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Bothrops snake venoms: impact of glycosylation on the complexity of proteomes and toxins function

Grant number: 17/09929-3
Support type:Scholarships in Brazil - Doctorate (Direct)
Effective date (Start): August 01, 2017
Effective date (End): July 31, 2020
Field of knowledge:Biological Sciences - Biochemistry
Principal Investigator:Solange Maria de Toledo Serrano
Grantee:Carolina Brás Costa
Home 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

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)