关于新耐药蛋白OptrA的2个关键活性位点

发布时间：2018-06-21 01:41

  本文选题：OptrA + ATP水解酶　； 参考：《中国兽医学报》2017年04期

【摘要】：通过ATP水解酶活性试验分析2个突变位点对OptrA活性的影响,并通过最低抑菌浓度试验分析不同突变位点对金黄色葡萄球菌耐药性的影响。将OptrA蛋白作抗原免疫日本大耳白兔,提取血清抗体,用Western bolt分析突变前后蛋白表达量的变化。结果显示,当把全长氨基酸序列208和488位的谷氨酸(E)突变后,OptrA在金黄色葡萄球菌中的表达量不变,但其ATP水解活性分别降低30%和70%,并且都导致金黄色葡萄球菌失去了对氟苯尼考的耐药性。说明OptrA需要水解ATP才能介导细菌耐药性,为以后研究新耐药蛋白OptrA的抑制剂和肠球菌感染的防制奠定基础。
[Abstract]:The effects of two mutation sites on OptrA activity were analyzed by ATP hydrolase activity test, and the effects of different mutation sites on the resistance of Staphylococcus aureus were analyzed by the minimum inhibitory concentration test. Optra protein was used as antigen to immunize Japanese white rabbits, and serum antibody was extracted. The changes of protein expression before and after mutation were analyzed by Western bolt. The results showed that the expression of OptrA in Staphylococcus aureus was unchanged after the mutation of the full length amino acid sequences 208 and 488. But its ATP hydrolysis activity decreased by 30% and 70%, respectively, and both of them caused Staphylococcus aureus to lose its resistance to florfenicol. The results showed that OptrA needed ATP hydrolysis to mediate bacterial resistance, which laid a foundation for the study of the inhibitor of new resistant protein OptrA and the prevention and control of enterococcal infection.
【作者单位】： 吉林大学动物科学学院;
【基金】：“十三五”国家重点研发计划资助项目(2016YFD05013)
【分类号】：S852.61
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本文编号：2046606