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Excreted Cytoplasmic Proteins Contribute to Pathogenicity in Staphylococcus aureus

机译:分泌的细胞质蛋白有助于金黄色葡萄球菌的致病性

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Excretion of cytoplasmic proteins in pro- and eukaryotes, also referred to as “nonclassical protein export,” is a well-known phenomenon. However, comparatively little is known about the role of the excreted proteins in relation to pathogenicity. Here, the impact of two excreted glycolytic enzymes, aldolase (FbaA) and glyceraldehyde-3-phosphate dehydrogenase (GAPDH), on pathogenicity was investigated in Staphylococcus aureus. Both enzymes bound to certain host matrix proteins and enhanced adherence of the bacterial cells to host cells but caused a decrease in host cell invasion. FbaA and GAPDH also bound to the cell surfaces of staphylococcal cells by interaction with the major autolysin, Atl, that is involved in host cell internalization. Surprisingly, FbaA showed high cytotoxicity to both MonoMac 6 (MM6) and HaCaT cells, while GAPDH was cytotoxic only for MM6 cells. Finally, the contribution of external FbaA and GAPDH to S. aureus pathogenicity was confirmed in an insect infection model.
机译:原核生物和真核生物中细胞质蛋白质的排泄,也称为“非经典蛋白质输出”,是众所周知的现象。但是,关于分泌蛋白与致病性的作用了解甚少。在这里,在金黄色葡萄球菌中研究了两种排泄的糖酵解酶醛缩酶(FbaA)和3磷酸甘油醛脱氢酶(GAPDH)对致病性的影响。两种酶均与某些宿主基质蛋白结合,并增强了细菌细胞对宿主细胞的粘附力,但导致宿主细胞入侵的减少。 FbaA和GAPDH还通过与主要自溶素Atl相互作用而结合到葡萄球菌细胞的细胞表面,后者参与宿主细胞的内在化。令人惊讶的是,FbaA对MonoMac 6(MM6)和HaCaT细胞均显示出高细胞毒性,而GAPDH仅对MM6细胞具有细胞毒性。最后,在昆虫感染模型中证实了外部FbaA和GAPDH对金黄色葡萄球菌致病性的贡献。

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