American Society of Hirudotherapy

Identification and characterization of a new member of snake venom thrombin inhibitors from Bothrops insularis using a proteomic approach

Research article published in Toxicon (2007)

Last Updated: June 18, 2026Reviewed by: ASH Editorial Board
Research article — evidence reviewArticle reference
Evidence: Preclinical (animal)Drug DevelopmentOliveira-Carvalho AL et al. · Toxicon, 2007

Abstract

Snake venom C-type lectin-like proteins (CLPs) are ubiquitously found in Viperidae snake venoms and differ from the C-type lectins as they display different biological activities but no carbohydrate-binding activity. Previous analysis of the transcriptome obtained from the Bothrops insularis venom gland showed the presence of two clusters homologous to bothrojaracin (BJC) chains alpha and beta. In an effort to identify a new BJC-like molecule, we used an approach associated with proteomic technologies to identify the presence of the expressed protein and then to purify and characterize a new thrombin inhibitor from B. insularis venom. We also constructed homology models of this protein and BJC, which were compared with other C-type lectin-like family members and revealed several conserved features of this intriguing snake venom toxin family.

Abstract sourced from PubMed (NCBI) for the cited record. See the original publication for the authoritative version.

Publication typeJournal ArticleResearch Support, Non-U.S. Gov't
Indexed MeSH termsAmino Acid SequenceAnimalsAnticoagulantsBothropsCrotalid VenomsModels, MolecularMolecular Sequence DataProteomicsThrombin

Summary

Identification and characterization of a new member of snake venom thrombin inhibitors from Bothrops insularis using a proteomic approach.

Why This Matters for Hirudotherapy

This study used a proteomic approach to identify and characterize a new thrombin inhibitor from Bothrops insularis snake venom, identified as a C-type lectin-like protein homologous to bothrojaracin. Researchers successfully purified the expressed protein and constructed molecular homology models to compare its structural features with other intriguing snake venom toxins. Although the research centers on isolating a thrombin inhibitor—a functional class that conceptually parallels the leech secretome's anticoagulant properties like hirudin—the molecule is entirely derived from snake venom. As a result, the study presents no leech-related data and possesses no direct relevance to clinical hirudotherapy.

Citation

Identification and characterization of a new member of snake venom thrombin inhibitors from Bothrops insularis using a proteomic approach

Oliveira-Carvalho AL et al. · Toxicon, 2007

DOI

Added to ASH library: May 27, 2026 · Site last updated: June 18, 2026

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