Oritavancin exhibits dual mode of action to inhibit cell-wall biosynthesis in Staphylococcus aureus.

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Citation

Kim SJ, Cegelski L, Stueber D, Singh M, Dietrich E, Tanaka KS, Parr TR Jr, Far AR, Schaefer J

Oritavancin exhibits dual mode of action to inhibit cell-wall biosynthesis in Staphylococcus aureus.

J Mol Biol. 2008 Mar 14;377(1):281-93. doi: 10.1016/j.jmb.2008.01.031. Epub 2008 Jan 17.

PubMed ID
18258256 [ View in PubMed
]
Abstract

Solid-state NMR measurements performed on intact whole cells of Staphylococcus aureus labeled selectively in vivo have established that des-N-methylleucyl oritavancin (which has antimicrobial activity) binds to the cell-wall peptidoglycan, even though removal of the terminal N-methylleucyl residue destroys the D-Ala-D-Ala binding pocket. By contrast, the des-N-methylleucyl form of vancomycin (which has no antimicrobial activity) does not bind to the cell wall. Solid-state NMR has also determined that oritavancin and vancomycin are comparable inhibitors of transglycosylation, but that oritavancin is a more potent inhibitor of transpeptidation. This combination of effects on cell-wall binding and biosynthesis is interpreted in terms of a recent proposal that oritavancin-like glycopeptides have two cell-wall binding sites: the well-known peptidoglycan D-Ala-D-Ala pentapeptide stem terminus and the pentaglycyl bridging segment. The resulting dual mode of action provides a structural framework for coordinated cell-wall assembly that accounts for the enhanced potency of oritavancin and oritavancin-like analogues against vancomycin-resistant organisms.

DrugBank Data that Cites this Article

Drugs
Drug Targets
DrugTargetKindOrganismPharmacological ActionActions
OritavancinBacterial cell wall peptide bridging segmentsGroupStaphylococcus aureus
Yes
Inhibitor
Details
OritavancinPentaglycyl bridging segmentGroupStaphylococcus aureus
Yes
Disruptor
Details
OritavancinPeptidoglycan precursorsGroup
Yes
Binder
Details