Neuropeptidomics of the mosquito Aedes aegypti

J Proteome Res. 2010 Apr 5;9(4):2006-15. doi: 10.1021/pr901187p.

Abstract

Neuropeptidomic data were collected on the mosquito Ae. aegypti, which is considered the most tractable mosquito species for physiological and endocrine studies. The data were solely obtained by direct mass spectrometric profiling, including tandem fragmentation, of selected tissues from single specimens, which yielded a largely complete accounting of the putative bioactive neuropeptides; truncated neuropeptides with low abundance were not counted as mature peptides. Differential processing within the CNS was detected for the CAPA-precursor, and differential post-translational processing (pyroglutamate formation) was detected for AST-C and CAPA-PVK-2. For the first time in insects, we succeeded in the direct mass spectrometric profiling of midgut tissue which yielded a comprehensive and immediate overview of the peptides involved in the endocrine system of the gut. Head peptides which were earlier identified as the most abundant RFamides of Ae. aegypti, were not detected in any part of the CNS or midgut. This study provides a framework for future investigations on mosquito endocrinology and neurobiology. Given the high sequence similarity of neuropeptide precursors identified in other medically important mosquitoes, conclusions regarding the peptidome of Ae. aegypti likely are applicable to these mosquitoes.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Aedes / chemistry*
  • Aedes / metabolism
  • Amino Acid Sequence
  • Animals
  • Brain / metabolism
  • Female
  • Insect Proteins / chemistry*
  • Insect Proteins / metabolism
  • Male
  • Malpighian Tubules / metabolism
  • Molecular Sequence Data
  • Neuropeptides / chemistry*
  • Neuropeptides / metabolism
  • Proteomics / methods*
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Tissue Distribution

Substances

  • Insect Proteins
  • Neuropeptides