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.
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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
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发表时间:
2001
影响因子:
3.1
通讯作者:
Scannapieco,FA
Scannapieco,FA
中科院分区:
医学2区
文献类型:
--
作者:
Rogers,JD;PalmerJr,RJ;Kolenbrander,PE;Scannapieco,FA

文献摘要

相似文献

细菌和唾液组分之间的相互作用被认为在口腔微生物菌群的建立和生态学中是重要的。α-淀粉酶是人类唾液中最主要的酶,它与戈登链球菌(Streptococcus gordonii)结合,戈登链球菌是牙齿的主要定植者。以前的研究表明,这种相互作用与细菌对唾液膜的粘附、膳食淀粉的分解和生物膜的形成有关。淀粉酶结合至少部分由淀粉酶结合蛋白A(AbpA)介导。为了研究该蛋白的功能,我们将红霉素抗性决定簇[λ(AM)]插入到S. gordonii菌株查利斯和FAS 4通过等位基因交换,产生abpA突变株Challis-E1和FAS 4-E1。野生型和突变株的比较没有发现任何显着差异的菌落形态,生化代谢谱,在复杂或确定的媒体,表面疏水性,或共聚集特性的增长。粘附等温线的Scatchard分析表明,野生型菌株粘附更好的人腮腺唾液和淀粉酶包被的羟基磷灰石比AbpA突变体。与此相反,突变菌株绑定到整个唾液包被的羟基磷灰石在更大程度上比野生型菌株。虽然野生型菌株与纯化的唾液淀粉酶预孵育生长良好,在确定的培养基中与马铃薯淀粉作为唯一的碳水化合物来源,在相同的条件下,即使在预孵育后,与淀粉酶的AbpA突变体不生长。此外,野生型菌株在流动细胞生物膜模型中产生大的小菌落,而abpA突变菌株生长更差,产生相对小的小菌落。综上所述,这些结果表明,AbpA ofS。gordonii作为淀粉酶包被的羟基磷灰石的粘附素,在唾液淀粉酶介导的膳食淀粉的催化作用中以及在人唾液支持的S. gordonii。
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.