塞拉提亚蛋白质与整合素的相互作用激活了促进入侵的信号通路
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1Institute of Cytology, Russian Academy of Sciences, Tikhoretsky av. 4, 194064 St. Petersburg, Russia.
塞拉蒂亚蛋白质使用其OmpX蛋白质与人类α5β1整合素受体结合,促进细菌入侵. 这种相互作用激活了涉及EGFR和FAK的信号通路,这对感染期间细胞骨变化至关重要.
科学领域:
- 微生物学 微生物学
- 细胞生物学 细胞生物学
- 生物化学 生物化学
背景情况:
- 塞拉蒂亚蛋白质虫是一种机会性病原体,能够侵入人类细胞.
- 众所周知,细菌表面蛋白OmpX可以促进细菌的粘附.
- 生产OmpX的细菌增强EGFR和β1整合素的表达,这些都参与了S. proteamaculans的入侵.
研究的目的:
- 阐明S. proteamaculans和真核细胞受体之间的相互作用机制.
- 为了确定细菌入侵中涉及的特定受体和信号通路.
主要方法:
- 研究了整合素结合酶 (ILK) 和EGFR氨酸酶在细菌入侵中的作用.
- 在 Tyr845 中通过 c-Src 激酶介导的 EGFR 酸化分析.
- 评估了S. proteamaculans入侵对c-Src和焦粘附激酶 (FAK) 的依赖性.
- 检查了与整蛋白的细菌相互作用,特别是RGD结合部位和RGD效应.
- 确定了OmpX在细菌粘附和整蛋白表达中的作用.
主要成果:
- 通过c-Src激酶在Tyr845的EGFR酸化是感染期间的早期事件.
- S. proteamaculans的入侵依赖于c-Src和FAK信号,它们是β1整合素和EGFR的桥梁.
- 细菌与整合素相互作用,独立于RGD结合部位;RGD增强了侵入和整合素子单元的表达.
- 在感染期间,OmpX负责细菌粘附和增加整合素表达.
结论:
- 在S. proteamaculans的OmpX蛋白与宿主细胞α5β1集成相互作用.
- 这种相互作用触发了涉及EGFR,c-Src和FAK的信号级联,导致细胞骨重组和细菌入侵.
- 在S. proteamaculans感染期间,α5β1整蛋白被确定为OmpX的可能受体.
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