O-Aminoacylation of Bacterial Glycoconjugates: From Native Structure to Vaccine Design
Autor: | Katarzyna Dzierzba, Monika Gawlik-Jedrysiak, Małgorzata Mieszała, Katarzyna Zielinska-Kuzniarz, Wiesław Szeja, Tomasz Lipinski, Andrzej Gamian, Jadwiga Pietkiewicz |
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Rok vydání: | 2011 |
Předmět: |
Lipopolysaccharides
Models Molecular Glycoconjugate Glycine Pharmaceutical Science Aminoacylation Biology Gram-Positive Bacteria Epitope Microbiology chemistry.chemical_compound Drug Discovery Gram-Negative Bacteria Humans chemistry.chemical_classification Teichoic acid Molecular Structure Bacterial polysaccharide Esters biology.organism_classification chemistry Biochemistry Bacterial Vaccines Bacterial antigen Glycoconjugates Bacteria Biotechnology |
Zdroj: | Current Pharmaceutical Biotechnology. 12:1781-1791 |
ISSN: | 1389-2010 |
Popis: | The aminoacylation of bacterial polysaccharide antigens and its biological role are poorly understood, although it might be relevant in infection and immunity. Due to the lability of ester-linked substituents on glycoconjugate antigens, such groups usually escape detection during routine structural investigation. Of the few data available, those on the occurrence of glycine in the endotoxic lipopolysaccharides of Gram-negative bacteria are well documented. This article summarizes these data on glycine as an integral constituent of bacterial LPS and also some other amino-acid esters in the teichoic acids and phosphatidylglycerol of Gram-positive bacteria. The possible functions of such noncarbohydrate ester-linked substituents in bacterial antigens are discussed. Because glycine, an inherent component of bacterial lipopolysaccharides in the core region, is supposed to participate in epitope formation, such a structure may be considered for potential use in the construction of a vaccine with broad specificity. |
Databáze: | OpenAIRE |
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