对PP01菌体gp38尾部纤维尖端与大肠杆菌OmpC受体之间的相互作用的结构和功能见解
Haruka Terasaki1, Aleksandar Zdravković2,3, Tatsuya Niwa2,3
1Department of Biochemistry and Molecular Biology, Graduate School of Science and Engineering, Saitama University, Saitama, Japan.
mBio
|January 9, 2026
概括
我们阐明了Escherichia coli O157外膜蛋白C (OmpC) 和菌体PP01之间的分子相互作用.
科学领域:
- 微生物学 微生物学
- 结构生物学 结构生物学
- 分子生物学分子生物学
背景情况:
- 菌体表现出严格的宿主特异性,对于感染至关重要.
- 菌体-宿主识别的分子机制尚未完全理解.
- 大肠杆菌的外膜蛋白C (OmpC) 是一种关键的细菌表面受体.
研究的目的:
- 研究来自菌体PP01.01的大肠杆菌O157和gp38的OmpC之间的相互作用.
- 为了确定菌体PP01宿主特异性的结构基础.
- 为改造具有改变宿主范围的菌体提供洞察力.
主要方法:
- 确定了菌体PP01.01的gp38受体结合域 (RBD) 的晶体结构.
- 使用p-基-L-氨 (pBPA) 的特定位置的照片交叉链接.
- 采用液体染色学-双重质谱法 (LC-MS/MS) 来识别交联的残留物.
- 构建并验证了gp38-OmpC复合物的结构模型,使用距离受约束的预测和突变发生.
主要成果:
- gp38PP01 RBD 的晶体结构揭示了具有受体识别循环的多糖氨酸II型螺旋.
- 通过照片交叉连接,确定了gp38PP01和OmpCO157之间的两个关键接触点.
- 证明了gp38PP01的循环-E与OmpCO157的循环-5和-7形成的裂相互作用.
- 通过向突变发生法验证了结合模型.
结论:
- 菌体PP01的特异性是由gp38循环-E与OmpC循环-5和-7.7的相互作用决定的.
- 结构和功能洞察力提高了对菌体与宿主体识别的理解.
- 这些发现可以为治疗应用提供改变宿主特异性的菌体的合理设计信息.
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