Aguilera Laura, Giménez Rosa, Badia Josefa, Aguilar Juan, Baldoma Laura
Department of Biochemistry and Molecular Biology, Institute of Biomedicine of the University of Barcelona (IBUB), Faculty of Pharmacy, University of Barcelona, Barcelona, Spain.
Int Microbiol. 2009 Sep;12(3):187-92.
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a multifunctional housekeeping protein reported to be a target of several covalent modifications in many organisms. In a previous study, enterohemorrhagic (EHEC) and enteropathogenic (EPEC) Escherichia coli strains were shown to secrete GAPDH and the protein to bind human plasminogen and fibrinogen. Here we report that GAPDH of these pathogens is ADP-ribosylated either in the cytoplasm or in the extracellular medium. GAPDH catalyzes its own modification, which involves Cys-149 at the active site. ADP-ribosylation of extracellular GAPDH may play an important role in the host-pathogen interaction, as also proposed in other pathogens.
甘油醛-3-磷酸脱氢酶（GAPDH）是一种多功能管家蛋白，据报道在许多生物体中是几种共价修饰的靶点。在先前的一项研究中，肠出血性大肠杆菌（EHEC）和肠致病性大肠杆菌（EPEC）菌株被证明会分泌GAPDH，且该蛋白能与人纤溶酶原和纤维蛋白原结合。在此我们报告，这些病原体的GAPDH在细胞质或细胞外培养基中会发生ADP-核糖基化。GAPDH催化自身的修饰，该修饰涉及活性位点的半胱氨酸-149。细胞外GAPDH的ADP-核糖基化可能在宿主-病原体相互作用中发挥重要作用，其他病原体也有类似的情况。
