info:eu-repo/semantics/article
Purification of a fragment obtained by autolysis of a PIIIb-SVMP from Bothrops alternatus venom
Fecha
2018-07Registro en:
Van de Velde, Andrea Carolina; Gay, Claudia Carolina; Olivera Moritz, Milene Nobrega de; dos Santos, Patty Karina; Bustillo, Soledad; et al.; Purification of a fragment obtained by autolysis of a PIIIb-SVMP from Bothrops alternatus venom; Elsevier Science; International Journal of Biological Macromolecules; 113; 7-2018; 205-211
0141-8130
CONICET Digital
CONICET
Autor
Van de Velde, Andrea Carolina
Gay, Claudia Carolina
Olivera Moritz, Milene Nobrega de
dos Santos, Patty Karina
Bustillo, Soledad
Rodríguez, Juan Pablo
Acosta, Ofelia Cristina
Biscoglio, Mirtha Josefa
Sobreiro Selistre de Araujo, Heloisa
Leiva, Laura Cristina Ana
Resumen
Snake Venom Metalloproteinases (SVMPs) represent 43.1% of the components in Bothrops alternatus venom and play an important role in envenomation. Disintegrins and disintegrin-like domains are released by proteolytic processing of PII and PIII classes of SVMPs respectively and are potent inhibitors of integrin–ligand interaction. Baltergin is a PIIIb-SVMP isolated from this venom and able to undergo autolysis in vitro, giving rise to a stable disintegrin-like/cystein-rich fragment (baltergin-DC). Conditions of baltergin autolysis were adjusted in order to carry out the purification of baltergin-DC and its effect on cell adhesion was studied. Autolysis was maximal at 37 °C and a pH range of 7.0–8.0. Baltergin-DC amino-terminal sequence begins with IISPPVCGNELLEVGEECDCGTPENCQNECCDAATC, which shows a high degree of homology with other disintegrin-like proteins. Baltergin and purified baltergin-DC were both able to inhibit C2C12 adhesion to fetal bovine serum (FBS) coated plates, indicating that a non-catalytic process is involved, probably mediated by binding to membrane integrins. Baltergin-DC, lacking proteolytic action, becomes an attractive molecule for future studies on blocking integrin–ligand interactions.