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Chapter 13 : β-Lactamase Inhibitors

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β-Lactamase Inhibitors, Page 1 of 2

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Abstract:

The most widespread mechanism of bacterial resistance to β-lactams is the biosynthesis of chromosomal or plasmid-mediated β-lactamases. Generally, the term β-lactamase inhibitor is reserved for β-lactams whose spectrum of inhibition covers all the β-lactamases to various degrees. While proposed in a fixed combination with ampicillin, only sulbactam was also available for extemporaneous combination with the most appropriate β-lactam for the β-lactamase-producing bacterial species concerned. It can be seen that for three TEM-3-producing species, the combinations of sulbactam plus cefotaxime, ceftazidime, and aztreonam are more effective than the fixed combinations clavulanic acid-ticarcillin and tazobactam-piperacillin. With 70% bioavailability following oral administration, clavulanic acid has proved to be well absorbed by the intestinal mucosa; as the same applies to amoxicillin, the combination of the two products is suggested for oral administration. The inhibitor and the β-lactam present in the bacterium compete for binding to the active site of the β-lactamase. As the inhibitors generally have a better affinity for the enzyme, the β-lactam may escape the hydrolytic activity of the β-lactamase if the concentration of inhibitor combined with it is sufficient to inactivate all of the β-lactamase molecules. It can thus be seen that the ideal combination is that of the best inhibitor with the β-lactam most resistant to the hydrolytic activity of the β-lactamases. The results obtained therapeutically suggest that clavulanic acid and tazobactam might also be proposed. This would allow the prescription of the most suitable combination of inhibitor and β-lactam for the bacterial species responsible for the infection.

Citation: Kazmierczak A. 2005. β-Lactamase Inhibitors, p 401-409. In Bryskier, M.D. A (ed), Antimicrobial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555815929.ch13

Key Concept Ranking

beta-Lactamase Inhibitors
1.8348837
Clavulanic acid
1.2355043
beta-Lactams
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Citation: Kazmierczak A. 2005. β-Lactamase Inhibitors, p 401-409. In Bryskier, M.D. A (ed), Antimicrobial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555815929.ch13
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Citation: Kazmierczak A. 2005. β-Lactamase Inhibitors, p 401-409. In Bryskier, M.D. A (ed), Antimicrobial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555815929.ch13
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Citation: Kazmierczak A. 2005. β-Lactamase Inhibitors, p 401-409. In Bryskier, M.D. A (ed), Antimicrobial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555815929.ch13
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Citation: Kazmierczak A. 2005. β-Lactamase Inhibitors, p 401-409. In Bryskier, M.D. A (ed), Antimicrobial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555815929.ch13
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Citation: Kazmierczak A. 2005. β-Lactamase Inhibitors, p 401-409. In Bryskier, M.D. A (ed), Antimicrobial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555815929.ch13
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Citation: Kazmierczak A. 2005. β-Lactamase Inhibitors, p 401-409. In Bryskier, M.D. A (ed), Antimicrobial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555815929.ch13
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Citation: Kazmierczak A. 2005. β-Lactamase Inhibitors, p 401-409. In Bryskier, M.D. A (ed), Antimicrobial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555815929.ch13
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Citation: Kazmierczak A. 2005. β-Lactamase Inhibitors, p 401-409. In Bryskier, M.D. A (ed), Antimicrobial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555815929.ch13
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Citation: Kazmierczak A. 2005. β-Lactamase Inhibitors, p 401-409. In Bryskier, M.D. A (ed), Antimicrobial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555815929.ch13
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References

/content/book/10.1128/9781555815929.ch13
1. Arisawa M,, Then RL, 1982, 6-Acetylmethylenepenicillanic acid (Ro 15-1903), a potent β-lactamase inhibitor. I. Inhibition of chromosomally and R-factor-mediated β-lactamases, J Antibiot, 35, 15781583.
2. Gutmann L,, Kitzis MD,, Yamabe S,, Acar JF, 1986, Comparative evaluation of a new β-lactamase inhibitor, YTR 830, combined with different β-lactam antibiotics against bacteria harboring known β-lactamases, Antimicrob Agents Chemother, 29, 955957.
3. Jacoby GA,, Carreras I, 1990, Activities of β-lactam antibiotics against Escherichia coli strains producing extended-spectrum β-lactamases, Antimicrob Agents Chemother, 34, 858862.
4. Kitzis MD,, Billot-Klein D,, Goldstein FW,, Williamson R,, Tran Van Nhieu G, Carlet J, Acar JF,, Gutmann L, 1988, Dissemination of the novel plasmid-mediated β-lactamase CTX-1, which confers resistance to broad-spectrum cephalosporins, and its inhibition by β-lactamase inhibitors, Antimicrob Agents Chemother, 32, 914.

Tables

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Table 1

Citation: Kazmierczak A. 2005. β-Lactamase Inhibitors, p 401-409. In Bryskier, M.D. A (ed), Antimicrobial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555815929.ch13
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Table 2

Citation: Kazmierczak A. 2005. β-Lactamase Inhibitors, p 401-409. In Bryskier, M.D. A (ed), Antimicrobial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555815929.ch13
Generic image for table
Table 3

Citation: Kazmierczak A. 2005. β-Lactamase Inhibitors, p 401-409. In Bryskier, M.D. A (ed), Antimicrobial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555815929.ch13
Generic image for table
Table 4

Citation: Kazmierczak A. 2005. β-Lactamase Inhibitors, p 401-409. In Bryskier, M.D. A (ed), Antimicrobial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555815929.ch13
Generic image for table
Table 5

Citation: Kazmierczak A. 2005. β-Lactamase Inhibitors, p 401-409. In Bryskier, M.D. A (ed), Antimicrobial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555815929.ch13
Generic image for table
Table 6

Citation: Kazmierczak A. 2005. β-Lactamase Inhibitors, p 401-409. In Bryskier, M.D. A (ed), Antimicrobial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555815929.ch13
Generic image for table
Table 7

Citation: Kazmierczak A. 2005. β-Lactamase Inhibitors, p 401-409. In Bryskier, M.D. A (ed), Antimicrobial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555815929.ch13
Generic image for table
Table 8

Citation: Kazmierczak A. 2005. β-Lactamase Inhibitors, p 401-409. In Bryskier, M.D. A (ed), Antimicrobial Agents. ASM Press, Washington, DC. doi: 10.1128/9781555815929.ch13

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