The role of the Map protein in Staphylococcus aureus matrix protein and eukaryotic cell adherence
The role of the Map protein in Staphylococcus aureus matrix protein and eukaryotic cell adherence
复制标题
DOI：
10.1078/1438-4221-00212
复制
发表时间：
2002-09-01
影响因子：
4.1
通讯作者：
Podbielski, A
中科院分区：
文献类型：
--
作者：
Kreikemeyer, B;McDevitt, D;Podbielski, A
金黄色葡萄球菌Map蛋白被认为是一种多功能粘附素。使用地图（-）突变体，补充菌株和重组地图，我们证明地图是不是一个传统的粘附素，并不参与结合可溶性细胞外基质（ECM）蛋白和葡萄球菌粘附固定ECM蛋白。然而，地图提供了一个基板的葡萄球菌细胞的有效和物种特异性的粘附。这种相互作用是剂量依赖性的，并被特异性抗Map抗体抑制。根据配体印迹，82和50 kDa的两个葡萄球菌表面蛋白的功能地图受体。与野生型和补充菌株相比，突变体对上皮细胞的粘附性降低了80%。然而，坚持并没有遵循类似的高内化率。总之，地图可以作为一个内源性的粘附基板的塑料表面和真核细胞通过相互作用与葡萄球菌表面粘附。
The Staphylococcus aureus Map protein was proposed to act as a multifunctional adhesin. Using a map(-) mutant, a complemented strain and recombinant Map, we demonstrated that Map was not a conventional adhesin and was not involved in binding soluble extracellular matrix (ECM) proteins and in staphylococcal adherence to immobilized ECM proteins. However, Map provided a substrate for efficient and species-specific adherence of staphylococcal cells. This interaction was dose-dependent and was inhibited by specific anti-Map antibodies. According to ligand blots, two staphylococcal surface proteins of 82 and 50 kDa appeared to function as Map receptors. Adherence of the mutant to epithelial cells was reduced by 80% as compared to wild-type and complemented strains. However, adherence was not followed by a similar high rate of internalization. In conclusion, Map can function as an endogenous adhesion substrate in the attachment to plastic surfaces and eukaryotic cells via interaction with staphylococcal surface adhesins.