Local and systemic effects of BtaMP-1, a new weakly hemorrhagic Snake Venom Metalloproteinase purified from Bothriopsis taeniata Snake Venom.

Autor: Torres-Huaco FD; Department of Biochemistry, Institute of Biology, University of Campinas (UNICAMP), PO Box 6109, CEP 13083-970 Campinas, SP, Brazil; Universidad Continental, Av. Los Incas, ZIP 4002 Arequipa, Peru. Electronic address: huacofrank@yahoo.com.br., Maruñak S; Laboratory of Pharmacology, Faculty of Veterinary Science, National Northeastern University (UNNE), Argentina., Teibler P; Laboratory of Pharmacology, Faculty of Veterinary Science, National Northeastern University (UNNE), Argentina., Bustillo S; Protein Research Laboratory (LabInPro), Faculty of Natural Sciences and Surveying (FACENA), National Northeastern University (UNNE), Corrientes 3400, Argentina., Acosta de Pérez O; Laboratory of Pharmacology, Faculty of Veterinary Science, National Northeastern University (UNNE), Argentina., Leiva LC; Protein Research Laboratory (LabInPro), Faculty of Natural Sciences and Surveying (FACENA), National Northeastern University (UNNE), Corrientes 3400, Argentina., Ponce-Soto LA; Department of Biochemistry, Institute of Biology, University of Campinas (UNICAMP), PO Box 6109, CEP 13083-970 Campinas, SP, Brazil., Marangoni S; Department of Biochemistry, Institute of Biology, University of Campinas (UNICAMP), PO Box 6109, CEP 13083-970 Campinas, SP, Brazil.
Jazyk: angličtina
Zdroj: International journal of biological macromolecules [Int J Biol Macromol] 2019 Dec 01; Vol. 141, pp. 1044-1054. Date of Electronic Publication: 2019 Sep 05.
DOI: 10.1016/j.ijbiomac.2019.09.032
Abstrakt: A new weak hemorrhagic metalloproteinase named BtaMP-1 was purified from Bothriopsis taeniata snake venom by molecular exclusion followed by anion exchange chromatographies. This protein showed a molecular mass of 25,968.16 Da and is composed of 218 amino acid residues. The multiple alignments of its partial amino acid sequence showed high structural identity with other P-I class SVMP. BtaMP-1 showed caseinolytic activity that was enhanced by Ca 2+ ion, completely inhibited by chelating and reducing agents and can be classified as an α-fibrinogenolytic enzyme. Locally, BtaMP-1 induces hemorrhage and edema, but not myotoxicity. These findings were confirmed by histological analysis of mouse gastrocnemius muscle. "In vitro" studies suggest that BtaMP-1 induce cytotoxicity in myoblast C2C12 but not in the myotubes cell line. BtaMP-1 induced systemic alterations in mice with one MHD and two hours exposure; histological analysis of lungs showed hemorrhagic areas, congestion, and increase the thickness of alveolar septum. Also, this protein induced mild effects on kidney and disruption of coagulation by depletion of fibrinogen plasma levels. This work provides insights into the importance of BtaMP-1 biological effects in envenomation by Bothropsis taeniata snake venom and providing further evidence to understand the role of P-I class SVMP in ophidian envenomation.
(Copyright © 2019 Elsevier B.V. All rights reserved.)
Databáze: MEDLINE