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阿维巴坦与头孢他啶水解型 D 类β-内酰胺酶的相互作用。

Interactions between Avibactam and Ceftazidime-Hydrolyzing Class D β-Lactamases.

机构信息

Centre for Protein Engineering, University of Liège, B 4000 Liège, Belgium.

National Reference Laboratory for Monitoring of Antimicrobial Resistance in Gram-Negative Bacteria, CHU Dinant-Godinne, UCL Namur, B 5530 Yvoir, Belgium.

出版信息

Biomolecules. 2020 Mar 23;10(3):483. doi: 10.3390/biom10030483.

DOI:10.3390/biom10030483
PMID:32209976
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7175300/
Abstract

Class D β-lactamases exhibit very heterogeneous hydrolysis activity spectra against the various types of clinically useful β-lactams. Similarly, and according to the available data, their sensitivities to inactivation by avibactam can vary by a factor of more than 100. In this paper, we performed a detailed kinetic study of the interactions between two ceftazidime-hydrolyzing OXA enzymes and showed that they were significantly more susceptible to avibactam than several other class D enzymes that do not hydrolyze ceftazidime. From a clinical point of view, this result is rather interesting if one considers that avibactam is often administered in combination with ceftazidime.

摘要

D 类 β-内酰胺酶对各种临床有用的β-内酰胺类药物的水解活性谱具有很大的异质性。同样,根据现有数据,它们对阿维巴坦失活的敏感性差异超过 100 倍。在本文中,我们对两种头孢他啶水解 OXA 酶之间的相互作用进行了详细的动力学研究,结果表明它们对阿维巴坦的敏感性明显高于其他几种不水解头孢他啶的 D 类酶。从临床的角度来看,如果考虑到阿维巴坦通常与头孢他啶联合使用,那么这一结果是非常有趣的。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f643/7175300/655df9f852b0/biomolecules-10-00483-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f643/7175300/e0a20dce2bf2/biomolecules-10-00483-g0A1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f643/7175300/ac02d35fbf63/biomolecules-10-00483-g0A2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f643/7175300/d711953283fb/biomolecules-10-00483-sch001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f643/7175300/6a9ac8bafcd6/biomolecules-10-00483-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f643/7175300/0e2a347a9752/biomolecules-10-00483-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f643/7175300/b92bf83c4e46/biomolecules-10-00483-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f643/7175300/655df9f852b0/biomolecules-10-00483-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f643/7175300/e0a20dce2bf2/biomolecules-10-00483-g0A1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f643/7175300/ac02d35fbf63/biomolecules-10-00483-g0A2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f643/7175300/d711953283fb/biomolecules-10-00483-sch001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f643/7175300/6a9ac8bafcd6/biomolecules-10-00483-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f643/7175300/0e2a347a9752/biomolecules-10-00483-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f643/7175300/b92bf83c4e46/biomolecules-10-00483-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f643/7175300/655df9f852b0/biomolecules-10-00483-g004.jpg

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Nat Rev Microbiol. 2019 May;17(5):295-306. doi: 10.1038/s41579-019-0159-8.
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Past and Present Perspectives on β-Lactamases.β-内酰胺酶的过去与现在观点。
Antimicrob Agents Chemother. 2018 Sep 24;62(10). doi: 10.1128/AAC.01076-18. Print 2018 Oct.
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Probing the Mechanism of Inactivation of the FOX-4 Cephamycinase by Avibactam.探究阿维巴坦对 FOX-4 头孢菌素酶失活机制。
CDD-1酶与阿维巴坦的时间分辨相互作用为D类β-内酰胺酶的催化机制提供了新见解。
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Genetic Diversity, Biochemical Properties, and Detection Methods of Minor Carbapenemases in Enterobacterales.肠杆菌科细菌中碳青霉烯类小酶的遗传多样性、生化特性及检测方法
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Structural and Biochemical Characterization of the Novel CTX-M-151 Extended-Spectrum β-Lactamase and Its Inhibition by Avibactam.新型 CTX-M-151 型扩展谱β-内酰胺酶的结构和生化特性及其被阿维巴坦的抑制作用。
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Inhibition of the Class D β-Lactamase CDD-1 by Avibactam.阿维巴坦对 Class D β-内酰胺酶 CDD-1 的抑制作用。
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Reply to "Noncarbapenemase OXA-48 Variants (OXA-163 and OXA-405) Falsely Detected as Carbapenemases by the β Carba Test".对“β-内酰胺酶检测法将非碳青霉烯酶OXA-48变体(OXA-163和OXA-405)误检测为碳青霉烯酶”的回复
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9
Noncarbapenemase OXA-48 Variants (OXA-163 and OXA-405) Falsely Detected as Carbapenemases by the β Carba Test.非碳青霉烯酶OXA-48变体(OXA-163和OXA-405)被β-卡巴测试错误检测为碳青霉烯酶。
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