| Grant number: | 17/09929-3 |
| Support Opportunities: | Scholarships in Brazil - Doctorate (Direct) |
| Start date: | August 01, 2017 |
| End date: | September 30, 2020 |
| 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 |
| Associated research grant: | 13/07467-1 - CeTICS - Center of Toxins, Immune-Response and Cell Signaling, AP.CEPID |
| Associated scholarship(s): | 19/24760-0 - Analysis of the function of sialic acid present in the glycan chains of proteinases from Bothrops venoms, BE.EP.DD |
Abstract The structural variability is a feature of snake venoms, and glycosylation is a major post-translational modification that contributes to diversification of proteomes. Recent studies by our group on the role of glycosylation in events of venom speciation in the Bothrops genus suggest its conservation, in parallel with other molecular markers that determine phylogenetic classification during evolution. In this context, this work aims at comparing the glicoproteomes of nine Bothrops venoms (B. cotiara, B. insularis, B. jararaca B. moojeni, B. neuwiedi, B. jararacussu, B. erythromelas, B. atrox and B. fonsecai). The glicoproteomic approaches will involve affinity chromatography using lectins SNA (Sambucus nigra lectin) and MAL I (Maackia amurensis lectin I), which bind sialic acid at positions alpha-2,6 and alpha-2,3, respectively, and PHA-E (Phaseolus vulgaris eritroaglutinina), which interacts with N-acetylglucosamine. The proteins that show affinity for these lectins will be identified by in-solution digestion with trypsin and mass spectrometric analysis. Based on previous results from our group that showed the recognition of non-glycosylated venom phospholipases A2 (PLAs2) by the lectins concanavalin A, wheat germ agglutinin and peanut agglutininin, the interaction between bothropic PLAs2 (acidic and basic) and these lectins will be 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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