一种多铁酶在一种不可型的Haemophilus influenzae病毒性因子上安装了结合铜的oxazolone/thioamide对
Olivia M Manley1,2, Tucker J Shriver3, Tian Xu1,2
1Department of Molecular Biosciences, Northwestern University, Evanston, IL 60208.
概括
一个新型的酶途径在非可定型的Haemophilus influenzae中修改了一个毒性因子,oxazolin,使用一个triiron辅因子. 这种修饰对于铜离子协调和细菌感染至关重要,是潜在的治疗标.
科学领域:
- 生物化学 生物化学
- 微生物学 微生物学
- 酶学 是一种酶学.
背景情况:
- 多核非海姆铁依赖氧化酶 (MNIO) 是合成天然产品的关键酶.
- 来自非类型性Haemophilus influenzae (NTHi) 的毒性因子与MNIO编码的操作子相关.
研究的目的:
- 描述MNIO HvfB及其在修改NTHi毒性因子HvfA中的作用.
- 为了阐明成熟毒性因子oxazolin的翻译后修饰和结构.
- 调查佐林在NTHi感染中的功能及其作为治疗点的潜力.
主要方法:
- 莫斯巴乌尔光谱法用于识别HVfB辅因子.
- 生物化学分析以证明HVfB和HVfC活动.
- 串联质谱和NMR用于修饰的结构特征.
主要成果:
- HvfB 含有三铁辅因子.
- HvfB 和 HvfC 催化了 HvfA 上的六种囊蛋白修饰,形成了 oxazolone 和 thioamide 双体.
- 成熟的,oxazolin,利用这些修改来协调Cu (I) 离子.
- 奥克萨佐林对于NTHi宿主细胞入侵至关重要.
结论:
- HvfB/HvfC酶系统进行了独特的翻译后修饰,产生了zolin.
- 奥克萨佐林的铜结合能力对于NTHi的毒性至关重要.
- 氧沙林生物合成途径是NTHi感染的潜在治疗标.
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