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- W2747388624 abstract "Snake bite envenoming is a neglected health conditionthat inflicts high rates of mortality and morbidity every year. The antivenom treatment, when properly administered, is effective in neutralizing the systemic effectsbut new approaches are needed to address the issue of morbidity. The resistance of the venomous snake Bothrops jararaca against its own venom is partly attributed to a serum glycoprotein, BJ46a,that acts as a natural snake venom metalloproteinase inhibitor. Our main goal was to characterize the glycan moiety of BJ46a and its relevance to its biological activity. The analyses have shown that the glycan portion of BJ46a is composed primarily by sialylated, complex-type N-glycans attached in the positions Asn76, Asn185, Asn263 and Asn274. Substantial glycan removal from BJ46a in native conditions was attained by prolonged incubation (72h) with exoglycosidases and PNGase F. Extensively deglycosylated BJ46a was able to interact with the class PIII metalloproteinase jararhagin and effectively inhibit its proteolytic activity upon azocasein. Also, we analyzed the interaction of BJ46a with different metalloproteinases isolated from snake venoms. The inhibitor was able to interact with the class P-I metalloproteinases BaP1, atroxlysin-Iand leucurolysin-ainhibiting their fibrinogenolyticactivities. The understanding of the structural requirements for the metalloproteinase inhibition by BJ46a could lead to the rational design of synthetic peptides that could be used in antiophidic therapy as well in other pathologies" @default.
- W2747388624 created "2017-08-31" @default.
- W2747388624 creator A5079734570 @default.
- W2747388624 date "2014-01-01" @default.
- W2747388624 modified "2023-09-24" @default.
- W2747388624 title "Caracterização da porção glicídica de BJ46a, um inibidor de metaloproteinases de venenos de serpentes" @default.
- W2747388624 hasPublicationYear "2014" @default.
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