Sociedad Americana de Hirudoterapia

The complete amino acid sequence of a hirudin variant from the leech Hirudinaria manillensis

Comparative study published in J Protein Chem (1993)

Última actualización: June 18, 2026Revisado por: ASH Editorial Board
Research article — evidence reviewArticle reference
Evidence: Observational studyGenómica y proteómicaFarmacología salivalElectricwala A et al. · J Protein Chem, 1993

Abstract

Unlike the European leech Hirudo medicinalis, the Asian jawed leech Hirudinaria manillensis is specialized for feeding on mammalian blood. In the salivary glands of both these leeches, there is a potent inhibitor of thrombin, called hirudin, which acts as an anticoagulant. We have reported previously the isolation and purification of a variant of hirudin, called bufrudin, from the head portions of Hirudinaria. In the present study, the complete amino acid sequence of bufrudin was determined by automated Edman degradation of peptide fragments generated after cleavage of protein with trypsin or thermolysin. Comparison of the primary structure of bufrudin, with hirudin HV1, show about 70% sequence identity with deletion of two amino acids, but the key amino acids at the C-terminus, involved in the inhibition of thrombin, are conserved. However, similar sequence comparison of bufrudin with hirullin P18, a hirudin variant isolated from the same leech species but from whole leech, instead of heads, reveals even less sequence identity of about 60%. From the amino acid sequence, it is suggested that the conformation of the C-terminal portion of bufrudin may be significantly different from hirullin P18, but similar to hirudin HV1, upon its interaction with thrombin. These results indicate that, as with Hirudo leech, various isoforms of hirudin also exist in Hirudinaria leech, with a significant change occurring in the structure of the molecule during the evolution of leeches.

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

Publication typeComparative StudyJournal Article
Indexed MeSH termsAmino Acid SequenceAnimalsHirudinsInvertebrate HormonesLeechesMolecular Sequence DataSequence Homology, Amino Acid

Resumen

Complete amino acid sequence of bufrudin, a hirudin variant from Hirudinaria manillensis, shows 70% sequence identity with hirudin HV1 with conserved C-terminal thrombin-inhibitory residues.

Por qué esto importa para la hirudoterapia

This study determined the complete amino acid sequence of bufrudin, a hirudin variant isolated from the head portions of the Asian leech Hirudinaria manillensis, by Edman degradation of peptide fragments. Bufrudin shows ~70% sequence identity with hirudin HV1 (from Hirudo medicinalis) with two deleted residues, but retains conserved C-terminal key amino acids involved in thrombin inhibition; comparison with hirullin P18 (from whole Hirudinaria) showed only ~60% identity and potentially different C-terminal conformation. These findings suggest multiple hirudin isoforms exist within Hirudinaria, reflecting evolutionary structural diversification. The study is relevant to ASH's domain as a molecular characterization of a thrombin-inhibiting leech secretome component. The honest caveat is that this is a protein-chemistry/taxonomy-level study with no functional, in vivo, animal, or clinical data presented; the abstract does not report inhibitory activity assays or therapeutic claims for bufrudin.

Citación

The complete amino acid sequence of a hirudin variant from the leech Hirudinaria manillensis.

Electricwala A et al. · J Protein Chem, 1993

Contexto clínico relacionado

Añadido a la biblioteca ASH: May 27, 2026 · Última actualización del sitio: June 18, 2026

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