STRUCTURE OF THE CELL-WALL ANCHOR OF SURFACE-PROTEINS IN STAPHYLOCOCCUS-AUREUS
STRUCTURE OF THE CELL-WALL ANCHOR OF SURFACE-PROTEINS IN STAPHYLOCOCCUS-AUREUS
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DOI：
10.1126/science.7701329
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发表时间：
1995-04-07
期刊：
影响因子：
56.9
通讯作者：
FAULL, KF
中科院分区：
文献类型：
--
作者：
SCHNEEWIND, O;FOWLER, A;FAULL, KF
许多表面蛋白锚定在革兰氏阳性菌的细胞壁上，并参与这些生物体的发病机制。设计了一种杂合分子，当在金黄色葡萄球菌中表达时，该杂合分子锚定在细胞壁上，并且可以通过受控的酶消化释放。通过分子生物学和质谱技术的结合，研究了S.金黄色葡萄球菌被发现。在保守的LPXTG基序的苏氨酸和甘氨酸之间的表面蛋白裂解后，苏氨酸的羧基与葡萄球菌细胞壁中的五甘氨酸交联桥的游离氨基酰胺连接。
Many surface proteins are anchored to the cell wall of Gram-positive bacteria and are involved in the pathogenesis of these organisms. A hybrid molecule was designed that, when expressed in Staphylococcus aureus, was anchored to the cell wall and could be released by controlled enzymatic digestion. By a combination of molecular biology and mass spectrometry techniques, the structure of the cell wall anchor of surface proteins in S. aureus was revealed. After cleavage of surface proteins between threonine and glycine of the conserved LPXTG motif, the carboxyl of threonine is amide-linked to the free amino group of the pentaglycine crossbridge in the staphylococcal cell wall.