Tyrosine72 Residue at the Bottom of Rim Domain in LukF Crucial for the Sequential Binding of the Staphylococcal γ-Hemolysin to Human Erythrocytes
Tyrosine72 Residue at the Bottom of Rim Domain in LukF Crucial for the Sequential Binding of the Staphylococcal γ-Hemolysin to Human Erythrocytes
复制标题
LukF 中 Rim 结构域底部的酪氨酸 72 残基对于葡萄球菌 γ-溶血素与人红细胞的顺序结合至关重要
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发表时间：
2000
期刊：
影响因子：
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通讯作者：
Y. Kamio
中科院分区：
文献类型：
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作者：
Kenji Yokota;Y. Kamio
葡萄球菌双组分细胞毒素，杀白细胞素（Luk）、潘通-瓦朗丁杀白细胞素（PVL）和γ-溶血素（Hlg）分别由LukF和LukS、LukF- pv和LukS- pv、LukF和Hlg2组成，Luk和Hlg共享LukF。尽管LukF- pv与LukF在氨基酸序列上有73%的同源性，在三维结构上也非常相似，但它们不能代替LukF代替Hlg。在这里，我们证明了LukF-PV与Hlg2合作缺乏溶血活性是由于LukF-PV与人红细胞结合失败。我们发现LukF边缘结构域底部的Y72残基是其结合的关键残基，这是Hlg2随后与人红细胞结合的先决条件。所获得的数据表明，LukF- pv突变体的T71残基被LukF的相应残基Y72取代，使LukF- pv具有与人红细胞的结合能力，并且在Hlg2存在下具有溶血活性。
Staphylococcal bi-component cytotoxins, leukocidin (Luk), Panton-Valentine leukocidin (PVL), and γ-hemolysin (Hlg) consist of LukF and LukS, LukF-PV and LukS-PV, and LukF and Hlg2, respectively, and Luk and Hlg share LukF. LukF-PV can not substitute for LukF for Hlg, despite 73% identity in amino acid sequence and close similarity in the 3-dimensional structure between them. Here, we demonstrated that the absence of hemolytic activity of LukF-PV in cooperation with Hlg2 is due to the failure of the binding of LukF-PV to human erythrocytes. We identified Y72 residue at the bottom of rim domain in LukF as the crucial residue for its binding, which is a prerequisite to the subsequent binding of Hlg2 to human erythrocytes. The data obtained showed that a mutant of LukF-PV in which T71 residue was replaced by the corresponding residue of LukF, Y72, endowed LukF-PV with the binding capability to human erythrocytes which was accompanied by its hemolytic activity in the presence of Hlg2.