冷大气压等离子体产生的物种超氧化物,单片氧和原子氧激活了分子伴侣Hsp33的分子伴侣
Tim Dirks1, Marco Krewing1, Katharina Vogel1
1Applied Microbiology, Faculty of Biology and Biotechnology, Ruhr University Bochum, Bochum, Germany.
Journal of the Royal Society, Interface
|October 25, 2023
概括
热冲击蛋白Hsp33通过防止蛋白质聚合来增强细菌对寒冷大气等离子体的抵抗力. 然而,长时间暴露在血中会通过氧化使Hsp33失活.
科学领域:
- 微生物学 微生物学
- 生物物理学的生物物理.
- 血科学是一门科学课.
背景情况:
- 寒冷的大气等离子体被用于表面去污染和消毒.
- 蛋白质聚合是血的一个关键的抗菌机制.
- 氧化还原激活的结合伴侣Hsp33可能通过防止蛋白质聚合在血抵抗中发挥作用.
研究的目的:
- 为了研究Hsp33在调解细菌抵抗冷大气等离子体中的作用.
- 为了比较野生型大肠杆菌与Hsp33缺乏和过度生产的菌株的血敏感性.
主要方法:
- 对暴露于寒冷大气等离子体的大肠杆菌菌株 (野生型,hslO删除突变,hsp33过度产生) 的比较分析.
- 使用活性氧物种进行体外激活试验,以识别Hsp33激活剂.
- 在血治疗后评估Hsp33激活,结合能力和蛋白质氧化.
主要成果:
- 过度生产Hsp33显著增加了在血暴露后大肠杆菌的存活率.
- 在体外和与PlasmaDerm源证实了Hsp33的激活,涉及醇氧化和展开.
- 长时间暴露于血导致不特定蛋白质的氧化,减少Hsp33的结合,并使其无活化.
- 超氧化物,单片氧和原子氧在体外被确定为Hsp33激活剂.
结论:
- Hsp33有助于细菌抵抗冷大气等离子体.
- 血诱导的Hsp33激活是可逆的,并由特定的活性氧物种介导.
- 过度暴露于血可能导致Hsp33的失活,限制其保护作用.
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