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Taking the starch out of oral biofilm formation: molecular basis and functional significance of salivary ?-amylase binding to oral streptococci.

ABSTRACT: ?-Amylase-binding streptococci (ABS) are a heterogeneous group of commensal oral bacterial species that comprise a significant proportion of dental plaque microfloras. Salivary ?-amylase, one of the most abundant proteins in human saliva, binds to the surface of these bacteria via specific surface-exposed ?-amylase-binding proteins. The functional significance of ?-amylase-binding proteins in oral colonization by streptococci is important for understanding how salivary components influence oral biofilm formation by these important dental plaque species. This review summarizes the results of an extensive series of studies that have sought to define the molecular basis for ?-amylase binding to the surface of the bacterium as well as the biological significance of this phenomenon in dental plaque biofilm formation.

SUBMITTER: Nikitkova AE

PROVIDER: S-EPMC3553756 | biostudies-literature | 2013 Jan

REPOSITORIES: biostudies-literature

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Taking the starch out of oral biofilm formation: molecular basis and functional significance of salivary α-amylase binding to oral streptococci.

Nikitkova Anna E AE Haase Elaine M EM Scannapieco Frank A FA

Applied and environmental microbiology 20121109 2

α-Amylase-binding streptococci (ABS) are a heterogeneous group of commensal oral bacterial species that comprise a significant proportion of dental plaque microfloras. Salivary α-amylase, one of the most abundant proteins in human saliva, binds to the surface of these bacteria via specific surface-exposed α-amylase-binding proteins. The functional significance of α-amylase-binding proteins in oral colonization by streptococci is important for understanding how salivary components influence oral ...[more]

PMID: 23144140

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Salivary Amylase-Responsive Buccal Tablets Wipe Out Chemotherapy-Rooted Refractory Oral Mucositis.

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Human saliva modifies growth, biofilm architecture and competitive behaviors of oral streptococci

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2023-08-22 | GSE239483 | GEO

Dynamics of the Streptococcus gordonii Transcriptome in Response to Medium, Salivary α-Amylase, and Starch.

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Human Saliva Modifies Growth, Biofilm Architecture and Competitive Behaviors of Oral Streptococci.

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Project description:In the current study, we determined whether increased digestion of starch by high salivary amylase concentrations predicted postprandial blood glucose following starch ingestion. Healthy, nonobese individuals were prescreened for salivary amylase activity and classified as high (HA) or low amylase (LA) if their activity levels per minute fell 1 SD higher or lower than the group mean, respectively. Fasting HA (n = 7) and LA (n = 7) individuals participated in 2 sessions during which they ingested either a starch (experimental) or glucose solution (control) on separate days. Blood samples were collected before, during, and after the participants drank each solution. The samples were analyzed for plasma glucose and insulin concentrations as well as diploid AMY1 gene copy number. HA individuals had significantly more AMY1 gene copies within their genomes than did the LA individuals. We found that following starch ingestion, HA individuals had significantly lower postprandial blood glucose concentrations at 45, 60, and 75 min, as well as significantly lower AUC and peak blood glucose concentrations than the LA individuals. Plasma insulin concentrations in the HA group were significantly higher than baseline early in the testing session, whereas insulin concentrations in the LA group did not increase at this time. Following ingestion of the glucose solution, however, blood glucose and insulin concentrations did not differ between the groups. These observations are interpreted to suggest that HA individuals may be better adapted to ingest starches, whereas LA individuals may be at greater risk for insulin resistance and diabetes if chronically ingesting starch-rich diets.

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1,2,3-Triazole-based inhibitors of Porphyromonas gingivalis adherence to oral streptococci and biofilm formation.

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| S-EPMC5119859 | biostudies-literature

Role of Streptococcus gordonii amylase-binding protein A in adhesion to hydroxyapatite, starch metabolism, and biofilm formation.

Project description:Interactions between bacteria and salivary components are thought to be important in the establishment and ecology of the oral microflora. alpha-Amylase, the predominant salivary enzyme in humans, binds to Streptococcus gordonii, a primary colonizer of the tooth. Previous studies have implicated this interaction in adhesion of the bacteria to salivary pellicles, catabolism of dietary starches, and biofilm formation. Amylase binding is mediated at least in part by the amylase-binding protein A (AbpA). To study the function of this protein, an erythromycin resistance determinant [erm(AM)] was inserted within the abpA gene of S. gordonii strains Challis and FAS4 by allelic exchange, resulting in abpA mutant strains Challis-E1 and FAS4-E1. Comparison of the wild-type and mutant strains did not reveal any significant differences in colony morphology, biochemical metabolic profiles, growth in complex or defined media, surface hydrophobicity, or coaggregation properties. Scatchard analysis of adhesion isotherms demonstrated that the wild-type strains adhered better to human parotid-saliva- and amylase-coated hydroxyapatite than did the AbpA mutants. In contrast, the mutant strains bound to whole-saliva-coated hydroxyapatite to a greater extent than did the wild-type strains. While the wild-type strains preincubated with purified salivary amylase grew well in defined medium with potato starch as the sole carbohydrate source, the AbpA mutants did not grow under the same conditions even after preincubation with amylase. In addition, the wild-type strain produced large microcolonies in a flow cell biofilm model, while the abpA mutant strains grew much more poorly and produced relatively small microcolonies. Taken together, these results suggest that AbpA of S. gordonii functions as an adhesin to amylase-coated hydroxyapatite, in salivary-amylase-mediated catabolism of dietary starches and in human saliva-supported biofilm formation by S. gordonii.

| S-EPMC100085 | biostudies-literature

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