Navegando por Palavras-chave "Peptidome"

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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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    Proteomic and glycoproteomic profilings reveal that posttranslational modifications of toxins contribute to venom phenotype in snakes
    (Amer Chemical Soc, 2016) Andrade-Silva, Debora; Zelanis, Andre [UNIFESP]; Kitano, Eduardo Shigueo; Junqueira-de-Azevedo, Inácio de Loiola Meirelles; Reis, Marcelo da Silva; Lopes, Aline Soriano [UNIFESP]; Serrano, Solange Maria de Toledo
    Snake venoms are biological weapon systems composed of secreted proteins and peptides that are used for immobilizing or killing prey. Although post-translational modifications are widely investigated because of their importance in many biological phenomena, we currently still have little understanding of how protein glycosylation impacts the variation and stability of venom proteomes. To address these issues, here we characterized the venom proteomes of seven Bothrops snakes using a shotgun proteomics strategy. Moreover, we compared the electrophoretic profiles of native and deglycosylated venoms and, in order to assess their subproteomes of glycoproteins, we identified the proteins with affinity for three lectins with different saccharide specificities and their putative glycosylation sites. As proteinases are abundant glycosylated toxins, we examined the effect of N-deglycosylation on their catalytic activities and show that the proteinases of the seven venoms were similarly affected by removal of N-glycans. Moreover, we prospected putative glycosylation sites of transcripts of a B. jararaca venom gland data set and detected toxin family related patterns of glycosylation. Based on our global analysis, we report that Bothrops venom proteomes and glycoproteomes contain a core of components that markedly define their composition, which is conserved upon evolution in parallel to other molecular markers that determine their phylogenetic classification.
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    Proteomic identification of gender molecular markers in Bothrops jararaca venom
    (Elsevier Science Bv, 2016) Zelanis, Andre [UNIFESP]; Menezes, Milene C.; Kitano, Eduardo S.; Liberato, Tarcisio [UNIFESP]; Tashima, Alexandre Keiji [UNIFESP]; Pinto, Antonio F. M.; Sherman, Nicholas E.; Ho, Paulo L.; Fox, Jay W.; Serrano, Solange Maria de Toledo [UNIFESP]
    Variation in the snake venom proteome is a well-documented phenomenon
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    Unraveling snake venom complexity with 'omics' approaches: Challenges and perspectives
    (Elsevier B.V., 2014-09-01) Zelanis, Andre [UNIFESP]; Tashima, Alexandre Keiji [UNIFESP]; Universidade Federal de São Paulo (UNIFESP)
    The study of snake venom proteomes (venomics) has been experiencing a burst of reports, however the comprehensive knowledge of the dynamic range of proteins present within a single venom, the set of post-translational modifications (PTMs) as well as the lack of a comprehensive database related to venom proteins are among the main challenges in venomics research. the phenotypic plasticity in snake venom proteomes together with their inherent toxin proteoform diversity, points out to the use of integrative analysis in order to better understand their actual complexity. in this regard, such a systems venomics task should encompass the integration of data from transcriptomic and proteomic studies (specially the venom gland proteome), the identification of biological PTMs, and the estimation of artifactual proteomes and peptidomes generated by sample handling procedures. (C) 2014 Elsevier B.V. All rights reserved.