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

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

Resumé

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.

OriginalsprogEngelsk
TidsskriftJournal of Proteome Research
Vol/bind12
Udgave nummer7
Sider (fra-til)3460-3470
Antal sider11
ISSN1535-3893
DOI
StatusUdgivet - 5. jul. 2013

Fingeraftryk

Venoms
Peptides
Scorpion Venoms
Proteolysis
Molecules
Neurotoxins
Bradykinin
Public health
Proteome
Medical problems
Diuretics
Proteins
Public Health
Databases
Enzymes
Pharmaceutical Preparations

Citer dette

Verano-Braga, Thiago ; Dutra, Alexandre A A ; León, Ileana R ; Melo-Braga, Marcella N ; Roepstorff, Peter ; Pimenta, Adriano M C ; Kjeldsen, Frank. / Moving pieces in a venomic puzzle : unveiling post-translationally modified toxins from Tityus serrulatus. I: Journal of Proteome Research. 2013 ; Bind 12, Nr. 7. s. 3460-3470.
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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.",
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Moving pieces in a venomic puzzle : unveiling post-translationally modified toxins from Tityus serrulatus. / Verano-Braga, Thiago; Dutra, Alexandre A A; León, Ileana R; Melo-Braga, Marcella N; Roepstorff, Peter; Pimenta, Adriano M C; Kjeldsen, Frank.

I: Journal of Proteome Research, Bind 12, Nr. 7, 05.07.2013, s. 3460-3470.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

TY - JOUR

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T2 - unveiling post-translationally modified toxins from Tityus serrulatus

AU - Verano-Braga, Thiago

AU - Dutra, Alexandre A A

AU - León, Ileana R

AU - Melo-Braga, Marcella N

AU - Roepstorff, Peter

AU - Pimenta, Adriano M C

AU - Kjeldsen, Frank

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N2 - 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.

AB - 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.

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