金黄色葡萄球菌GrlB蛋白中的喹诺酮耐药性突变。
Quinolone resistance mutations in the GrlB protein of Staphylococcus aureus.
作者信息
Tanaka M, Onodera Y, Uchida Y, Sato K
机构信息
New Product Research Laboratories I, Daiichi Pharmaceutical Co. Ltd., Edogawa-ku, Tokyo 134-8630, Japan.
出版信息
Antimicrob Agents Chemother. 1998 Nov;42(11):3044-6. doi: 10.1128/AAC.42.11.3044.
Abstract
Two altered GrlB proteins (one with an Asp-432-->Asn alteration and one with an Asn-470-->Asp alteration) of Staphylococcus aureus were purified as fusion proteins to maltose-binding protein. The 50% inhibitory concentrations of levofloxacin were 14 and 3.4 microg/ml against topoisomerase IV containing GrlB proteins with alterations at positions 432 and 470, respectively. These results suggest that the alteration of Asp to Asn at position 432 may be responsible for quinolone resistance.
摘要
将金黄色葡萄球菌的两种改变的GrlB蛋白（一种是Asp-432→Asn改变，另一种是Asn-470→Asp改变）作为与麦芽糖结合蛋白的融合蛋白进行纯化。左氧氟沙星对含有分别在432位和470位发生改变的GrlB蛋白的拓扑异构酶IV的50%抑制浓度分别为14和3.4微克/毫升。这些结果表明，432位的Asp变为Asn的改变可能是喹诺酮耐药的原因。
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