人体肠道细菌为分解饮食和宿主衍生的甘氨酸量身定制细胞外囊泡载荷
Mariana G Sartorio1, Evan J Pardue1, Nichollas E Scott2
1Department of Molecular Microbiology, Washington University School of Medicine, Saint Louis, MO 63110.
概括
细菌外膜囊泡 (OMV) 生产是一个受管制的过程. 研究人员可视化了BActeroides thetaiotaomicron中的OMV生物发生,揭示了特定的蛋白质分类信号,并适应了OMV货物用于营养利用.
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:
- 细胞外囊泡在真核生物和古生物中具有共同的古代起源,但细菌囊泡生物发生仍然不太清楚,这导致人们对它们的生物学相关性持怀疑态度.
- 细菌菌体thetaiotaomicron (Bt),一个关键的人类肠道共生体,产生外膜囊泡 (OMVs) 涉及至关重要的生理作用.
研究的目的:
- 阐明细菌中OMV生物发生的机制,特别是在Bacteroides中thetaiotaomicron.
- 调查对OMV生产和货物分类的监管,以响应环境线索.
主要方法:
- 使用光蛋白的双标记系统,通过时间缩短显微镜可视化OMV生物发生.
- 进行了比较蛋白质组学分析,以描述OMV货物的组成.
- 确定了参与OMV分类的特定蛋白质图案.
主要成果:
- 证明Bt的OMV生产是一个高度受监管的过程.
- 证明Bt OMV含有专门适应各种多糖的货物.
- 鉴定出负电荷的N端模因作为蛋白质分类到OMV的信号,独立于营养的可用性.
结论:
- 细菌OMV生物发生是一个受管制和机械定义的过程.
- Bt OMV 在营养获取中发挥作用,通过提供酶来分解多糖.
- 蛋白质分类到OMV是由特定信号控制的,确保功能性货物交付.
相关概念视频
Oligosaccharide Assembly
2.9K
Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
Multiple sugar molecules that may or may...
2.9K
Lysosomal Hydrolases
3.9K
Lysosomes are the site for the degradation of macromolecules and biological polymers released during membrane trafficking events such as secretory, endocytic, autophagic, and phagocytic pathways. The membrane-enclosed area of the lysosome, called the lumen, contains hydrolytic enzymes active in an acidic environment. These acid hydrolases are functional at a pH between 4.5 and 5 and are involved in cellular processes such as cell signaling, energy metabolism, restoration of the plasma membrane,...
3.9K
Delivery Pathways to the Lysosome
6.6K
Eukaryotic cells use different mechanisms to eliminate toxic waste obsolete and worn-out substances. Lysosomes play a pivotal role in this, and hence, these substances are carried to the lysosome from other parts of the cell and extracellular space through different pathways. The most elaborately studied pathways to the lysosome are the endocytic pathways.
Endocytosis
In endocytosis, the cell membrane takes up macromolecules and particles from the surrounding medium. Clathrin-mediated...
Endocytosis
In endocytosis, the cell membrane takes up macromolecules and particles from the surrounding medium. Clathrin-mediated...
6.6K
Export of Misfolded Proteins out of the ER
3.7K
After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
3.7K
Lysosomes
19.2K
Lysosomes are membrane-enclosed spherical sacs derived from the Golgi apparatus. The most important function of the lysosome is degrading macromolecules and biological polymers that are released during membrane trafficking events such as the secretory, endocytic, autophagic, and phagocytic pathways. The degradation is carried out by several hydrolytic enzymes active in an acidic environment of the lysosomal lumen. These acid hydrolases are involved in cellular processes such as cell signaling,...
19.2K
Proteoglycans
4.0K
Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
4.0K


