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首页> 外文期刊>Infection and immunity >Identification of a salivary agglutinin-binding domain within cell surface adhesin P1 of Streptococcus mutans.
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Identification of a salivary agglutinin-binding domain within cell surface adhesin P1 of Streptococcus mutans.

机译：变形链球菌细胞表面粘附素P1中唾液凝集素结合结构域的鉴定。

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DNA encoding the alanine-rich region (A-region) of the cell surface adhesin, P1, from Streptococcus mutans was subcloned and expressed as a fusion protein with the maltose-binding protein (MBP) of Escherichia coli. The A-region fusion protein was shown to competitively inhibit both adherence of S. mutans to salivary agglutinin-coated hydroxyapatite and fluid-phase agglutinin-mediated aggregation of this organism. MBP alone or an MBP-paramyosin fusion protein was not inhibitory. Proteolytic cleavage of the fusion protein into its component moieties, MBP and A-region, resulted in breakdown of the A-region into three main fragments. Western immunoblot analysis of calcium-dependent agglutinin binding to this preparation revealed binding specificity for a 28-kDa fragment. Thus, the A-region of P1 is an important domain which interacts directly with salivary agglutinin, and this interaction interferes with both the aggregation and the adherence mechanisms in vitro.
机译：将来自变形链球菌的编码细胞表面粘附素P1的富含丙氨酸的区域（A区域）的DNA亚克隆，并表达为与大肠杆菌的麦芽糖结合蛋白（MBP）融合的蛋白。已显示A区融合蛋白竞争性抑制变形链球菌对唾液凝集素包被的羟基磷灰石的粘附和该生物体的液相凝集素介导的聚集。单独的MBP或MBP-副肌球蛋白融合蛋白无抑制作用。融合蛋白的蛋白水解切割成其组成部分MBP和A区，导致A区分解成三个主要片段。钙依赖性凝集素与该制剂结合的蛋白质免疫印迹分析显示了对28 kDa片段的结合特异性。因此，P1的A区是一个重要的域，直接与唾液凝集素相互作用，并且这种相互作用在体外会干扰聚集和粘附机制。

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