Interactions of surface-displayed glycolytic enzymes of Mycoplasma pneumoniae with components of the human extracellular matrix.
Mycoplasma pneumoniae is a major cause of community-acquired respiratory infections worldwide. Due to the strongly reduced genome, the number of virulence factors expressed by this cell wall-less pathogen is limited. To further understand the processes during host colonization, we investigated the interactions of the previously confirmed surface-located glycolytic enzymes of M. pneumoniae (pyruvate dehydrogenase A-C [PdhA-C], glyceraldehyde-3-phosphate dehydrogenase [GapA], lactate dehydrogenase [Ldh], phosphoglycerate mutase [Pgm], pyruvate kinase [Pyk] and transketolase [Tkt]) to the human extracellular matrix (ECM) proteins fibrinogen (Fn), fibronectin (Fc), lactoferrin (Lf), laminin (Ln) and vitronectin (Vc), respectively. Concentration-dependent interactions between Fn and Vc and all eight recombinant proteins derived from glycolytic enzymes, between Ln and PdhB-C, GapA, Ldh, Pgm, Pyk and Tkt, between Lf and PdhA-C, GapA and Pyk, and between Fc and PdhC and GapA were demonstrated. In most cases, these associations are significantly influenced by ionic forces and by polyclonal sera against recombinant proteins. In immunoblotting, the complex of human plasminogen, activator (tissue-type or urokinase plasminogen activator) and glycolytic enzyme was not able to degrade Fc, Lf and Ln, respectively. In contrast, degradation of Vc was confirmed in the presence of all eight enzymes tested. Our data suggest that the multifaceted associations of surface-localized glycolytic enzymes play a potential role in the adhesion and invasion processes during infection of human respiratory mucosa by M. pneumoniae.
Technische Universität Dresden, Medizinische Fakultät Carl Gustav Carus, Institut für Medizinische Mikrobiologie und Hygiene, Fetscherstrasse 74, 01307 Dresden, Germany.
Anne
A
Gründel
Technische Universität Dresden, Medizinische Fakultät Carl Gustav Carus, Institut für Medizinische Mikrobiologie und Hygiene, Fetscherstrasse 74, 01307 Dresden, Germany.
Enno
E
Jacobs
Technische Universität Dresden, Medizinische Fakultät Carl Gustav Carus, Institut für Medizinische Mikrobiologie und Hygiene, Fetscherstrasse 74, 01307 Dresden, Germany. Electronic address: roger.dumke@tu-dresden.de.
Roger
R
Dumke
D001426:Bacterial Proteins / Q000378:metabolism*; D004798:Enzymes / Q000378:metabolism*; D016326:Extracellular Matrix Proteins / Q000378:metabolism*; D054884:Host-Pathogen Interactions; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism*; D009177:Mycoplasma pneumoniae / Q000201:enzymology*; D011485:Protein Binding; D025941:Protein Interaction Mapping
D001426:Bacterial Proteins; D004798:Enzymes; D016326:Extracellular Matrix Proteins; D008565:Membrane Proteins
Host-pathogen interaction; Human extracellular matrix protein; Mycoplasma pneumoniae; Surface-displayed glycolytic enzyme