Interaction of the salivary low-molecular-weight mucin (MG2) with Actinobacillus actinomycetemcomitans |
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Authors: | J Groenink A J M Ligtenberg E C I Veerman J G M Bolscher A V Nieuw Amerongen |
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Institution: | (1) Department of Oral Biochemistry, Academic Centre for Dentistry Amsterdam (ACTA), Amsterdam, the Netherlands |
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Abstract: | 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.Abbreviations S-IgA
Secretory IgA
- MG1
high-molecular-weight mucin
- MG2
low-molecular-weight mucin
- EP-GP
extra parotid-glycoprotein
- PRPs
proline-rich proteins
- SNA
Sambucus nigra agglutinin
- MAA
Maackia amurensis agglutinin
- PNA
peanut agglutinin
- UEA
Ulex europaeus agglutinin |
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Keywords: | Actinobacillus actinomycetemcomitans adherence mucins periodontitis saliva sialic acid |
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