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来自Leishmania donovani的T复合蛋白-1的三角形子单元的分子,结构和功能表征
Apeksha Anand1,2, Gunjan Gautam1, Gaurava Srivastava1
1Division of Biochemistry and Structural Biology, CSIR-Central Drug Research Institute, Lucknow, Uttar Pradesh, India.
Infection and immunity
|September 9, 2024
概括
这项研究描述了Leishmania donovani TCP1δ chaperonin的特征,揭示了其独特的家族遗传分支和同类寡合体复合体形成. 过度表达增强了寄生虫的感染力和繁殖能力,突出了它在Leishmania donovani病变发生中的作用.
科学领域:
- 分子生物学分子生物学
- 寄生虫学的寄生虫学
- 蛋白质的生物化学 蛋白质的生物化学
背景情况:
- 像热冲击蛋白60一样的护卫蛋白对所有生物体中的蛋白质折叠至关重要.
- 欧核生物II组沙佩罗宁 (TRiC/TCP1/CCT) 由多个子单元组成,形成一个异质寡合体复合体.
- 在Leishmania donovani中,以前只有LdTCP1γ亚单元得到了良好的特征.
研究的目的:
- 从分子,结构和功能上描述来自Leishmania donovani的TCP1δ子单元 (LdTCP1δ).
- 调查LdTCP1δ.的寡合状态和体外沙佩罗宁活性.
- 确定LdTCP1δ在Leishmania donovani感染力和繁殖中的作用.
主要方法:
- 基因测序和遗传学分析以比较LdTCP1δ与LdTCP1γ.
- 重组LdTCP1δ复合物的蛋白质净化和表征 (大小和组装).
- 在试验室中使用依赖ATP的光酶折叠的Chaperonin测定.
- 在Leishmania promastigotes中进行基因表达分析和过度表达研究.
主要成果:
- LdTCP1δ与LdTCP1γ只有27.9%的相同性,并形成了一个独特的基因组.
- 纯化的重组LdTCP1δ形成了一个高分子量 (0.75 MDa) 的16-mer同类寡合体复合体.
- LdTCP1δ在体外表现出依赖ATP的沙佩罗宁活性,并且在分裂的寄生虫中被上调.
- 过度表达LdTCP1δ显著增加了Leishmania donovani的感染力和细胞内巨的繁殖.
结论:
- 在Leishmania donovani中,LdTCP1δ形成了一个独立的,功能性活跃的同类寡合体沙佩罗宁复合体.
- LdTCP1δ在寄生虫感染性和繁殖中发挥着关键作用,这表明它是潜在的治疗点.
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