IsdA of Staphylococcus aureus is a broad spectrum, iron-regulated adhesin
IsdA of Staphylococcus aureus is a broad spectrum, iron-regulated adhesin
复制标题
DOI：
10.1111/j.1365-2958.2003.03938.x
复制
发表时间：
2004-03-01
影响因子：
3.6
通讯作者：
Foster, SJ
中科院分区：
文献类型：
--
作者：
Clarke, SR;Wiltshire, MD;Foster, SJ
作为宿主-病原体相互作用的一个重要方面，金黄色葡萄球菌具有通过一系列表面蛋白粘附于人细胞外基质（ECM）组分的能力。在这里，我们已经表明，IsdA具有广谱配体结合活性，包括纤维蛋白原和纤连蛋白。映射研究揭示了一个独特的结构域负责配体结合。该结构域存在于S.金黄色葡萄球菌和其他革兰氏阳性生物。isdA基因仅在Fur控制下的铁限制条件下表达，而不在标准实验室培养基中表达。这种情况在体外和感染期间发生在血清中。全细胞结合和凝集试验表明，当细菌在铁限制条件下生长时，IsdA构成与纤维蛋白原和纤连蛋白两者生理相关的粘附素。对于S。在金黄色葡萄球菌中，铁是宿主环境的重要标志物，细菌通过其粘附策略的至少一种元素的差异调节来响应宿主环境。
As an important facet of host-pathogen interaction, Staphylococcus aureus has the ability to adhere to human extracellular matrix (ECM) components via a range of surface proteins. Here we have shown that IsdA has broad-spectrum ligand-binding activity, including fibrinogen and fibronectin. Mapping studies revealed a distinct domain responsible for ligand binding. This domain is present in a number of iron-regulated proteins of S. aureus and in other Gram-positive organisms. The isdA gene is only expressed in iron-limited conditions under the control of Fur and not in standard laboratory media. Such conditions occur in serum in vitro and during infection. Whole cell binding and clumping assays revealed that when the bacteria are grown under iron-limited conditions, IsdA constitutes a physiologically relevant adhesin to both fibrinogen and fibronectin. Thus for S. aureus, iron is an important marker for the host environment, to which the bacterium responds by differential regulation of at least one element of its adhesive strategy.