旗素与O结合的甘氨酸对于Campylobacter jejuni和Acanthamoebae castellanii之间的相互作用是必需的
Fauzy Nasher1, Brendan W Wren1
1London School of Hygiene and Tropical Medicine, London, UK.
Microbiology (Reading, England)
|August 23, 2023
概括
阿坎萨莫贝菌吞了细菌,成为像Campylobacter jejuni.这样的病原体的存储库. 在C. jejuni flagellin (FlaA) 上的特定O-链 glycan 修饰对于Acanthamoeba castellanii的相互作用和吸收至关重要,而不是鞭毛运动性.
科学领域:
- 微生物学 微生物学
- 病原体生态学 病原体生态学
- 细菌病原体的产生
背景情况:
- 阿坎萨莫贝菌是细胞化细菌,影响病原体生理学,生态学和进化.
- 坎皮洛巴克特 (Campylobacter jejuni) 是导致食物传播疾病的主要原因,在环境中存在,但其传播机制尚不清楚.
- 阿坎萨摩巴群作为C. jejuni的暂时宿主,其鞭毛突变影响了它们的相互作用.
研究的目的:
- 为了研究鞭毛成分在C. jejuni-Acanthamoeba castellanii相互作用中的作用.
- 为了确定鞭毛机动性是否对于C. jejuni与A. castellanii的相互作用至关重要.
- 为了识别特定的C. jejuni旗蛋白修饰,这对于Acanthamoeba的识别和 fagocytosis很重要.
主要方法:
- 对C. jejuni野生型,鞭毛突变 (ΔflaA) 和特定部位的FlaA糖化突变 (S415A,T477A,S405A) 与A. castellanii相互作用的比较分析.
- 显微镜和共同培养试验评估细菌的识别,粘附和被A. castellanii吞.
- 对C. jejuni旗蛋白 (FlaA) 的基因操纵. O-链接的糖化位点.
主要成果:
- 对于C. jejuni与A. castellanii的相互作用,不需要旗运动.
- 在C. jejuni flagellin FlaA上,特定的O-链接糖化位点 (Ser415和Thr477) 对A. castellanii的识别和细胞形成至关重要.
- 这些糖化位点的突变使得C. jejuni在与A. castellanii相互作用时无法与ΔflaA突变体区分,而Ser405的突变没有影响.
结论:
- 在C. jejuni旗蛋白FlaA的O-联结糖化,而不是旗运动性,介导与Acanthamoeba castellanii的相互作用.
- 这些发现凸显了鞭毛糖化在宿主-病原体相互作用中的重要性,这可能对其他病原体产生潜在影响.
- 了解这些相互作用可能会为C. jejuni.的环境持久性和传播提供见解.
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