American Society of Hirudotherapy

Identification and cloning of an invertebrate-type lysozyme from Eisenia andrei

Basic science published in Dev Comp Immunol (2009)

Last Updated: June 18, 2026Reviewed by: ASH Editorial Board
Research article — evidence reviewArticle reference
Evidence: Preclinical (animal)Antimicrobial ResistanceGenomics & ProteomicsJoskova R et al. · Developmental and comparative immunology, 2009

Abstract

Lysozyme is a widely distributed antimicrobial protein having specificity for cleaving the beta-(1,4)-glycosidic bond between N-acetylmuramic acid (NAM) and N-acetylglucosamine (GlcNAc) of peptidoglycan of the bacterial cell walls and thus efficiently contributes to protection against infections caused mainly by Gram-positive bacteria. In the present study, we assembled a full-length cDNA of a novel invertebrate-type lysozyme from Eisenia andrei earthworm (EALys) by RT-PCR and RACE system. The primary structure of EALys shares high homology with other invertebrate lysozymes; however the highest, 72% identity, was shown for the destabilase I isolated from medicinal leech. Recombinant EALys expressed in Escherichia coli exhibited the lysozyme and isopeptidase activity. Moreover, real-time PCR revealed increased levels of lysozyme mRNA in coelomocytes of E. andrei after the challenge with both Gram-positive and Gram-negative bacteria.

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 termsAnimalsBacillus subtilisBacterial AdhesionCarbon-Nitrogen LyasesChitinasesCloning, MolecularEchinodermataEndopeptidasesEscherichia coliEscherichia coli InfectionsGlucosamineGram-Positive Bacterial Infections

Summary

Earthworm EALys lysozyme shares 72% identity with leech destabilase I and exhibits both lysozyme and isopeptidase activity.

Why This Matters for Hirudotherapy

This study identified and cloned a novel invertebrate-type lysozyme (EALys) from the earthworm Eisenia andrei, noting that its primary structure shares the highest identity (72%) with destabilase I from the medicinal leech. Recombinant EALys exhibited both lysozyme and isopeptidase activity, and mRNA levels increased in coelomocytes after bacterial challenge with Gram-positive and Gram-negative species. The relevance to ASH's domain is indirect: this study concerns an earthworm enzyme, not leeches or hirudotherapy, but it provides comparative molecular context for the invertebrate-type lysozyme family that includes leech destabilase. No leech material, secretions, or therapeutic applications are examined; the connection is limited to sequence homology.

Citation

Identification and cloning of an invertebrate-type lysozyme from Eisenia andrei.

Joskova R et al. · Developmental and comparative immunology, 2009

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.