title: Glycosylation of the Arg-gingipains of Porphyromonas gingivalis and comparison with glycoconjugate structure and synthesis in other bacteria.
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.
authors.affiliation: MRC Molecular Pathogenesis Group, Centre for Infectious Disease, Institute of Cell and Molecular Sciences, Barts & The London, Queen Mary-s School of Medicine and Dentistry, 32 Newark Street, London E1 2AA, UK. a.gallagher@qmul.ac.uk
authors.forename: Alexandra
authors.initials: A
authors.lastname: Gallagher
authors.forename: Joseph
authors.initials: J
authors.lastname: Aduse-Opoku
authors.forename: Minnie
authors.initials: M
authors.lastname: Rangarajan
authors.forename: Jennifer M
authors.initials: JM
authors.lastname: Slaney
authors.forename: Michael A
authors.initials: MA
authors.lastname: Curtis
mesh_terms: D018829:Adhesins, Bacterial; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D003546:Cysteine Endopeptidases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D000080867:Gingipain Cysteine Endopeptidases; D006023:Glycoproteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D006031:Glycosylation; D006388:Hemagglutinins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D016966:Porphyromonas gingivalis / Q000737:chemistry* / Q000201:enzymology* / Q000378:metabolism; D011499:Protein Processing, Post-Translational
chemical_list: D018829:Adhesins, Bacterial; D001426:Bacterial Proteins; D000080867:Gingipain Cysteine Endopeptidases; D006023:Glycoproteins; D006388:Hemagglutinins; D003546:Cysteine Endopeptidases