ArticleBioMed research international2014
Purification and biochemical characterization of three myotoxins from Bothrops mattogrossensis snake venom with toxicity against Leishmania and tumor cells.
Article in BioMed research international, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Venomics across theJournal of proteome research · 2026Article
- Antischistosomal Potential of Animal-Derived Natural Products and Compounds.Microorganisms · 2025Review
- Biomedical and Biotechnological Potential of Animal Venoms:Current medicinal chemistry · 2025Review
- Review
- The Potassium Channel Blocker β-Bungarotoxin from the KraitBiomedicines · 2023Article
- Purification, Characterization and Evaluation of the Antitumoral Activity of a Phospholipase A2 from the SnakePharmaceuticals (Basel, Switzerland) · 2022Article
- Black-necked spitting cobra (Naja nigricollis) phospholipases AScientific reports · 2022Article
- Antiprotozoal Effect of Snake Venoms and Their Fractions: A Systematic Review.Pathogens (Basel, Switzerland) · 2021Review
- Inflammatory Effects ofToxins · 2021Review
- In-depth transcriptome reveals the potential biotechnological application ofThe journal of venomous animals and toxins including tropical diseases · 2020Article
- Viperidae snakebites in Ecuador: A review of epidemiological and ecological aspects.Toxicon: X · 2020Article
- Article
- Cytotoxic and pro-apoptotic action of MjTX-I, a phospholipase A2 isolated fromThe journal of venomous animals and toxins including tropical diseases · 2018Article
- Article
- L-Aminoacid Oxidase from Bothrops leucurus Venom Induces Nephrotoxicity via Apoptosis and Necrosis.PloS one · 2015Article
- Antitumor potential of the myotoxin BthTX-I from Bothrops jararacussu snake venom: evaluation of cell cycle alterations and death mechanisms induced in tumor cell lines.The journal of venomous animals and toxins including tropical diseases · 2015Article
- Article
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Authors and funding
16 authors.
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Abstract
Bothrops mattogrossensis snake is widely distributed throughout eastern South America and is responsible for snakebites in this region. This paper reports the purification and biochemical characterization of three new phospholipases A2 (PLA2s), one of which is presumably an enzymatically active Asp49 and two are very likely enzymatically inactive Lys49 PLA2 homologues. The purification was obtained after two chromatographic steps on ion exchange and reverse phase column. The 2D SDS-PAGE analysis revealed that the proteins have pI values around 10, are each made of a single chain, and have molecular masses near 13 kDa, which was confirmed by MALDI-TOF mass spectrometry. The N-terminal similarity analysis of the sequences showed that the proteins are highly homologous with other Lys49 and Asp49 PLA2s from Bothrops species. The PLA2s isolated were named BmatTX-I (Lys49 PLA2-like), BmatTX-II (Lys49 PLA2-like), and BmatTX-III (Asp49 PLA2). The PLA2s induced cytokine release from mouse neutrophils and showed cytotoxicity towards JURKAT (leukemia T) and SK-BR-3 (breast adenocarcinoma) cell lines and promastigote forms of Leishmania amazonensis. The structural and functional elucidation of snake venoms components may contribute to a better understanding of the mechanism of action of these proteins during envenomation and their potential pharmacological and therapeutic applications.
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