Acquired Class D β-Lactamases

doi:10.3390/antibiotics3030398

Review

. 2014 Aug 21;3(3):398-434.

doi: 10.3390/antibiotics3030398.

Acquired Class D β-Lactamases

Nuno T Antunes¹, Jed F Fisher²

Affiliations

¹ Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN 46556, USA. ngiaoant@nd.edu.
² Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN 46556, USA. Jed.F.Fisher.57@nd.edu.

PMID: 27025753
PMCID: PMC4790369
DOI: 10.3390/antibiotics3030398

Review

Acquired Class D β-Lactamases

Nuno T Antunes et al. Antibiotics (Basel). 2014.

. 2014 Aug 21;3(3):398-434.

doi: 10.3390/antibiotics3030398.

Authors

Nuno T Antunes¹, Jed F Fisher²

Affiliations

¹ Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN 46556, USA. ngiaoant@nd.edu.
² Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN 46556, USA. Jed.F.Fisher.57@nd.edu.

PMID: 27025753
PMCID: PMC4790369
DOI: 10.3390/antibiotics3030398

Abstract

The Class D β-lactamases have emerged as a prominent resistance mechanism against β-lactam antibiotics that previously had efficacy against infections caused by pathogenic bacteria, especially by Acinetobacter baumannii and the Enterobacteriaceae. The phenotypic and structural characteristics of these enzymes correlate to activities that are classified either as a narrow spectrum, an extended spectrum, or a carbapenemase spectrum. We focus on Class D β-lactamases that are carried on plasmids and, thus, present particular clinical concern. Following a historical perspective, the susceptibility and kinetics patterns of the important plasmid-encoded Class D β-lactamases and the mechanisms for mobilization of the chromosomal Class D β-lactamases are discussed.

Keywords: OXA; carbapenemase; class D; crystal structure; kinetics; plasmid; β-lactamase.

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Figures

**Figure 1**
Amino acid alignment of seven Class D β-lactamases. Shaded in gray are motifs that are well conserved among this class of enzymes.

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References

1. Testero S.A., Fisher J.F., Mobashery S. β-Lactam antibiotics. In: Abraham D.J., Rotella D.P., editors. Burger’s Medicinal Chemistry and Drug Discovery. John Wiley & Sons, Inc.; Indianapolis, IN, USA: 2010. pp. 259–404.
1. Vollmer W., Joris B., Charlier P., Foster S. Bacterial peptidoglycan (murein) hydrolases. FEMS Microb. Rev. 2008;32:259–286. - PubMed
1. Yao Z., Kahne D., Kishony R. Distinct single-cell morphological dynamics under β-lactam antibiotics. Mol. Cell. 2012;48:705–712. doi: 10.1016/j.molcel.2012.09.016. - DOI - PMC - PubMed
1. Pratt R.F., McLeish M.J. Structural relationship between the active sites of β-lactam-recognizing and amidase signature enzymes: Convergent evolution? Biochemistry. 2010;49:9688–9697. doi: 10.1021/bi1012222. - DOI - PubMed
1. Fisher J.F., Meroueh S.O., Mobashery S. Bacterial resistance to β-lactam antibiotics: Compelling opportunism, compelling opportunity. Chem. Rev. 2005;105:395–424. doi: 10.1021/cr030102i. - DOI - PubMed

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[1] Testero S.A., Fisher J.F., Mobashery S. β-Lactam antibiotics. In: Abraham D.J., Rotella D.P., editors. Burger’s Medicinal Chemistry and Drug Discovery. John Wiley & Sons, Inc.; Indianapolis, IN, USA: 2010. pp. 259–404.

[2] Testero S.A., Fisher J.F., Mobashery S. β-Lactam antibiotics. In: Abraham D.J., Rotella D.P., editors. Burger’s Medicinal Chemistry and Drug Discovery. John Wiley & Sons, Inc.; Indianapolis, IN, USA: 2010. pp. 259–404.

[3] Vollmer W., Joris B., Charlier P., Foster S. Bacterial peptidoglycan (murein) hydrolases. FEMS Microb. Rev. 2008;32:259–286. - PubMed

[4] Vollmer W., Joris B., Charlier P., Foster S. Bacterial peptidoglycan (murein) hydrolases. FEMS Microb. Rev. 2008;32:259–286. - PubMed

[5] Yao Z., Kahne D., Kishony R. Distinct single-cell morphological dynamics under β-lactam antibiotics. Mol. Cell. 2012;48:705–712. doi: 10.1016/j.molcel.2012.09.016. - DOI - PMC - PubMed

[6] Yao Z., Kahne D., Kishony R. Distinct single-cell morphological dynamics under β-lactam antibiotics. Mol. Cell. 2012;48:705–712. doi: 10.1016/j.molcel.2012.09.016. - DOI - PMC - PubMed

[7] Pratt R.F., McLeish M.J. Structural relationship between the active sites of β-lactam-recognizing and amidase signature enzymes: Convergent evolution? Biochemistry. 2010;49:9688–9697. doi: 10.1021/bi1012222. - DOI - PubMed

[8] Pratt R.F., McLeish M.J. Structural relationship between the active sites of β-lactam-recognizing and amidase signature enzymes: Convergent evolution? Biochemistry. 2010;49:9688–9697. doi: 10.1021/bi1012222. - DOI - PubMed

[9] Fisher J.F., Meroueh S.O., Mobashery S. Bacterial resistance to β-lactam antibiotics: Compelling opportunism, compelling opportunity. Chem. Rev. 2005;105:395–424. doi: 10.1021/cr030102i. - DOI - PubMed

[10] Fisher J.F., Meroueh S.O., Mobashery S. Bacterial resistance to β-lactam antibiotics: Compelling opportunism, compelling opportunity. Chem. Rev. 2005;105:395–424. doi: 10.1021/cr030102i. - DOI - PubMed

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Acquired Class D β-Lactamases

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Acquired Class D β-Lactamases

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