Navegando por Palavras-chave "Ontogenetic venom variation"

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    Analysis of the Ontogenetic Variation in the Venom Proteome/Peptidome of Bothrops jararaca Reveals Different Strategies to Deal with Prey
    (Amer Chemical Soc, 2010-05-01) Zelanis, Andre; Tashima, Alexandre Keiji [UNIFESP]; Rocha, Marisa Maria Teixeira; Furtado, Maria F.; Camargo, Antonio Carlos Martins de; Ho, Paulo Lee; Serrano, Solange Maria de Toledo; Inst Butantan; Universidade de São Paulo (USP); Universidade Federal de São Paulo (UNIFESP)
    Previous studies have demonstrated that the pharmacological activities displayed by Bothrops jararaca venom undergo a significant ontogenetic shift. Variation in the venom proteome is a well-documented phenomenon; however, variation in the venom peptidome is poorly understood. We report a comparative proteomic and peptidomic analysis of venoms from newborn and adult specimens of B. jararaca and correlate it with the evaluation of important venom features. We demonstrate that newborn and adult venoms have similar hemorrhagic activities, while the adult venom has a slightly higher lethal activity in mice; however, the newborn venom is extremely more potent to kill chicks. the coagulant activity of newborn venom upon human plasma is 10 times higher than that of adult venom. These differences were clearly reflected in their different profiles of SDS-PAGE, gelatin zimography, immunostaining using specific antibodies, glycosylation pattern, and concanavalin A-binding proteins. Furthermore, we report for the first time the analysis of the peptide fraction of newborn and adult venoms by MALDI-TOF mass spectrometry and LC-MS/MS, which revealed different contents of peptides, while the bradykinin potentiating peptides (BPPs) showed rather similar profiles and were detected in the venoms showing their canonical sequences and also novel sequences corresponding to BPPs processed from their precursor protein at sites so far not described. As a result of these studies, we demonstrated that the ontogenetic shift in diet, from ectothermic prey in early life to endothermic prey in adulthood, and in animal size are associated with changes in the venom proteome in B. jararaca species.
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    Bothrops jararaca venom proteome rearrangement upon neonate to adult transition
    (Wiley-Blackwell, 2011-11-01) Zelanis, Andre; Tashima, Alexandre Keiji [UNIFESP]; Pinto, Antônio Frederico Michel; Paes Leme, Adriana Franco; Stuginski, Daniel Rodrigues; Furtado, Maria de Fatima Domingues; Sherman, Nicholas E.; Ho, Paulo Lee; Fox, Jay W.; Serrano, Solange Maria de Toledo; Inst Butantan; Universidade de São Paulo (USP); Universidade Federal de São Paulo (UNIFESP); Ctr Biotecnol UFRGS; LNBio; Univ Virginia
    The pharmacological activities displayed by Bothrops jararaca venom undergo a significant ontogenetic shift. Similarly, the diet of this species changes from ectothermic prey in early life to endothermic prey in adulthood. in this study we used large and representative newborn and adult venom samples consisting of pools from 694 and 110 specimens, respectively, and demonstrate a significant ontogenetic shift in the venom proteome complexity of B. jararaca. 2-DE coupled to MS protein identification showed a clear rearrangement of the toxin arsenal both in terms of the total proteome, as of the glycoproteome. N-glycosylation seems to play a key role in venom protein variability between newborn and adult specimens. Upon the snake development, the subproteome of metalloproteinases undergoes a shift from a P-III-rich to a P-I-rich profile while the serine proteinase profile does not vary significantly. We also used isobaric tag labeling (iTRAQ) of venom tryptic peptides for the first time to examine the quantitative changes in the venom toxins of B. jararaca upon neonate to adult transition. the iTRAQ analysis showed changes in various toxin classes, especially the proteinases. Our study expands the in-depth understanding of venom complexity variation particularly with regard to toxin families that have been associated with envenomation pathogenesis.