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首页> 外文期刊>Infection and immunity >Identification and Characterization of a Nonimmunoglobulin Factor in Human Saliva That Inhibits Streptococcus mutans Glucosyltransferase
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Identification and Characterization of a Nonimmunoglobulin Factor in Human Saliva That Inhibits Streptococcus mutans Glucosyltransferase

机译：鉴定和表征人唾液中的一种非免疫球蛋白因子，可抑制变形链球菌葡萄糖基转移酶

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Saliva contains an array of nonimmunoglobulin defense factors which are thought to contribute to the protection of the hard and soft tissue surfaces of the oral cavity by modulating microbial colonization and metabolism. Here we report the discovery of a putative innate defense factor in human saliva that inhibits the glucosyltransferase (GTF) of Streptococcus mutans, a virulence enzyme involved in oral colonization by this pathogen. The GTF-inhibiting factor (GIF) was initially identified as a nonimmunoglobulin salivary component that interfered with detection of antibodies to the glucan-binding region (GLU) of GTF by an enzyme-linked immunosorbent assay. This inhibitory activity was present in whole saliva and submandibular-sublingual saliva, but it was essentially absent from parotid saliva. GIF inhibited the recognition of S. mutans cell surface-associated GTF by specific antibodies but had no effect on antibodies to other cell surface antigens, suggesting that GIF specifically binds to GTF on S. mutans. GIF purified by size exclusion or affinity chromatography was used for biochemical and functional characterization. Analysis of GIF by sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed a high-molecular-weight glycoprotein after staining with Coomassie blue or Schiff's reagent. Heating and reduction with 2-mercaptoethanol of GIF resulted in the release of a ～58-kDa protein that was identified as α-amylase by Western blotting using anti-α-amylase antibodies. GLU bound blotted α-amylase, suggesting that the latter molecule is the GLU-binding component of the GIF complex. The ability of GTF to synthesize extracellular glucans was inhibited by GIF but not by uncomplexed α-amylase or an unrelated high-molecular-weight glycoprotein. In conclusion, our findings demonstrate that in human saliva, there is a high-molecular-weight glycoprotein-α-amylase complex which is capable of inhibiting GTF and may contribute to control of S. mutans colonization in the oral cavity.
机译：唾液含有一系列非免疫球蛋白防御因子，据认为可通过调节微生物定植和代谢来帮助保护口腔的硬组织和软组织表面。在这里，我们报道了在人类唾液中发现一种潜在的先天防御因子的发现，该因子可抑制变形链球菌（em）的糖基转移酶（GTF），变形链球菌是一种由该病原体参与口腔定殖的毒力酶。 GTF抑制因子（GIF）最初被鉴定为非免疫球蛋白唾液成分，通过酶联免疫吸附测定干扰了针对GTF的葡聚糖结合区（GLU）抗体的检测。这种抑制活性存在于整个唾液和颌下舌下唾液中，但腮腺唾液中基本上没有。 GIF抑制了对 S的识别。突变体通过特定抗体与细胞表面相关的GTF，但对其他细胞表面抗原的抗体没有影响，表明GIF与 S上的GTF特异性结合。通过尺寸排阻或亲和层析纯化的GIF用于生化和功能表征。通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳对GIF进行分析，结果显示，用考马斯亮蓝或席夫氏试剂染色后，分子量较高的糖蛋白较高。加热并用GIF的2-巯基乙醇还原导致释放出约58 kDa的蛋白质，该蛋白质经抗α-淀粉酶抗体的Western印迹鉴定为α-淀粉酶。 GLU结合印迹的α-淀粉酶，表明后者是GIF复合物的GLU结合成分。 GIF抑制GTF合成细胞外葡聚糖的能力，但不受复合的α-淀粉酶或无关的高分子糖蛋白抑制。总之，我们的发现表明，在人类唾液中，存在一种高分子量糖蛋白-α-淀粉酶复合物，该复合物能够抑制GTF，并可能有助于控制 S。变形菌在口腔中定植。

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