| Texto completo | |
| Autor(es): |
Torres-Bonilla, Kristian A.
;
Bayona-Serrano, Juan D.
;
Saenz-Suarez, Paula A.
;
Munoz-Gomez, Luis M.
;
Bernal-Bautista, Manuel H.
;
Hyslop, Stephen
Número total de Autores: 6
|
| Tipo de documento: | Artigo Científico |
| Fonte: | Toxicon; v. 263, p. 18-pg., 2025-08-01. |
| Resumo | |
The venom of the double-banded false coralsnake, Erythrolamprus bizona, is proteolytic and attenuates neuromuscular contractile activity in vitro. Here, we examined the Duvernoy's venom gland histology and general composition of E. bizona venom using a combination of chromatographic, electrophoretic, enzymatic and proteomic analyses. Histologically, the venom gland consisted of serous epithelium-lined secretory tubules and a supralabial gland that stained positively for mucopolysaccharide. SDS-PAGE showed that the venom had a simple composition, with proteins in the range of 15-60 kDa. This simple composition was confirmed by RP-HPLC that revealed 15 main protein peaks. The venom (1-10 mu g) was highly proteolytic towards azocasein, but was devoid of esterase, phospholipase (PLA2), and L-amino acid oxidase activities. The venom also degraded casein and gelatin in zymographic assays, with activity towards gelatin being particularly potent and detected over the range of 18.7 ng-30 mu g of venom; gelatinolytic activity was also detected in four of the RP-HPLC peaks. The venom (10 mu g) selectively degraded the alpha-chain of fibrinogen. All proteolytic activity was inhibited by EDTA (metalloproteinase inhibitor) but not by AEBSF (serine proteinase inhibitor). SDS-PAGE followed by in-gel digestion of the main electrophoretic bands coupled with LC-MS/MS analysis revealed the presence of five toxin families: C-type lectin-like proteins (CTL), cysteine-rich secretory proteins (CRiSP), phospholipase B (PLB), snake venom matrix metalloproteinases (svMMP), and snake venom metalloproteinases (SVMP). These findings extend our knowledge of the toxinology of E. bizona and suggest that the local manifestations (pain, edema, erythema, and ecchymosis) seen in human envenomation by this species are probably mediated by venom metalloproteinases. (AU) | |
| Processo FAPESP: | 17/24498-9 - Análises venômicas de serpentes Dipsadidae focando em adaptações a ofiofagia |
| Beneficiário: | Juan David Bayona Serrano |
| Modalidade de apoio: | Bolsas no Brasil - Doutorado Direto |
| Processo FAPESP: | 16/50127-5 - Dimensions US-BIOTA São Paulo: scales of biodiversity: integrated studies of snake venom evolution and function across multiple levels of diversity |
| Beneficiário: | Inácio de Loiola Meirelles Junqueira de Azevedo |
| Modalidade de apoio: | Auxílio à Pesquisa - Programa BIOTA - Temático |