Glycan-binding specificities of Streptococcus mutans and Streptococcus sobrinus lectin-like adhesins
- نوع فایل : کتاب
- زبان : انگلیسی
- مؤلف : Viviane Schüler & Adrian Lussi & Andreas Kage & Rainer Seemann
- چاپ و سال / کشور: 2011
Description
Since the adhesion of bacteria to the tooth surface is a prerequisite for dental plaque and subsequent caries development, a promising caries preventive strategy could be to block the lectin–glycan-mediated adherence of cariogenic bacteria. The aim of the study was to evaluate potential differences in glycan-binding specificities of two Streptococcus mutans strains (DSM 20523 and DSM 6178) and Streptococcus sobrinus (DSM 20381). A competitive enzyme-linked lectin-binding assay was used to identify the binding specificities of isolated bacterial surface lectins. Blotting of the microbial proteins on neoglycoprotein-coated PVP membranes enabled a qualitative protein analysis of all specific bacterial lectins. Different glycan-binding sites could be identified for the S. mutans strains in comparison to S. sobrinus. An earlier reported glycan-binding specificity for terminal galactose residues could be confirmed for the S. mutans strains. For the S. sobrinus strain, more than one glycan-binding specificity could be found (oligomannose and terminal sialyl residues). Each of the tested strains showed more than one surface lectin responsible for the specific lectin-binding with varying molecular weight (S. mutans, 90/155 kDa and S. sobrinus, 35/45 kDa). The established experimental setup could be used as future standard procedure for the identification of bacterial lectinderived binding specificities. The findings from this study might serve as basis for the design of an individual ‘glycan cocktail’ for the competitive inhibition of lectin-mediated adhesion of mutans streptococci to oral surfaces
Clin Oral Invest DOI 10.1007/s00784-011-0568-1 Received: 6 December 2010 / Accepted: 13 May 2011
