Bioanalytical tools for the discovery of eukaryotic glycoproteins applied to the analysis of bacterial glycoproteins
Language English Country Great Britain, England Media print
Document type Journal Article, Research Support, Non-U.S. Gov't, Review
PubMed
19210128
DOI
10.1586/14789450.6.1.75
PII: 10.1586/14789450.6.1.75
Knihovny.cz E-resources
- MeSH
- Bacterial Proteins analysis MeSH
- Chemistry Techniques, Analytical methods MeSH
- Eukaryotic Cells metabolism MeSH
- Glycoproteins analysis MeSH
- Glycosylation MeSH
- Prokaryotic Cells metabolism MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Review MeSH
- Names of Substances
- Bacterial Proteins MeSH
- Glycoproteins MeSH
The commonly accepted theory that prokaryotes lack the ability to glycosylate their proteins has been disproved recently. The field of bacterial glycoprotein research is no longer considered novel owing to the rapid progress in analytical technologies and genome sequencing that has been made in the last few years. Enhanced interest in glycoprotein discovery in bacteria can be explained by a proven correlation between the presence of glycosylation and bacterial pathogenicity. Eukaryotic and prokaryotic organisms' features share certain similarities. However, with respect to inherent differences between these two distinct domains of life, the use of bioanalytical tools for glycoprotein analysis in eukaryotic systems often needs modification to be applied successfully to bacteria. In this article, we draw attention to the differences between eukaryotic and prokaryotic glycoproteins. We also focus on the main bottlenecks that may be encountered in the search for glycosylation in concrete bacterium and outline a possible work-flow for the exploration of glycoproteins in bacteria.
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