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Related Concept Videos

Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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...
Glycocalyx and its Functions01:14

Glycocalyx and its Functions

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.
Components of...
Protein Glycosylation01:25

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...
Proteoglycans01:05

Proteoglycans

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,...

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Structural Biology and Analytical Chemistry Approaches for Characterizing C-Glycoside Metabolic Enzymes in Human Gut Microbiota
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Structural characterization of surface glycans from Clostridium difficile.

Christopher W Reid1, Evgeny Vinogradov, Jianjun Li

  • 1National Research Council-Institute for Biological Sciences, 100 Sussex Drive, Ottawa, ON, Canada K1A 0R6.

Carbohydrate Research
|May 8, 2012
PubMed
Summary

High-resolution magic angle spinning NMR revealed conserved surface polysaccharides in Clostridium difficile, including a novel lipoteichoic acid structure. This method offers new insights into Gram-positive bacterial surface carbohydrate analysis.

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Area of Science:

  • Microbiology
  • Analytical Chemistry
  • Biochemistry

Background:

  • Clostridium difficile is a significant human pathogen.
  • Understanding its surface polysaccharides is crucial for developing new therapeutic strategies.
  • Previous studies have characterized some surface components, but a comprehensive survey was lacking.

Purpose of the Study:

  • To investigate the surface polysaccharide profiles of clinical and environmental Clostridium difficile isolates.
  • To characterize the structures of identified polysaccharides, including lipoteichoic acid (LTA).
  • To evaluate the utility of high-resolution magic angle spinning (HR-MAS) NMR for analyzing bacterial surface carbohydrates.

Main Methods:

  • Whole-cell HR-MAS NMR was used to survey surface polysaccharides.
  • Structural characterization involved isolation and analysis of polysaccharides using conventional NMR and mass spectrometry.
  • Comparative analysis was performed across multiple clinical and environmental strains.

Main Results:

  • A highly conserved surface polysaccharide profile was observed across all Clostridium difficile strains studied.
  • The conserved water-soluble polysaccharide, previously described, was confirmed.
  • A conserved lipoteichoic acid (LTA) was identified, with a novel structure containing a unique phosphodiester bridge and glyceric acid.

Conclusions:

  • HR-MAS NMR is a valuable tool for examining surface carbohydrates of Gram-positive bacteria.
  • Clostridium difficile possesses conserved surface polysaccharides, including a novel LTA structure.
  • These findings contribute to a deeper understanding of Clostridium difficile cell wall composition and potential targets.