Mass spectrometric analysis of the individual variability of Bothrops jararaca venom peptide fraction. Evidence for sex‐based variation among the bradykinin‐potentiating peptides

Rapid Communications in Mass Spectrometry - Tập 21 Số 6 - Trang 1034-1042 - 2007
Daniel C. Pimenta1, Benedito C. Prezoto2, Katsuhiro Konno1, Robson L. Melo1, Maria F. Furtado3, Antônio Carlos Martins de Camargo1, Solange M.T. Serrano1
1Laboratório Especial de Toxinologia Aplicada/CAT-CEPID, Instituto Butantan, Av. Vital Brasil, 1500, São Paulo–SP 05503-900, Brazil
2Laboratório de Farmacologia, Instituto Butantan, Av. Vital Brasil, 1500, São Paulo–SP 05503-900, Brazil
3Laboratório de Herpetologia, Instituto Butantan, Av. Vital Brasil, 1500, São Paulo SP 05503-900, Brazil

Tóm tắt

AbstractVariation in the snake venom proteome is well documented and it is a ubiquitous phenomenon at all taxonomical levels. However, variation in the snake venom peptidome is so far not described. In this work we used mass spectrometry [liquid chromatography/mass spectrometry (LC/MS) and matrix‐assisted laser desorption/ionization time‐of‐flight (MALDI‐TOFMS)] to explore sex‐based differences among the venom peptides of eighteen sibling specimens of Bothrops jararaca of a single litter born and raised in the laboratory. MALDI‐TOFMS analyses showed individual variability among the bradykinin‐potentiating peptides (BPPs), and, interestingly, four new peptides were detected only in female venoms and identified by de novo sequencing as cleaved BPPs lacking the C‐terminal Q‐I‐P‐P sequence. Similar results were obtained with venom from wild‐caught adult non‐sibling specimens of B. jararaca and in this case we were able to identify the gender of the specimen by analyzing the MALDI‐TOF profile of the peptide fraction and finding the cleaved peptides only in female venoms. Synthetic replicates of the cleaved BPPs were less potent than the full‐length BPP‐10c in potentiating the bradykinin hypotensive effect, suggesting that the C‐terminus is critical for the interaction of the BPPs with their mammalian molecular targets. This work represents a comprehensive mass spectrometric analysis of the peptide fraction of B. jararaca venom and shows for the first time sex‐based differences in the snake venom peptidome of sibling and non‐sibling snakes and suggests that the BPPs may follow distinct processing pathways in female and male individuals. Copyright © 2007 John Wiley & Sons, Ltd.

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Rapid Communications in Mass Spectrometry

Tập 21 Số 6

1034-1042

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