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Adherence of Streptococcus pneumoniae to immobilized fibronectin.

机译:肺炎链球菌对固定化纤连蛋白的粘附。

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Adherence to extracellular matrix proteins, such as fibronectin, affords pathogens with a mechanism to invade injured epithelia. Streptococcus pneumoniae was found to adhere to immobilized fibronectin more avidly than other streptococci and staphylococci do. Binding was dose, time, and temperature dependent. Trypsin treatment of the bacteria resulted in decreased binding, suggesting that the bacterial adhesive component was a protein. Fragments of fibronectin generated by proteolysis or by expression of recombinant gene segments were compared for the ability to bind pneumococci and to compete against bacterial binding to immobilized fibronectin. Fragments from the carboxy-terminal heparin binding domain were consistently active, suggesting that this region contains the pneumococcal binding site, a region distinct from that supporting the attachment of most other bacteria.
机译:对细胞外基质蛋白(如纤连蛋白)的粘附为病原体提供了入侵受损上皮的机制。发现肺炎链球菌比其他链球菌和葡萄球菌更强烈地粘附于固定的纤连蛋白。结合是剂量,时间和温度依赖性的。用胰蛋白酶处理细菌会导致结合减少,这表明细菌粘附成分是蛋白质。比较通过蛋白水解或通过表达重组基因片段产生的纤连蛋白片段的结合肺炎球菌和竞争细菌与固定纤连蛋白结合的能力。羧基末端肝素结合结构域的片段始终具有活性,表明该区域包含肺炎球菌结合位点,该区域不同于支持大多数其他细菌附着的区域。

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