Ceremuga Ireneusz, Seweryn Ewa, Bednarz-Misa Iwona, Pietkiewicz Jadwiga, Jermakow Katarzyna, Banaś Teresa, Gamian Andrzej
Department of Medical Biochemistry, Wroclaw Medical University, Chalubinskiego 10, 50-368, Wroclaw, Poland,
Folia Microbiol (Praha). 2014 Sep;59(5):391-7. doi: 10.1007/s12223-014-0311-9. Epub 2014 Mar 27.
Pseudomonas aeruginosa is one of the pathogenic bacteria which utilize binding of the host plasminogen (Plg) to promote their invasion throughout the host tissues. In the present study, we confirmed that P. aeruginosa exhibits binding affinity for human plasminogen. Furthermore, we showed that the protein detected on the cell wall of P. aeruginosa and binding human plasminogen is an enolase-like protein. The hypothesis that alpha-enolase, a cytoplasmatic glycolytic enzyme, resides also on the cell surface of the bacterium was supported by electron microscopy analysis. The plasminogen-binding activity of bacterial cell wall outer membrane enolase-like protein was examined by immunoblotting assay.
铜绿假单胞菌是一种致病细菌，它利用宿主纤溶酶原（Plg）的结合来促进其在整个宿主组织中的侵袭。在本研究中，我们证实铜绿假单胞菌对人纤溶酶原具有结合亲和力。此外，我们表明在铜绿假单胞菌细胞壁上检测到的与人纤溶酶原结合的蛋白质是一种烯醇化酶样蛋白。电子显微镜分析支持了细胞质糖酵解酶α-烯醇化酶也存在于细菌细胞表面的假说。通过免疫印迹分析检测了细菌细胞壁外膜烯醇化酶样蛋白的纤溶酶原结合活性。
