Moving Pieces in a Venomic Puzzle: Unveiling Post-translationally Modified Toxins from Tityus serrulatus
peer-reviewed · Journal of Proteome Research · 2013
| Date | 2013-07-05 |
| Type | peer-reviewed |
| Venue | Journal of Proteome Research |
| Publisher | American Chemical Society (ACS) |
| Contribution | downstream-application |
| DOI | 10.1021/pr4003068 |
| Citations (OpenAlex) | 56 |
| Venue 2-year citedness | 3.83 |
Abstract
Besides being a public health problem, scorpion venoms have a potential biotechnological application since they contain peptides that may be used as drug leads and/or to reveal novel pharmacological targets. A comprehensive Tityus serrulatus venom proteome study with emphasis on the phosphoproteome and N-glycoproteome was performed to improve our knowledge on the molecular diversity of the proteinaceous toxins. We combined two peptide identification methodologies, i.e., database search and de novo sequencing, to achieve a more comprehensive overview of the molecular diversity of the venoms. A total of 147 proteins were identified, including neurotoxins, enzymes, bradykinin-potentiating peptides, and molecules with antimicrobial and diuretic activities. Among those, three proteins were found to be phosphorylated, and one N-glycosylated. Finally, cleavage of toxin polypeptide chains seems to be a common post-translational modification in the venom since 80% of the identified molecules were, in fact, products of toxins proteolysis.
Methods and tools
- Tityus serrulatus venom PTM toxins: Characterises Tityus serrulatus scorpion venom, including phospho- and glycoproteome, combining database search with de novo sequencing to reveal modified toxins.
Methods it uses
- PEAKS: Commercial DP-based de novo