Identificación y cribado de nuevos péptidos antimicrobianos de la sanguijuela medicinal mediante expresión heteróloga en Escherichia coli

The growing threat of infectious diseases requires novel therapeutics with different mechanisms of action. Antimicrobial peptides (AMPs), which are crucial for innate immunity, are a promising research area. The medicinal leech (Hirudo medicinalis) is a potential source of bioactive AMPs that are vital while interacting with microorganisms. This study aims to investigate the antimicrobial properties of peptides found in the H. medicinalis genome using a novel high-throughput screening method based on the expression of recombinant AMP genes in Escherichia coli. This approach enables the direct detection of AMP activity within cells, skipping the synthesis and purification steps, while allowing the simultaneous analysis of multiple peptides. The application of this method to the first identified candidate AMPs from H. medicinalis resulted in the discovery of three novel peptides: LBrHM1, NrlHM1 and NrlHM2. These peptides, which belong to the lumbricin and macin families, exhibit significant activity against E. coli. Two fragments of the new LBrHM1 homologue were synthesised and studied: a unique N-terminal fragment (residues 1-23) and a fragment (residues 27-55) coinciding with the active site of lumbricin I. Both fragments exhibited antimicrobial activity in a liquid medium against Bacillus subtilis. Notably, the N-terminal fragment lacks homologues among previously described AMPs.

Resumen tomado de PubMed (NCBI) para el registro citado, en el idioma original. La versión de referencia es la de la publicación original.

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Los autores desarrollaron un cribado de alto rendimiento que expresa péptidos antimicrobianos (PAM) recombinantes del genoma de Hirudo medicinalis directamente en Escherichia coli y mide su actividad intracelular, sin síntesis ni purificación. Identificaron tres nuevos PAM – LBrHM1, NrlHM1 y NrlHM2 – de las familias de lumbricinas y macinas, con actividad significativa frente a E. coli. Dos fragmentos del homólogo LBrHM1 mostraron actividad antimicrobiana en medio líquido frente a Bacillus subtilis, incluido un fragmento N-terminal (residuos 1–23) sin homólogos conocidos.

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