本文選題：OptrA + ATP水解酶�。� 參考：《中國獸醫(yī)學報》2017年04期

【摘要】：通過ATP水解酶活性試驗分析2個突變位點對OptrA活性的影響,并通過最低抑菌濃度試驗分析不同突變位點對金黃色葡萄球菌耐藥性的影響。將OptrA蛋白作抗原免疫日本大耳白兔,提取血清抗體,用Western bolt分析突變前后蛋白表達量的變化。結(jié)果顯示,當把全長氨基酸序列208和488位的谷氨酸(E)突變后,OptrA在金黃色葡萄球菌中的表達量不變,但其ATP水解活性分別降低30%和70%,并且都導致金黃色葡萄球菌失去了對氟苯尼考的耐藥性。說明OptrA需要水解ATP才能介導細菌耐藥性,為以后研究新耐藥蛋白OptrA的抑制劑和腸球菌感染的防制奠定基礎。
[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.
【作者單位】： 吉林大學動物科學學院;
【基金】：“十三五”國家重點研發(fā)計劃資助項目(2016YFD05013)
【分類號】：S852.61
，

本文編號：2046606