毒素膜内醇脂结合蛋白TgREMIND对于分泌器官功能和宿主感染至关重要
Rodrigue Houngue1, Lamba Omar Sangaré2, Tchilabalo Dilezitoko Alayi3
1Université Paris Saclay, CNRS UMR 9198-CEA, Institute for Integrative Biology of the Cell (I2BC), 91190 Gif sur Yvette, France.
Cell reports
|December 29, 2023
概括
托克索普拉斯马洪迪蛋白TgREMIND对于飞和密集颗粒生物生成至关重要. 它的缺失会通过破坏基本分泌器官的功能来损害寄生虫感染.
科学领域:
- 细胞生物学 细胞生物学
- 寄生虫学的寄生虫学
- 分子生物学分子生物学
背景情况:
- 像Toxoplasma gondii这样的虫寄生虫利用专门的分泌器官来侵入宿主细胞.
- 罗普特体,微粒体和密集的颗粒体对于寄生虫的生存和病变产生至关重要.
- 了解这些有机体的生物发生和功能是开发抗寄生虫策略的关键.
研究的目的:
- 调查新型蛋白TgREMIND在Toxoplasma gondii分泌器官的生物发生和功能中的作用.
- 阐明TgREMIND对其活动至关重要的结构领域.
主要方法:
- 在Toxoplasma gondii中,TgREMIND蛋白的耗尽.
- 显微镜评估器官形态和蛋白质定位.
- 从罗普特里和密集颗粒中分泌蛋白质的分析.
- 评估寄生虫的入侵和传播能力.
主要成果:
- TgREMIND对于rhoptries和密集颗粒的生物发生是必不可少的.
- 耗尽TgREMIND导致密集颗粒的丰富性降低,并导致异常.
- TgREMIND拥有一个膜结合的F-BAR域和一个新的REMIND域,这两者都对其功能至关重要.
- 由于TgREMIND缺失而导致的器官功能减少,显著抑制宿主入侵和寄生虫传播.
结论:
- 在Toxoplasma gondii中,TgREMIND对于关键分泌器官的正确形成和功能至关重要.
- TgREMIND 的 F-BAR 和 REMIND 域对于其在有机体生物发生中的作用至关重要.
- 向TgREMIND可能代表对抗毒素菌感染的新型治疗方法.
相关概念视频
01:43SNAREs and Membrane Fusion
10.9K
Once a transport vesicle has recognized its target organelle, the vesicular membrane needs to fuse with the target membrane to unload the cargo. Transmembrane proteins called SNAREs present on organelle membranes and their vesicles, mediate vesicle fusion.
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
10.9K
01:21Structure of Porins
3.0K
Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel...
3.0K
01:19Translocation of Proteins into the Mitochondria
3.1K
Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
3.1K
01:28Assembly of the Lipid Bilayer in the ER
3.2K
Biological membranes are more than just a barrier separating cell cytoplasm from the outside environment. They are highly dynamic and help maintain the integrity and physiological stability of the cells as well as membrane-bound organelles. Membranes also play vital roles in cell-to-cell and intracellular communication.
A large chunk of any biological membrane is composed of phospholipids. These lipids have a heterogeneous distribution across different subcellular organelles and even between...
A large chunk of any biological membrane is composed of phospholipids. These lipids have a heterogeneous distribution across different subcellular organelles and even between...
3.2K
01:45Tail-anchoring of Proteins in the ER Membrane
3.1K
Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
3.1K
01:28The Early Endosome: Endocytosis of Transferrin
3.3K
Essential proteins such as insulin or low-density lipoprotein (LDL) and micronutrients such as iron enter a eukaryotic cell through receptor-mediated endocytosis. Subsequently, the early endosomes fuse with the vesicles containing such receptor-ligand complexes and play a vital role in sorting the incoming ligands and receptors. While the ligands are either degraded inside the vesicle or released into the cytosol, their receptors are returned to the plasma membrane for further rounds of...
3.3K