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The discovery of a new lantibiotic, epilancin A37, by researchers at the University Hospital Bonn, the University of Bonn, and the German Center for Infection Research is significant in the face of increasing antibiotic resistance in pathogens. Lantibiotics are antimicrobial peptides produced by gram-positive bacteria with a narrow spectrum of activity, making them promising candidates for targeted antibiotic therapy. Epilancin A37, produced by skin-colonizing staphylococci, specifically targets corynebacteria, highlighting the intense competition between bacterial species within the human microbiota.

The research team, led by Dr. Fabian Grein and Dr. Tanja Schneider, along with Professor Ulrich Kubitscheck, has shed light on the mechanism of action of epilancin A37. This lantibiotic penetrates corynebacterial cells, accumulating inside without initially destroying the cell. It then dissolves the cell membrane from the inside, leading to the demise of the corynebacterium. This unique mode of action demonstrates the ability of epilancin A37 to specifically combat a single bacterial species, offering a potential strategy for targeted antibiotic therapy.

The ecological importance of epilancins is underscored by their widespread presence in staphylococci, indicating a key role in the competitive dynamics of the skin microbiome. Staphylococci and corynebacteria are vital components of the human microbiota, influencing health and disease. The fact that staphylococci produce epilancin A37 as a defense mechanism against corynebacteria highlights the intense competition between these species for survival and colonization within the microbiota.

Dr. Grein emphasizes the importance of specific antimicrobial compounds like epilancin A37 in combating bacterial infections without disrupting the entire bacterial flora. Broad-spectrum antibiotics can have detrimental effects on beneficial bacteria, making targeted antibacterial agents like lantibiotics a valuable resource in the fight against antibiotic resistance. The discovery of epilancin A37 adds to the growing body of knowledge on antimicrobial peptides and their potential applications in medical therapeutics.

The detailed deciphering of the mechanism of action of epilancin A37 provides insights into the complex “bacterial war” within the skin microbiome. By understanding how these antimicrobial peptides target specific bacterial species, researchers can develop more precise and effective antibacterial agents. The research serves as a proof of concept for the use of specific mechanisms of action to combat individual bacterial species, offering a glimpse into the future of targeted antibiotic therapy.

Overall, the discovery of epilancin A37 and its unique mechanism of action represents a significant advancement in the field of antimicrobial research. By uncovering the ecological and competitive dynamics of the skin microbiome, researchers are paving the way for the development of more targeted and effective antibacterial therapies. The specific targeting of corynebacteria by epilancin A37 highlights the potential of lantibiotics as a valuable resource in the fight against antibiotic resistance and infectious diseases.

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