ArticleThe Journal of biological chemistry2013
Batroxobin binds fibrin with higher affinity and promotes clot expansion to a greater extent than thrombin.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed.
- Efficacy of Defibrinogenation Therapy for Sudden Sensorineural Hearing Loss: A Systematic Review and Meta-Analysis.Laryngoscope investigative otolaryngology · 2026Review
- Animal Venoms Targeting Cellular Mechanisms: Advances and Implications for Drug Discovery and Disease Therapy.Toxins · 2026Review
- Effects of Cape Cobra (Toxins · 2026Article
- Fibrinogen exacerbates α-synuclein aggregation and mitochondrial dysfunction via alpha5beta3 integrin in Parkinson's disease.Journal of advanced research · 2026Article
- Article
- Review
- Acute myocardial infarction after batroxobin treatment of sudden sensorineural hearing loss: Case report.Medicine · 2025Article
- Article
- Biomedical and Biotechnological Potential of Animal Venoms:Current medicinal chemistry · 2025Review
- Newly diagnosed multiple myeloma with bleeding and coagulation abnormalities caused by a thrombin-inhibiting substance.International journal of hematology · 2024Article
- Exploring the Diversity and Function of Serine Proteases in Toxicofera Reptile Venoms: A Comprehensive Overview.Toxins · 2024Review
- Review
- Venom-derived peptides for breaking through the glass ceiling of drug development.Frontiers in chemistry · 2024Review
- A Review of Rattlesnake Venoms.Toxins · 2023Review
- Bothrops venom-induced hemostasis disorders in the rat: Between Scylla and Charybdis.PLoS neglected tropical diseases · 2023Article
- Article
- Fibrinogen BOE II: dysfibrinogenemia with bleeding and defective thrombin binding.Research and practice in thrombosis and haemostasis · 2023Article
- Risk factors and clinical outcomes associated with acquired hypofibrinogenemia in patients administered hemocoagulase batroxobin for hemoptysis.Journal of thoracic disease · 2023Article
- The plasma fibrinogen levels in the nitroglycerin-induced chronic migraine rat model and its association between migraine-associated vestibular dysfunction.Frontiers in neurology · 2023Article
- Mathematical modeling to understand the role of bivalent thrombin-fibrin binding during polymerization.PLoS computational biology · 2022Article
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6 authors.
Funding
Abstract
Batroxobin is a thrombin-like serine protease from the venom of Bothrops atrox moojeni that clots fibrinogen. In contrast to thrombin, which releases fibrinopeptide A and B from the NH2-terminal domains of the Aα- and Bβ-chains of fibrinogen, respectively, batroxobin only releases fibrinopeptide A. Because the mechanism responsible for these differences is unknown, we compared the interactions of batroxobin and thrombin with the predominant γA/γA isoform of fibrin(ogen) and the γA/γ' variant with an extended γ-chain. Thrombin binds to the γ'-chain and forms a higher affinity interaction with γA/γ'-fibrin(ogen) than γA/γA-fibrin(ogen). In contrast, batroxobin binds both fibrin(ogen) isoforms with similar high affinity (Kd values of about 0.5 μM) even though it does not interact with the γ'-chain. The batroxobin-binding sites on fibrin(ogen) only partially overlap with those of thrombin because thrombin attenuates, but does not abrogate, the interaction of γA/γA-fibrinogen with batroxobin. Furthermore, although both thrombin and batroxobin bind to the central E-region of fibrinogen with a Kd value of 2-5 μM, the α(17-51) and Bβ(1-42) regions bind thrombin but not batroxobin. Once bound to fibrin, the capacity of batroxobin to promote fibrin accretion is 18-fold greater than that of thrombin, a finding that may explain the microvascular thrombosis that complicates envenomation by B. atrox moojeni. Therefore, batroxobin binds fibrin(ogen) in a manner distinct from thrombin, which may contribute to its higher affinity interaction, selective fibrinopeptide A release, and prothrombotic properties.
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