Interaction of the salivary low-molecular-weight mucin (MG2) with Actinobacillus actinomycetemcomitans. 1996

J Groenink, and A J Ligtenberg, and E C Veerman, and J G Bolscher, and A V Nieuw Amerongen
Department of Oral Biochemistry, Academic Centre for Dentistry Amsterdam (ACTA), The Netherlands. J.Groenink.obc.acta@med.vu.nl

Periodontitis is associated with the presence of certain Gram-negative bacteria in the oral cavity, among these Actinobacillus actinomycetemcomitans. In order to determine which types of salivary components interact with A. actinomycetemcomitans two strains (HG 1175 and FDC Y4) were incubated with whole saliva and individual glandular secretions, viz. parotid, submandibular, and sublingual saliva. Immunochemical analysis by immunoblotting of bacteria-bound salivary proteins showed that IgA, the low-molecular mucin MG2, parotid agglutinin, and a 300 kDa sublingual and submandibular glycoprotein, were bound to the bacterial strains tested. In addition, adherence of A. actinomycetemcomitans to salivary proteins in a solid-phase was studied. After electrophoresis and transfer of salivary proteins to nitrocellulose membranes A. actinomycetemcomitans adhered only to MG2. In this assay periodate treatment, mild acid hydrolysis or neuraminidase digestion of the saliva glycoproteins abolished binding of two clinical isolates (HG 1175 and NY 664), suggesting that sialic acid residues on MG2 are involved in the binding. In contrast, adherence of the smooth laboratory strain Y4 was not affected by removal of sialic acid residues or even periodate treatment of MG2.

UI MeSH Term Description Entries
D009077 Mucins High molecular weight mucoproteins that protect the surface of EPITHELIAL CELLS by providing a barrier to particulate matter and microorganisms. Membrane-anchored mucins may have additional roles concerned with protein interactions at the cell surface. Mucin
D009439 Neuraminidase An enzyme that catalyzes the hydrolysis of alpha-2,3, alpha-2,6-, and alpha-2,8-glycosidic linkages (at a decreasing rate, respectively) of terminal sialic residues in oligosaccharides, glycoproteins, glycolipids, colominic acid, and synthetic substrate. (From Enzyme Nomenclature, 1992) Sialidase,Exo-alpha-Sialidase,N-Acylneuraminate Glycohydrolases,Oligosaccharide Sialidase,Exo alpha Sialidase,Glycohydrolases, N-Acylneuraminate,N Acylneuraminate Glycohydrolases,Sialidase, Oligosaccharide
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D004591 Electrophoresis, Polyacrylamide Gel Electrophoresis in which a polyacrylamide gel is used as the diffusion medium. Polyacrylamide Gel Electrophoresis,SDS-PAGE,Sodium Dodecyl Sulfate-PAGE,Gel Electrophoresis, Polyacrylamide,SDS PAGE,Sodium Dodecyl Sulfate PAGE,Sodium Dodecyl Sulfate-PAGEs
D006023 Glycoproteins Conjugated protein-carbohydrate compounds including MUCINS; mucoid, and AMYLOID glycoproteins. C-Glycosylated Proteins,Glycosylated Protein,Glycosylated Proteins,N-Glycosylated Proteins,O-Glycosylated Proteins,Glycoprotein,Neoglycoproteins,Protein, Glycosylated,Proteins, C-Glycosylated,Proteins, Glycosylated,Proteins, N-Glycosylated,Proteins, O-Glycosylated
D006090 Gram-Negative Bacteria Bacteria which lose crystal violet stain but are stained pink when treated by Gram's method. Gram Negative Bacteria
D000373 Agglutinins A substance that makes particles (such as bacteria or cells) stick together to form a clump or a mass. Agglutinin
D012469 Salivary Glands Glands that secrete SALIVA in the MOUTH. There are three pairs of salivary glands (PAROTID GLAND; SUBLINGUAL GLAND; SUBMANDIBULAR GLAND). Gland, Salivary,Glands, Salivary,Salivary Gland
D012471 Salivary Proteins and Peptides Proteins and peptides found in SALIVA and the SALIVARY GLANDS. Some salivary proteins such as ALPHA-AMYLASES are enzymes, but their composition varies in different individuals. Salivary Gland Protein,Salivary Gland Proteins,Salivary Peptide,Salivary Protein,Salivary Proteins,Salivary Peptides,Gland Protein, Salivary,Peptide, Salivary,Protein, Salivary,Protein, Salivary Gland
D015153 Blotting, Western Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes. Immunoblotting, Western,Western Blotting,Western Immunoblotting,Blot, Western,Immunoblot, Western,Western Blot,Western Immunoblot,Blots, Western,Blottings, Western,Immunoblots, Western,Immunoblottings, Western,Western Blots,Western Blottings,Western Immunoblots,Western Immunoblottings

Related Publications

J Groenink, and A J Ligtenberg, and E C Veerman, and J G Bolscher, and A V Nieuw Amerongen
May 1999, Journal of clinical periodontology,
J Groenink, and A J Ligtenberg, and E C Veerman, and J G Bolscher, and A V Nieuw Amerongen
November 1996, Journal of dental research,
J Groenink, and A J Ligtenberg, and E C Veerman, and J G Bolscher, and A V Nieuw Amerongen
December 2002, Journal of periodontal research,
J Groenink, and A J Ligtenberg, and E C Veerman, and J G Bolscher, and A V Nieuw Amerongen
January 1998, Microbiology and immunology,
J Groenink, and A J Ligtenberg, and E C Veerman, and J G Bolscher, and A V Nieuw Amerongen
February 1995, Oral microbiology and immunology,
J Groenink, and A J Ligtenberg, and E C Veerman, and J G Bolscher, and A V Nieuw Amerongen
December 2006, FEMS immunology and medical microbiology,
J Groenink, and A J Ligtenberg, and E C Veerman, and J G Bolscher, and A V Nieuw Amerongen
January 1993, Critical reviews in oral biology and medicine : an official publication of the American Association of Oral Biologists,
J Groenink, and A J Ligtenberg, and E C Veerman, and J G Bolscher, and A V Nieuw Amerongen
January 1991, Archives of oral biology,
J Groenink, and A J Ligtenberg, and E C Veerman, and J G Bolscher, and A V Nieuw Amerongen
January 2011, Annales Academiae Medicae Stetinensis,
J Groenink, and A J Ligtenberg, and E C Veerman, and J G Bolscher, and A V Nieuw Amerongen
January 1990, Archives of oral biology,
Copied contents to your clipboard!