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) | 57 |
| 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
Cites (4)
- PEAKS DB: De Novo Sequencing Assisted Database Search for Sensitive and Accurate Peptide Identification (2012) crossref
- The Diversity of Bioactive Proteins in Australian Snake Venoms (2007) crossref
- Molecular Diversity in Venom from the Australian Brown Snake, Pseudonaja textilis (2006) crossref
- PEAKS: powerful software for peptide de novo sequencing by tandem mass spectrometry (2003) crossref
Cited by (4)
- Unveiling the Diversity and Modifications of Short Peptides in Scorpion Venom through Liquid Chromatography-High Resolution Mass Spectrometry (2024) both
- FT‐MS in the de novo top‐down sequencing of natural nontryptic peptides (2022) crossref
- Peptide de novo sequencing of mixture tandem mass spectra (2016) both
- Revealing the functional structure of a new PLA2 K49 from Bothriopsis taeniata snake venom employing automatic “de novo” sequencing using CID/HCD/ETD MS/MS analyses (2015) crossref