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Updated: Jun 25, 2025

Generation of Null Mutants to Elucidate the Role of Bacterial Glycosyltransferases in Bacterial Motility
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甜味复杂性:在致病性尼塞利亚菌中与O相关的蛋白质糖化

Bente Børud1, Michael Koomey2

  • 1Department of Bacteriology, Division for Infection Control and Environmental Health, Norwegian Institute of Public Health, Oslo, Norway.

Frontiers in cellular and infection microbiology
|May 29, 2024
PubMed
概括

尼塞利亚细菌利用O链蛋白糖化,导致各种表面糖蛋白. 尼塞利亚菌中的甘氨酸变异性可能有助于逃避人类免疫系统,病原性和开始性物种之间存在差异.

关键词:
尼塞里亚淋病菌 (Neisseria gonorrhoeae) 是一种传染病.脑膜炎的尼塞利亚菌.糖甘多样性的多样性免疫系统逃脱,逃离免疫系统.免疫性 免疫性 免疫性

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Proteoglycans

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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...
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Protein Glycosylation

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...
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GPI Anchoring of Proteins in the ER Membrane

GPI-anchoring is a post-translational, reversible protein modification that is ubiquitous in eukaryotes. Such proteins are primarily present on the exoplasmic leaflet of the plasma membrane.
GPI-anchor structure
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