Approved glycopeptide antibacterial drugs: Mechanism of action and resistance

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Abstract

The glycopeptide antimicrobials are a group of natural product and semisynthetic glycosylated peptides that show antibacterial activity against Gram-positive organisms through inhibition of cell-wall synthesis. This is achieved primarily through binding to the Dalanyl- D-alanine terminus of the lipid II bacterial cell-wall precursor, preventing crosslinking of the peptidoglycan layer. Vancomycin is the foundational member of the class, showing both clinical longevity and a still preferential role in the therapy of methicillinresistant Staphylococcus aureus and of susceptible Enterococcus spp. Newer lipoglycopeptide derivatives (telavancin, dalbavancin, and oritavancin) were designed in a targeted fashion to increase antibacterial activity, in some cases through secondary mechanisms of action. Resistance to the glycopeptides emerged in delayed fashion and occurs via a spectrum of chromosome- and plasmid-associated elements that lead to structural alteration of the bacterial cell-wall precursor substrates.

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Zeng, D., Debabov, D., Hartsell, T. L., Cano, R. J., Adams, S., Schuyler, J. A., … Pace, J. L. (2016). Approved glycopeptide antibacterial drugs: Mechanism of action and resistance. Cold Spring Harbor Perspectives in Medicine, 6(12). https://doi.org/10.1101/cshperspect.a026989

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