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Development of new method for the eradication of etiological organism of dental caries using bovine milk containing antibodies against virulence factors of the organism and the adherence-inhibiting component.

开发利用含有针对微生物毒力因子的抗体和粘附抑制成分的牛奶来根除龋齿病原微生物的新方法。

基本信息

批准号：
13672158
负责人：
OHO Takahiko
金额：
$ 2.3万
依托单位：
Kyushu University
依托单位国家：
日本
项目类别：
Grant-in-Aid for Scientific Research (C)
财政年份：
2001
资助国家：
日本
起止时间：
2001 至 2002
项目状态：
已结题

来源：
https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-13672158/
关键词：
Dental caries Streptococcus mutans Adherence Bovine milk Lactoferrin

项目摘要

Bovine milk inhibits the saliva-induced aggregation of S. mutans. In this study, the milk component that possesses inhibitory activity against this aggregation was isolated and found to be lactoferrin. Surface plasmon resonance analysis indicated that bovine lactoferrin binds more strongly to salivary agglutinin than to recombinant PAc. To identify the saliva-binding region of bovine lactoferrin, 11 truncated bovine lactoferrin fragments were constructed. A fragment corresponding to the C-terminal half of the lactoferrin molecule had a strong inhibitory effect on the saliva-induced aggregation of S. mutans, whereas a fragment corresponding to the N-terminal half had a weak inhibitory effect. Seven shorter fragments corresponding to lactoferrin residues 473 to 538 also showed a high ability to inhibit the aggregation of S. mutans. These results suggest that residues 473 to 538 of bovine lactoferrin are important in the inhibition of saliva-induced aggregation of S. mutans.Next, the effect of bovine milk lactoferrin on S. mutans adherence to a salivary film was investigated. Bovine lactoferrin molecule and relatively long lactoferrin fragments containing residues 473-538 strongly inhibited S. mutans adherence to saliva-coated hydroxyapatite beads. Each cysteine residue in Lf411 (residues 473-538) was substituted by a serine residue, and the mutants Lf411-C481S and Lf411-C532S strongly inhibited S. mutans adherence. These results suggest that the functional domain of lactoferrin that binds to a salivary film lies in residues 473-538, and that the region might be concealed by disulfied bond formation between Cys481 and Cys532 in the Lf411 fragment.

牛乳抑制唾液诱导的S.变异人在这项研究中，具有抑制活性的牛奶成分，对这种聚集被分离出来，并发现是乳铁蛋白。表面等离子体共振分析表明，牛乳铁蛋白结合更强烈的唾液凝集素比重组PAc。为了鉴定牛乳铁蛋白的唾液结合区域，构建了11个截短的牛乳铁蛋白片段。对应于乳铁蛋白分子的C-末端一半的片段对唾液诱导的S.而对应于N-末端一半的片段具有弱的抑制作用。对应于乳铁蛋白残基473至538的七个较短片段也显示出高的抑制S.变异人这些结果表明，牛乳铁蛋白的残基473至538在抑制唾液诱导的S.接下来，研究牛乳铁蛋白对S. mutans的影响。研究了变形菌对唾液膜的粘附。牛乳铁蛋白分子和含有473 - 538残基的较长乳铁蛋白片段强烈抑制S。变形菌粘附在唾液涂层的羟基磷灰石珠上。突变体Lf411-C481S和Lf411-C532S对S.变形菌粘附。这些结果表明，结合唾液膜的乳铁蛋白的功能结构域位于残基473 - 538，并且该区域可能被Lf411片段中Cys481和Cys532之间的二硫键形成所隐藏。