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Two related thrombin-like enzymes present in Bothrops atrox venom
J H Petretski1, M Kanashiro, C P Silva
1Laboratório de Biologia do Reconhecer, Universidade Estadual do Norte Fluminense, Campos dos Goytacazes, RJ, Brasil.
Summary
Two novel thrombin-like enzymes from Bothrops atrox venom exhibit fibrinogen-clotting activity. Monoclonal antibodies confirmed distinct epitopes and enzyme presence across several Bothrops species.
Area of Science:
- Biochemistry
- Enzymology
- Venom research
Background:
- Thrombin-like enzymes (TLEs) in snake venom play crucial roles in hemostasis.
- Bothrops atrox venom is a source of bioactive proteins with potential medical applications.
Purpose of the Study:
- To characterize two new TLEs from Bothrops atrox venom.
- To investigate the antigenic properties and cross-reactivity of these enzymes using monoclonal antibodies.
Main Methods:
- Purification and molecular mass determination of TLEs.
- N-terminal amino acid sequencing and homology analysis.
- Monoclonal antibody production and characterization (Western blotting, immunoprecipitation).
Main Results:
- Two TLEs (38 kDa) from B. atrox venom were identified, both cleaving fibrinogen and casein.
- N-terminal sequences showed 80% homology to batroxobin and flavoxobin.
- Monoclonal antibodies revealed distinct epitopes and precipitated TLEs from multiple Bothrops species, inhibiting fibrinogen-clotting activity in most.
Conclusions:
- B. atrox venom contains at least two distinct TLEs with conserved enzymatic and structural features.
- Monoclonal antibodies provide valuable tools for studying TLEs and their distribution in Bothrops venoms.
- The identified TLEs and their epitopes have implications for antivenom development and understanding snakebite pathophysiology.