鲍曼不动杆菌中参与对亚胺培南耐药的水解苯唑西林β-内酰胺酶
Oxacillin-hydrolyzing beta-lactamase involved in resistance to imipenem in Acinetobacter baumannii.
作者信息
Hornstein M, Sautjeau-Rostoker C, Péduzzi J, Vessières A, Hong L T, Barthélémy M, Scavizzi M, Labia R
机构信息
Service de Bactériologie-Virologie, Centre Hospitalier Universitaire Avicenne, Université Paris Nord, Bobigny, France.
出版信息
FEMS Microbiol Lett. 1997 Aug 15;153(2):333-9. doi: 10.1111/j.1574-6968.1997.tb12593.x.
Acinetobacter baumannii strain A148, a clinical isolate resistant to imipenem (MIC = 32 mg l-1), synthesized two beta-lactamases with pIs 6.3 and > 9.2. The pI 6.3 enzyme hydrolyzed the penicillins, including isoxazoylpenicillins, first-, second- and, to a lesser extent, third-generation cephalosporins. It was inhibited by chloride ions and by the penem beta-lactamase inhibitor BRL 42715. Clavulanate was a weak inhibitor and EDTA did not affect the beta-lactamase activity. This enzyme also hydrolyzed imipenem with a catalytic efficiency (Kcat/Km) of 1500 mM-1 s-1. Moreover, this purified beta-lactamase produced a positive microbiological clover-leaf test with imipenem. Therefore, the pI 6.3 beta-lactamase was considered to be involved in the imipenem resistance of A. baumannii strain A148.
鲍曼不动杆菌A148菌株是一株对亚胺培南耐药（MIC = 32 mg l-1）的临床分离株，它合成了两种pI分别为6.3和> 9.2的β-内酰胺酶。pI为6.3的酶可水解青霉素类，包括异恶唑青霉素类、第一代、第二代以及程度较轻的第三代头孢菌素。它受到氯离子和青霉烯β-内酰胺酶抑制剂BRL 42715的抑制。克拉维酸是一种弱抑制剂，而EDTA不影响β-内酰胺酶活性。该酶还能以1500 mM-1 s-1的催化效率（Kcat/Km）水解亚胺培南。此外，这种纯化的β-内酰胺酶与亚胺培南进行微生物学三叶草叶试验呈阳性。因此，pI为6.3的β-内酰胺酶被认为与鲍曼不动杆菌A148菌株对亚胺培南的耐药性有关。
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