期刊
CLINICAL ORAL INVESTIGATIONS
卷 16, 期 3, 页码 789-796出版社
SPRINGER HEIDELBERG
DOI: 10.1007/s00784-011-0568-1
关键词
Dental caries; Streptococcus mutans; Streptococcus sobrinus; Lectin-like adhesins; Glycan pattern
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 strains (DSM 20523 and DSM 6178) and (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 strains in comparison to . An earlier reported glycan-binding specificity for terminal galactose residues could be confirmed for the strains. For the 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 (, 90/155 kDa and , 35/45 kDa). The established experimental setup could be used as future standard procedure for the identification of bacterial lectin-derived 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.
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