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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Molecular cloning and characterization of two Helicobacter pylori genes coding for plasminogen-binding proteins
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Molecular cloning and characterization of two Helicobacter pylori genes coding for plasminogen-binding proteins

机译：编码纤溶酶原结合蛋白的两个幽门螺杆菌基因的分子克隆和鉴定

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摘要

Helicobacter pylori binds a number of host cell proteins, including the plasma protein plasminogen, which is the proenzyme of the serine protease plasmin. Two H. pylori plasminogen-binding proteins have been described; however, no genes were identified. Here we report the use of a phage display library to clone two genes from the H. pylori CCUG 17874 genome that mediate binding to plasminogen. DNA sequence analysis of one of these genes revealed 96.6% homology with H. pylori 26695 HP0508. A subsequent database search revealed that the amino acid sequence of a lysine-rich C-terminal segment of HP0508 is identical to the C terminus of HP0863. Recombinant proteins expressed from HP0508 and HP0863 bound plasminogen specifically and in a lysine-depen-dent manner. We designate these genes pgbA and pgbB, respectively. These proteins are expressed by a variety of H. pylori strains, have surface-exposed domains, and do not inhibit plasminogen activation. These results indicate tbat pgbA and pgbB may allow H. pylori to coat its exterior with plasminogen, which subsequently can be activated to plasmin. The surface acquisition of protease activity may enhance the virulence of H. pylori.
机译：幽门螺杆菌结合许多宿主细胞蛋白，包括血浆蛋白纤溶酶原，后者是丝氨酸蛋白酶纤溶酶的原酶。已经描述了两种幽门螺杆菌纤溶酶原结合蛋白。但是，没有发现基因。在这里，我们报告使用噬菌体展示库从幽门螺杆菌CCUG 17874基因组中克隆两个介导与纤溶酶原结合的基因。这些基因之一的DNA序列分析显示与幽门螺杆菌26695 HP0508有96.6％的同源性。随后的数据库搜索显示，HP0508的富含赖氨酸的C末端片段的氨基酸序列与HP0863的C末端相同。从HP0508和HP0863表达的重组蛋白以赖氨酸依赖性方式特异性结合纤溶酶原。我们分别指定这些基因pgbA和pgbB。这些蛋白质由多种幽门螺杆菌菌株表达，具有表面暴露的结构域，并且不抑制纤溶酶原激活。这些结果表明，tbat pgbA和pgbB可能使幽门螺杆菌用纤溶酶原包被其外部，随后可将其活化为纤溶酶。蛋白酶活性的表面获得可以增强幽门螺杆菌的毒力。

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