Moving pieces in a venomic puzzle: unveiling post-translationally modified toxins from Tityus serrulatus

Thiago Verano-Braga, Alexandre A A Dutra, Ileana R León, Marcella N Melo-Braga, Peter Roepstorff, Adriano M C Pimenta, Frank Kjeldsen

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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.

Original languageEnglish
JournalJournal of Proteome Research
Issue number7
Pages (from-to)3460-3470
Number of pages11
Publication statusPublished - 5. Jul 2013


  • PTMs
  • Tityus serrulatus
  • animal venom
  • bottom-up
  • post-translational modifications
  • scorpion venom
  • top-down
  • venom proteome
  • venomics


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    Thiago Verano-Braga


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