the Tsetse Fly Glossina morsitans morsitans.
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. Graphical Abstract ᅟ.
authors.affiliation: Functional Genomics and Proteomics, Department of Biology, KU Leuven, 3000, Leuven, Belgium.
authors.forename: Jelle
authors.initials: J
authors.lastname: Caers
authors.affiliation: Functional Genomics and Proteomics, Department of Biology, KU Leuven, 3000, Leuven, Belgium.
authors.forename: Kurt
authors.initials: K
authors.lastname: Boonen
authors.affiliation: Unit of Veterinary Protozoology, Department of Biomedical Sciences, Institute of Tropical Medicine, 2000, Antwerp, Belgium.|Laboratory of Zoophysiology, Department of Physiology, University of Ghent, 9000, Ghent, Belgium.
authors.forename: Jan
authors.initials: J
authors.lastname: Van Den Abbeele
authors.affiliation: Functional Genomics and Proteomics, Department of Biology, KU Leuven, 3000, Leuven, Belgium.
authors.forename: Liesbeth
authors.initials: L
authors.lastname: Van Rompay
authors.affiliation: Functional Genomics and Proteomics, Department of Biology, KU Leuven, 3000, Leuven, Belgium. liliane.schoofs@bio.kuleuven.be.
authors.forename: Liliane
authors.initials: L
authors.lastname: Schoofs
authors.affiliation: Functional Genomics and Proteomics, Department of Biology, KU Leuven, 3000, Leuven, Belgium.
authors.forename: Matthias B
authors.initials: MB
authors.lastname: Van Hiel
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D056148:Chromatography, Reverse-Phase / Q000379:methods; D005260:Female; D008969:Molecular Sequence Data; D009479:Neuropeptides / Q000032:analysis*; D040901:Proteomics / Q000379:methods*; D053719:Tandem Mass Spectrometry / Q000379:methods*; D014370:Tsetse Flies / Q000033:anatomy & histology / Q000737:chemistry*
chemical_list: D009479:Neuropeptides
keywords: Glossina; Insect; Mass spectrometry; Neuropeptide; Peptidomics; Tsetse fly