Role of Streptococcus gordonii amylase-binding protein A in adhesion to hydroxyapatite, starch metabolism, and biofilm formation.
Role of Streptococcus gordonii amylase-binding protein A in adhesion to hydroxyapatite, starch metabolism, and biofilm formation.
复制标题
戈登链球菌淀粉酶结合蛋白 A 在羟基磷灰石粘附、淀粉代谢和生物膜形成中的作用。
DOI:
10.1128/iai.69.11.7046-7056.2001
复制
发表时间:
2001
影响因子:
3.1
通讯作者:
Scannapieco,FA
中科院分区:
文献类型:
--
作者:
Rogers,JD;PalmerJr,RJ;Kolenbrander,PE;Scannapieco,FA
Interactions between bacteria and salivary components are thought to be important in the establishment and ecology of the oral microflora. α-Amylase, the predominant salivary enzyme in humans, binds toStreptococcus 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 theabpAgene ofS. gordoniistrains Challis and FAS4 by allelic exchange, resulting inabpAmutant 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 theabpAmutant strains grew much more poorly and produced relatively small microcolonies. Taken together, these results suggest that AbpA ofS. gordoniifunctions as an adhesin to amylase-coated hydroxyapatite, in salivary-amylase-mediated catabolism of dietary starches and in human saliva-supported biofilm formation byS. gordonii.