Glycopeptide Antibiotics in the Era of Resistance: An Updated Overview

Glycopeptide antibiotics are a family of antimicrobials that function primarily by sharing a similar macromolecular structure. The second commercially available glycopeptide antibiotic is tecoplanin, a ristocetin-type lipoglycopeptide molecule originally discovered in 1978 from the Actinoplanes teichomyceticus. Outside the cell membrane, peptidoglycan, or murein, provides structural support for the bacterial cell wall. Polypeptide and disaccharide units are connected on a sugar backbone by glycosidic bonds in peptidoglycan monomers, which allow for the formation of long chains by transglycosylation. Three novel lipoglycopeptides are now undergoing clinical trials: oritavancin, dalbavancin, and telavancin. Vancomycin is effective against a wide variety of streptococci, including those with viridian, anaerobic, or microaerophilic characteristics, and against penicillin-sensitive or -resistant pneumococci.