Subunits of the Pyruvate Dehydrogenase Cluster of Mycoplasma pneumoniae Are Surface-Displayed Proteins that Bind and Activate Human Plasminogen

摘要: The dual role of glycolytic enzymes in cytosol-located metabolic processes and cell surface-mediated functions with an influence on virulence is described for various micro-organisms. Cell wall-less bacteria the class Mollicutes including common human pathogen Mycoplasma pneumoniae possess a reduced genome limiting repertoire factors pathways. After initial contact cells respiratory epithelium via specialized complex adhesins release cell-damaging factors, surface-displayed may facilitate further interaction between host microbe. In this study, we detection four subunits pyruvate dehydrogenase (PDHA-D) among cytosolic membrane-associated proteins M. pneumoniae. Subunits PDH were cloned, expressed purified to produce specific polyclonal guinea pig antisera. Using colony blotting, fractionation total immunofluorescence experiments, surface localization PDHA-C was demonstrated. All recombinant are able bind HeLa plasminogen. These interactions can be specifically blocked by corresponding addition, ionic PDHC-binding plasminogen as well lysine residues association PDHA-D confirmed. PDHB subunit shown activate PDHB-plasminogen induces degradation fibrinogen. Hence, our data indicate that surface-associated might play pathogenesis infections