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首页> 外文期刊>Molecular Microbiology >THE DIPEPTIDE REPEAT REGION OF THE FIBRINOGEN-BINDING PROTEIN (CLUMPING FACTOR) IS REQUIRED FOR FUNCTIONAL EXPRESSION OF THE FIBRINOGEN-BINDING DOMAIN ON THE STAPHYLOCOCCUS AUREUS CELL SURFACE
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THE DIPEPTIDE REPEAT REGION OF THE FIBRINOGEN-BINDING PROTEIN (CLUMPING FACTOR) IS REQUIRED FOR FUNCTIONAL EXPRESSION OF THE FIBRINOGEN-BINDING DOMAIN ON THE STAPHYLOCOCCUS AUREUS CELL SURFACE

机译：纤维蛋白原结合蛋白（凝聚因子）的双重复区需要在金黄色葡萄球菌细胞表面上功能性表达纤维蛋白原结合域

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Clumping factor of Staphylococcus aureus is a fibrinogen-binding protein that is located on the bacterial cell surface. The protein has an unusual repeat domain (region R) comprising mainly the dipeptide aspartate and serine. To determine if region R has a role in the surface display of the fibrinogen-binding region A domain, deletions lacking the region R encoding region of the clfA gene were generated. To determine the minimum length of region R required for wild-type levels of ClfA expression, variants with truncated region R domains were constructed. S. aureus cells expressing mutated clfA genes were tested for (i) proteins released by lysostaphin treatment that reacted with antisera specific for region A, (ii) clumping in soluble fibrinogen, (iii) adherence to immobilized fibrinogen and (iv) expression of the ClfA antigen on the cell surface by fluorescent activated cell sorting analysis. Each construct expressed three major immunoreactive proteins, two of which were putative N-terminal degradation products. Region R residues greater than 40 were required between region A and W (72 residues between region A and the LPDTG sorting signal) for wild-type levels of clumping in fibrinogen. A stepwise decrease in clumping titre was observed as the distance between region A and LPDTG was decreased from 72 to 4 residues. Similarly, a decrease in binding of anti-ClfA serum and in binding to fibrinogen-coated plastic surfaces was observed with cells expressing ClfA with 40 region R residues or less. Nevertheless, low levels of adherence to fibrinogen and binding to anti-ClfA serum occurred with ClfA derivatives that lacked region R altogether. This indicates that a small proportion of the ClfA molecules are linked to peptidoglycan very close to the cell surface but that residues greater than 72 are needed to allow sufficient ClfA molecules to span the entire cell wall and to display the biologically active A domain in a form that can participate fully in fibrinogen binding. [References: 37]
机译：金黄色葡萄球菌的聚集因子是纤维蛋白原结合蛋白，位于细菌细胞表面。该蛋白质具有不寻常的重复结构域（R区），主要包含二肽天冬氨酸和丝氨酸。为了确定区域R是否在纤维蛋白原结合区域A结构域的表面展示中起作用，产生了缺少clfA基因的区域R编码区域的缺失。为了确定野生型水平的ClfA表达所需的区域R的最小长度，构建了具有截短的区域R结构域的变体。测试表达突变的clfA基因的金黄色葡萄球菌细胞（i）溶葡萄球菌素处理释放的蛋白，该蛋白与A区特异的抗血清反应，（ii）聚集在可溶性纤维蛋白原中，（iii）粘附于固定的纤维蛋白原和（iv）表达通过荧光激活细胞分选分析细胞表面的ClfA抗原。每个构建体表达三种主要的免疫反应蛋白，其中两种是推定的N末端降解产物。 A和W区之间需要大于40的R区残基（A区和LPDTG分类信号之间存在72个残基），以实现纤维蛋白原聚集的野生型聚集。随着区域A和LPDTG之间的距离从72个残基减少到4个残基，观察到了成团滴度的逐步降低。类似地，用表达具有40个或更小的R区域残基的ClfA的细胞，观察到抗ClfA血清的结合和与纤维蛋白原包被的塑料表面的结合减少。然而，完全缺乏R区的ClfA衍生物发生了对纤维蛋白原的低水平粘附和与抗ClfA血清的结合。这表明一小部分ClfA分子与非常靠近细胞表面的肽聚糖相连，但是需要大于72的残基才能使足够的ClfA分子跨越整个细胞壁并以某种形式展示生物活性A结构域可以完全参与纤维蛋白原的结合。 [参考：37]

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