Binding of plasma fibronectin to Candida albicans occurs through the cell binding domain.
Binding of plasma fibronectin to Candida albicans occurs through the cell binding domain.
复制标题
血浆纤连蛋白与白色念珠菌的结合通过细胞结合域发生。
作者：
Christopher Penn;S. A. Klotz
白色念珠菌酵母细胞通过位于细胞表面的糖蛋白受体（粘附素）与可溶性人血浆纤维连接蛋白（Fn）结合。这项工作表明，包含细胞结合域的Fn蛋白水解片段比亲本Fn分子更能与酵母细胞粘附素结合。未检测到含有Fn的肝素和明胶结合结构域的Fn片段的结合。120 kDa片段的结合可被含有氨基酸序列精氨酸-甘氨酸-天冬氨酸（RGD）的单克隆抗体和含有约23-mer RGD的Fn肽抑制，但不与肝素或GRGDSPL结合。可溶性Fn的细胞结合结构域比亲本分子更容易结合，这一事实可能解释了可溶性Fn和固定化Fn与念珠菌相互作用的差异。这是可能的，在固定后，Fn可能暴露分子的结构域以前未暴露时，分子处于可溶性状态。
Candida albicans yeast cells bind soluble human plasma fibronectin (Fn) through a glycoprotein receptor (adhesin) located on the cell surface. This work demonstrates that a 120 kDa proteolytic fragment of Fn encompassing the cell binding domain binds more avidly to the yeast cell adhesin than does the parent Fn molecule. The presence of binding of Fn fragments containing heparin- and gelatin-binding domains of Fn could not be detected. The binding of the 120 kDa fragment is inhibited by a monoclonal antibody to the cell binding domain containing the amino acid sequence, Arginine-Glycine-Aspartic acid (RGD) as well as by an RGD-containing approximately 23-mer Fn peptide, but not with heparin or GRGDSPL. The fact that the cell binding domain of soluble Fn binds more avidly than does the parent molecule may explain the difference in the interaction of soluble Fn and immobilized Fn with Candida. It is possible that, upon immobilization, Fn may expose domains of the molecule previously unexposed when the molecule is in the soluble state.