A Lithium Chloride-Extracted, Broad-Spectrum-Adhesive 42-Kilodalton Protein of Staphylococcus epidermidis Is Ornithine Carbamoyltransferase

To identify novel putative staphylococcal adhesins, lithium chloride extraction (an established method for selective surface molecule solubilization) was employed. N-terminal sequencing and functional assays identified a 42-kDa fibronectin-binding protein from Staphylococcus epidermidis as ornithine carbamoyltransferase (OCTase). However, OCTase was not recognizable extracellularly, and this fact together with the fact that LiCl induced DNA release and a decrease in viability suggests that LiCl extraction may not be the method of choice for selective surface molecule extraction from staphylococci.

为鉴定新型潜在葡萄球菌黏附素，本研究采用氯化锂萃取法——一种已被广泛认可的选择性表面分子溶解方法。通过N端测序与功能实验，我们从表皮葡萄球菌（Staphylococcus epidermidis）中鉴定出一种分子量为42 kDa的纤连蛋白结合蛋白，经确认其为鸟氨酸氨甲酰转移酶（ornithine carbamoyltransferase, OCTase）。然而，该蛋白并未在细胞外被检出；结合氯化锂可诱导DNA释放并降低细胞存活率这一现象，提示氯化锂萃取法或许并非葡萄球菌表面分子选择性萃取的首选方法。