Amerikanische Gesellschaft für Hirudotherapie

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

Basic science published in Dev Comp Immunol (2009)

Zuletzt aktualisiert: June 18, 2026Geprüft von: ASH Editorial Board
Research article — evidence reviewArticle reference
Evidence: Preclinical (animal)Antimikrobielle ResistenzGenomik & ProteomikJoskova 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

Zusammenfassung

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

Warum dies für die Hirudotherapie relevant ist

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.

Zitation

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

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

DOI

Verwandter klinischer Kontext

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