描述Ssc,一个含有 Staphylococcus aureus 的 N - 乙甲糖胺表面多糖体
Mei G Lei1, Matthew A Jorgenson1, Emily J Robbs1
1Department of Microbiology and Immunology, University of Arkansas for Medical Sciences, Little Rock, Arkansas, USA.
Journal of bacteriology
|May 7, 2024
概括
研究人员在金黄色葡萄球菌中发现了一种新的葡萄球菌表面碳水化合物 (Ssc). 这种N-乙甲胺多糖对菌体相互作用产生影响,这表明它在细菌表面结构和防御中发挥了作用.
科学领域:
- 微生物学 微生物学
- 葡萄糖生物学 葡萄糖生物学
- 细菌病原体的产生
背景情况:
- 黄金葡萄球菌 (Staphylococcus aureus) 具有具有良好特征的表面多糖,这对其生物学和毒性至关重要.
- 全基因组测序发现了一种新型的5基因操作子 (葡萄球菌表面碳水化合物,SSC),可能参与多糖化合物合成和出口.
研究的目的:
- 描述新型葡萄球菌表面碳水化合物 (Ssc) 的特征,该碳水化合物由黄金葡萄球菌中的ssc操作子编码.
- 为了确定新发现的多糖的组成和表面暴露.
主要方法:
- 在大肠杆菌中ssc基因的异质表达.
- 蛋白质甘氨酸合技术 (PGCT) 用于糖合物形成.
- 配对质谱仪用于组合分析.
- 在S. aureus中菌体吸附和敏感性的评估.
主要成果:
- ssc操作子编码了一种多糖,主要由N-乙糖氨酸胺 (GalNAc) 组成.
- 这是首次发现Staphylococcus aureus中含有GalNAc的多糖体.
- ssc基因的表达影响了菌体吸附和敏感性,表明了表面暴露.
结论:
- 黄金葡萄球菌产生一种新型的表面多糖体,Ssc,含有N-乙甲胺.
- Ssc在调节与细菌菌体相互作用方面发挥着作用.
- 这一发现为了解Ssc在S. aureus表面结构和病变发生中的作用开辟了道路.
相关概念视频
Oligosaccharide Assembly
2.8K
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...
2.8K
Proteoglycans
3.9K
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,...
3.9K
Protein Glycosylation
6.9K
Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
Glycosylation occurs in...
6.9K
Glycocalyx and its Functions
4.0K
The glycocalyx is a carbohydrate-rich, fuzzy-appearing layer on the outer surface of the cell membrane. It is highly hydrophilic, because of this it attracts large amounts of water to the cell's surface. This aids the cell's interaction with the watery environment and also helps it to obtain substances dissolved in the water. It is also important for cell identification, self/non-self determination, and embryonic development and is used in cell-to-cell attachments to form tissues.
4.0K
Glycosaminoglycans
4.8K
Glycosaminoglycans (GAGs), also known as mucopolysaccharides, are long and linear polymers comprising of specific repeating disaccharides - the amino sugar that can be N-acetylglucosamine or N-acetylgalactosamine, and a uronic acid that is usually glucuronic acid or iduronic acid.
GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
Hyaluronic...
GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
Hyaluronic...
4.8K


