Statherin and histatin 1 reduce parotid saliva-promoted Streptococcus mutans strain MT8148 adhesion to hydroxyapatite surfaces
Statherin and histatin 1 reduce parotid saliva-promoted Streptococcus mutans strain MT8148 adhesion to hydroxyapatite surfaces
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DOI：
10.1159/000094286
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发表时间：
2006-01-01
期刊：
影响因子：
4.2
通讯作者：
Takaesu, Y.
中科院分区：
文献类型：
--
作者：
Shimotoyodome, A.;Kobayashi, H.;Takaesu, Y.
小唾液磷蛋白-成纤维细胞生成素（ST）和组蛋白1（HT 1）-被发现在获得性釉质表膜，调节变形链球菌粘附到牙釉质。然而，他们在S.变形菌在牙釉质表面上的粘附性仍然不确定。本研究的目的是探讨ST和HT 1是否以及如何影响（i）S。变形链球菌粘附和（ii）S.在体外，变形杆菌粘附促进唾液蛋白到羟基磷灰石（HA）上。我们通过吸附HA和进一步通过凝胶过滤色谱分离人腮腺唾液。[H-3]标记的S.高分子量糖蛋白组分（HMWGP）显著促进变形杆菌菌株MT 8148在烧结的HA板上的粘附（> 10倍），但纯化的ST或HT 1不促进。更有趣的是，S.通过向HMWGP中加入纯化的ST或HT 1，可显著降低HMWGP对HA的变形菌粘附。[H-3]标记S. HA上的变形杆菌粘附与[C-14]-标记的HMWGP在HA上的吸附呈正相关，这也通过加入纯化的ST和HT 1而降低。与ST和HT 1对应的合成肽减少腮腺唾液促进的S。变形粘附然而，ST和HT 1 N端结构域的负电荷的去除降低了它们对S.腮腺唾液促进变形菌粘附。我们得出结论，ST和HT 1竞争性抑制唾液HMWGP的吸附，从而减少S。变形杆菌粘附到HA表面上。版权所有（c）2006 S. Karger AG，巴塞尔。
Small salivary phosphoproteins - statherin (ST) and histatin 1 (HT1) - are found in the acquired enamel pellicle which modulates Streptococcus mutans adhesion onto dental enamel. However, their roles in S. mutans adhesion onto enamel surfaces are still undefined. The aim of this study was to investigate whether and how ST and HT1 affect (i) S. mutans adhesion and (ii) the adsorption of S. mutans adhesion-promoting salivary proteins onto hydroxyapatite (HA) in vitro. We fractionated human parotid saliva by adsorption to HA and further by gel filtration chromatography. Adhesion of [H-3]-labeled S. mutans strain MT8148 onto sintered HA plates was promoted significantly (> 10-fold) by high-molecular weight glycoprotein fraction (HMWGP), but not by purified ST or HT1. More interestingly, promotion of S. mutans adhesion onto HA by HMWGP was significantly reduced by adding purified ST or HT1 to HMWGP. [H-3]-labeled S. mutans adhesion on HA was positively correlated to the [C-14]-labeled HMWGP adsorption onto HA, which was also reduced by the addition of purified ST and HT1. Synthetic peptides corresponding to ST and HT1 reduced the parotid saliva-promoted S. mutans adhesion. However, removal of the negative charges in the N-terminal domains of ST and HT1 diminished their inhibitory effects on S. mutans adhesion promoted by parotid saliva. We conclude that ST and HT1 competitively inhibit the adsorption of salivary HMWGP, and thereby reduce S. mutans adhesion onto HA surfaces. Copyright (c) 2006 S. Karger AG, Basel.