肺炎链球菌对固定化纤连蛋白的黏附作用。
Adherence of Streptococcus pneumoniae to immobilized fibronectin.
作者信息
van der Flier M, Chhun N, Wizemann T M, Min J, McCarthy J B, Tuomanen E I
机构信息
Laboratory of Molecular Infectious Diseases, Rockefeller University, New York, New York 10021, USA.
出版信息
Infect Immun. 1995 Nov;63(11):4317-22. doi: 10.1128/iai.63.11.4317-4322.1995.
Abstract
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.
摘要
对细胞外基质蛋白（如纤连蛋白）的黏附为病原体提供了一种侵入受损上皮细胞的机制。已发现肺炎链球菌比其他链球菌和葡萄球菌更强烈地黏附于固定化的纤连蛋白。结合呈剂量、时间和温度依赖性。用胰蛋白酶处理细菌会导致结合减少，这表明细菌黏附成分是一种蛋白质。比较了通过蛋白水解或重组基因片段表达产生的纤连蛋白片段与肺炎链球菌结合以及竞争细菌与固定化纤连蛋白结合的能力。来自羧基末端肝素结合域的片段始终具有活性，这表明该区域包含肺炎链球菌结合位点，该区域与支持大多数其他细菌附着的区域不同。
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