American Society of Hirudotherapy

Destabilase from the medicinal leech is a representative of a novel family of lysozymes

Basic science published in Biochim Biophys Acta (2000)

Last Updated: June 18, 2026Reviewed by: ASH Editorial Board
Research article — evidence reviewArticle reference
Evidence: In vitro / laboratoryGenomics & ProteomicsSalivary PharmacologyZavalova LL et al. · Biochimica et biophysica acta, 2000

Abstract

Intrinsic lysozyme-like activity was demonstrated for destabilase from the medicinal leech supported by (1) high specific lysozyme activity of the highly purified destabilase, (2) specific inhibition of the lysozyme-like activity by anti-destabilase antibodies, and (3) appreciable lysozyme-like activity in insect cells infected with recombinant baculoviruses carrying cDNAs encoding different isoforms of destabilase. Several isoforms of destabilase constitute a protein family at least two members of which are characterized by lysozyme activity. The corresponding gene family implies an ancient evolutionary history of the genes although the function(s) of various lysozymes in the leech remains unclear. Differences in primary structures of the destabilase family members and members of known lysozyme families allow one to assign the former to a new family of lysozymes. New proteins homologous to destabilase were recently described for Caenorhabditis elegans and bivalve mollusks suggesting that the new lysozyme family can be widely distributed among invertebrates. It remains to be investigated whether the two enzymatic activities (isopeptidase and lysozyme-like) are attributes of one and the same protein.

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 SequenceAnimalsAntibodiesBaculoviridaeCarbon-Nitrogen LyasesCell LineDNA, ComplementaryEndopeptidasesEscherichia coliGene ExpressionIsoenzymesLeeches

Summary

Highly purified destabilase shows specific lysozyme activity confirmed by anti-destabilase antibodies and baculovirus-recombinant isoforms; destabilase family assigned to a new lysozyme family widely distributed in invertebrates.

Why This Matters for Hirudotherapy

This study demonstrated that destabilase, a protein from the medicinal leech, possesses intrinsic lysozyme-like activity, confirmed through purified enzyme assays, antibody inhibition, and recombinant expression of destabilase isoforms in insect cells. Multiple destabilase isoforms form a novel family of lysozymes distinct from known families, with homologs identified in Caenorhabditis elegans and bivalve mollusks. The study characterizes a leech-derived protein with enzymatic activity of potential interest to ASH's domain. However, the work is purely biochemical and molecular in nature, does not involve hirudotherapy or clinical application, and the biological function of these lysozymes in the leech remains undetermined per the abstract.

Citation

Destabilase from the medicinal leech is a representative of a novel family of lysozymes.

Zavalova LL et al. · Biochimica et biophysica acta, 2000

DOI

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

This website provides educational information and does not constitute medical advice, diagnosis, or treatment recommendations. Medicinal leech therapy carries clinically meaningful risks and should be performed only by qualified clinicians under institutionally approved protocols. FDA 510(k) clearance for medicinal leeches is limited to specific indications; investigational and off-label discussions are labeled accordingly. For patient-specific guidance, consult a qualified healthcare provider.