Abstract
Post-translational modification of proteins by covalent attachment of sugars to the protein backbone (protein glycosylation) is the most common post-translational modification in the eucaryotic cell. However, the addition of carbohydrates to proteins of Eubacteria and Archaea has been demonstrated and accepted only recently. There is now a rapidly expanding list of bacterial glycoproteins that have been characterised from a variety of different organisms including many important pathogens. The Arg-gingipains of Porphyromonas gingivalis are recent additions to this list. In this review we present a summary of our investigations on the structure of the glycan additions to these proteolytic enzymes, the genetics of the glycosylation process and some of the effects on enzyme function and recognition. These findings are placed in the context of the current status of understanding of glycoconjugate structure and synthesis in other bacteria. Given the importance of glycosylation of eucaryotic proteins to their stability, structure, resistance to proteolysis and recognition, the modifications to the proteases described in the present report are likely to have a functional role in the properties of these enzymes in periodontal disease.
Keywords: porphyromonas gingivalis, proteases, bacteria, protein glycosylation, surface glycan polymer
Current Protein & Peptide Science
Title: Glycosylation of the Arg-gingipains of Porphyromonas gingivalis and Comparison with Glycoconjugate Structure and Synthesis in other Bacteria
Volume: 4 Issue: 6
Author(s): Alexandra Gallagher, Joseph Aduse-Opoku, Minnie Rangarajan, Jennifer M. Slaney and Michael A. Curtis
Affiliation:
Keywords: porphyromonas gingivalis, proteases, bacteria, protein glycosylation, surface glycan polymer
Abstract: Post-translational modification of proteins by covalent attachment of sugars to the protein backbone (protein glycosylation) is the most common post-translational modification in the eucaryotic cell. However, the addition of carbohydrates to proteins of Eubacteria and Archaea has been demonstrated and accepted only recently. There is now a rapidly expanding list of bacterial glycoproteins that have been characterised from a variety of different organisms including many important pathogens. The Arg-gingipains of Porphyromonas gingivalis are recent additions to this list. In this review we present a summary of our investigations on the structure of the glycan additions to these proteolytic enzymes, the genetics of the glycosylation process and some of the effects on enzyme function and recognition. These findings are placed in the context of the current status of understanding of glycoconjugate structure and synthesis in other bacteria. Given the importance of glycosylation of eucaryotic proteins to their stability, structure, resistance to proteolysis and recognition, the modifications to the proteases described in the present report are likely to have a functional role in the properties of these enzymes in periodontal disease.
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Cite this article as:
Gallagher Alexandra, Aduse-Opoku Joseph, Rangarajan Minnie, Slaney M. Jennifer and Curtis A. Michael, Glycosylation of the Arg-gingipains of Porphyromonas gingivalis and Comparison with Glycoconjugate Structure and Synthesis in other Bacteria, Current Protein & Peptide Science 2003; 4 (6) . https://dx.doi.org/10.2174/1389203033486974
DOI https://dx.doi.org/10.2174/1389203033486974 |
Print ISSN 1389-2037 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5550 |
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