Citation

Verano-Braga T, Dutra AA, León IR, Melo-Braga MN, Roepstorff P, Pimenta AM, Kjeldsen F. J. Proteome Res. 2013; 12(7): 3460-3470.

Copyright

(Copyright © 2013, American Chemical Society)

DOI

10.1021/pr4003068

PMID

23731212

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.

Language: en