格兰阳性细菌中排序酶组装Pili的生物发生和功能
Chungyu Chang1, Nicholas A Ramirez2, Aadil H Bhat1
1Division of Oral and Systemic Health Sciences, School of Dentistry, University of California, Los Angeles, California, USA;
Annual review of microbiology
|August 14, 2024
概括
格拉姆阳性细菌使用特定于pilus的排序酶在细胞表面组装 pili (fimbriae). 这些 pili对于细菌粘附,免疫调节和毒性至关重要,在生物技术中具有应用.
科学领域:
- 微生物学 微生物学
- 细菌细胞表面结构的结构
- 蛋白质组装组合是什么
背景情况:
- 格拉姆阳性细菌利用 pili,也称为 fimbriae,它们是多重蛋白质结构,联联成子单元.
- 这些 pili 被组装在细菌细胞表面上,并通过保存的转酶酶,pilus-specific sortase.通过细菌细胞表面显示.
- 皮利菌在各种生态的多种格拉姆阳性细菌中发现,包括人类的口腔,肠道,泌尿器官和皮肤.
研究的目的:
- 为了提供一种全面的审查,在格拉姆阳性细菌的sortase-assembled pili.
- 阐明这些表面附件的组装机制和各种功能.
- 讨论 pili 在疫苗开发和生物技术中的当前状态和未来潜力.
主要方法:
- 综述了广泛的遗传研究.
- 分析生化和生理数据.
- 检查结构生物学发现的结果.
主要成果:
- 排序酶组装的 pili 是细菌功能不可或缺的组成部分,作为分子粘合剂,免疫调节剂和毒性因子.
- 这些表面结构显著影响细菌的共生性和病原性特征.
- 组装和显示机制在广泛的グラム阳性细菌中保持一致.
结论:
- 排序酶组装的 pili 是细菌与其环境和宿主相互作用的关键决定因素.
- 了解的组装和功能对于开发包括疫苗在内的新生物技术应用至关重要.
- 对的持续研究为微生物病原和治疗策略的未来进步提供了有希望的途径.
相关概念视频
Cytoskeletal Proteins in Bacteria
3.3K
Bacterial cells were initially considered simple, randomly organized structures lacking a cytoskeleton. However, the discovery of cytoskeleton homologs in bacteria led to the change of this opinion. Bacterial cytoskeletal filaments regulate the cell shape, cell polarity, cell division, and partitioning of plasmids during cell division. It was later discovered that bacterial cytoskeletal proteins, mainly actin and tubulin homologs, are diverse compared to their eukaryotic counterparts. On the...
3.3K
Mechanism of Filopodia Formation
2.3K
Filopodia are thin, actin-rich cellular protrusions that play an important role in many fundamental cellular functions. They vary in their occurrence, length, and positioning in different cell types, suggesting their diverse roles.
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
Their main function is to guide migrating cells during normal tissue morphogenesis or cancer metastasis by recognizing and making initial contacts with the extracellular matrix. However, they can also act as stationary cell anchors or help to establish communication...
2.3K
Structure of Porins
2.9K
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...
2.9K
Generation of Straight or Branched Actin Filaments
2.9K
The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
2.9K
Septins
1.8K
Septins are protein filaments forming the cytoskeleton along with the microtubules, microfilaments, intermediate filaments, and other accessory proteins. In 1971 while studying the cell division cycle in mutant Saccharomyces cerevisiae Harwell et al. first identified the septin-related genes playing a crucial role in yeast cytokinesis. Fluorescence microscopy revealed that these proteins localize at the budding neck as rings. These ring-like proteins were then named Septins by John Pringle, and...
1.8K
Formation of Higher-order Actin Filaments
3.0K
The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
The high-order actin...
The high-order actin...
3.0K


