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Analysis of the complexity of venom glycoproteomes of Bothrops genus

Grant number: 15/23017-1
Support Opportunities:Scholarships in Brazil - Master
Effective date (Start): March 01, 2016
Effective date (End): July 31, 2017
Field of knowledge:Biological Sciences - Biochemistry - Molecular Biology
Principal Investigator:Solange Maria de Toledo Serrano
Grantee:Carolina Brás Costa
Host Institution: Instituto Butantan. Secretaria da Saúde (São Paulo - Estado). São Paulo , SP, Brazil


Snake venoms are complex mixtures composed mainly of proteins and peptides, which are used to immobilize or capture prey. Structural variability is a well-known feature of snake venoms, and glycosylation is a major post-translational modification (PTM) that contributes to the diversification of proteomes. However, little is known about the post-translational modifications of Bothrops toxins and the level of variability among species. Considering that venoms of Bothrops species share most of their toxin classes, the characterization of PTMs may advance the knowledge on the differences between the accidents with Bothrops snakes. Glycosylation is the most common PTM occurring in proteins, which is important for their stability and function, and this fact, coupled with the presence of large portions of carbohydrates in toxins that play important roles in Bothrops envenomation, highlights the importance of studies to characterize the glycoproteomes Bothrops venoms. This study aims at comparing the glycoproteomes of nine Bothrops venoms (B. cotiara, B. insularis, B. jararaca B. moojeni, B. neuwiedi, B. jararacussu, B. erythromelas, B. atrox and B. fonsecai). The glycoproteomic approaches will involve affinity chromatography using two lectins SNA (Sambucus nigra lectin) and PHA-E (Phaseolus vulgaris erythroagglutinin). The specific affinities of the selected lectins are, respectively, by units of sialic acid and N-acetylglucosamine. The proteins that show affinity for these lectins will be identified by digestion with trypsin and analyzed by mass spectrometry. Considering that metalloproteinases and serine proteinases are important components involved in Bothrops envenomation, and that these classes of enzymes contain several glycosylation sites, the role of sialic acid units in their proteolytic activities will also be evaluated. This study will put in perspective a hitherto little explored form of snake venom proteome variability and allow further evaluation of the importance of glycosylation to these important biological fluids. (AU)

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Scientific publications
(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)
BRAS-COSTA, CAROLINA; CHAVES, ALISON FELIPE ALENCAR; CAJADO-CARVALHO, DANIELA; DA SILVA PIRES, DAVID; ANDRADE-SILVA, DEBORA; SERRANO, SOLANGE M. T.. Profilings of subproteomes of lectin-binding proteins of nine Bothrops venoms reveal variability driven by different glycan types. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, v. 1870, n. 7, p. 15-pg., . (15/23017-1, 17/09929-3, 13/13548-4)
BRAS-COSTA, CAROLINA; CHAVES, ALISON FELIPE ALENCAR; TREVISAN-SILVA, DILZA; MENEZES, MILENE C.; ROCHA, MARISA M. T.; CAJADO-CARVALHO, DANIELA; ANDRADE-SILVA, DEBORA; SERRANO, SOLANGE M. T.. Sialic acid-containing glycans play a role in the activity of snake venom proteases. Biochimie, v. 204, p. 14-pg., . (13/13548-4, 13/07467-1, 15/23017-1, 17/09929-3)

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