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Review
. 2017 Apr;77(6):615-628.
doi: 10.1007/s40265-017-0725-1.

Novel Beta-Lactamase Inhibitors: Unlocking Their Potential in Therapy

Affiliations
Review

Novel Beta-Lactamase Inhibitors: Unlocking Their Potential in Therapy

Darren Wong et al. Drugs. 2017 Apr.

Abstract

Carbapenem-resistant Enterobacteriaceae are amongst the most feared pathogens due to severely limited treatment options. In response to this threat, three novel β-lactamase inhibitors have been developed in an attempt to reinvigorate and sustain our current antimicrobial therapies. Avibactam, vaborbactam, and relebactam are inhibitor agents with high affinity to Ambler class A and C β-lactamases and favorable outcomes in current clinical trials. However, although they do possess key similarities, these agents have unique differences which may have important clinical implications. The microbiologic spectrum, pharmacokinetics, and key clinical trials for each of these novel agents are reviewed. A proposed role in therapy and potential novel combinations are examined.

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Conflict of interest statement

Conflict of Interest:

No potential conflicts: D.W.

Potential conflicts of interest: D.v.D.:

Actavis, Allergan, Achaogen, Shionogi, Tetraphase, Sanofi-Pasteur, MedImmune, Astellas, Advisory Board. Steris Inc., Research funding. Scynexis Research funding.

Figures

Figure 1
Figure 1
Chemical structures of avibactam, vaborbactam and relebactam

References

    1. Öztürk H, Ozkirimli E, Özgür A. Classification of Beta-lactamases and penicillin binding proteins using ligand-centric network models. PLoS One. 2015;10(2):e0117874. - PMC - PubMed
    1. Bush K, Jacoby GA. Updated functional classification of beta-lactamases. Antimicrob Agents Chemother. 2010 Mar;54(3):969–76. - PMC - PubMed
    1. Bonomo RA. beta-Lactamases: A Focus on Current Challenges. Cold Spring Harb Perspect Med. 2017 Jan;03:7. (1) - PMC - PubMed
    1. Drawz SM, Papp-Wallace KM, Bonomo RA. New β-lactamase inhibitors: a therapeutic renaissance in an MDR world. Antimicrob Agents Chemother. 2014;58(4):1835–46. - PMC - PubMed
    1. van Duin D, Doi Y. The global epidemiology of carbapenemase-producing Enterobacteriaceae. Virulence. 2016 Aug;11:1–10. - PMC - PubMed

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