Enolase-like protein present on the outer membrane of Pseudomonas aeruginosa binds plasminogen
Ireneusz Ceremuga1, Ewa Seweryn, Iwona Bednarz-Misa
1Department of Medical Biochemistry, Wroclaw Medical University, Chalubinskiego 10, 50-368, Wroclaw, Poland, ireneusz.ceremuga@am.wroc.pl.
Abstract:
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.
Insights
Pseudomonas aeruginosa bacteria bind human plasminogen using an enolase-like protein on their cell surface. This binding aids bacterial invasion into host tissues, as confirmed by microscopy and immunoblotting assays.
Area of Science:
- Microbiology
- Molecular Biology
- Biochemistry
Background:
- * Pseudomonas aeruginosa is a pathogenic bacterium known to invade host tissues.
- * Bacterial invasion is often facilitated by interactions with host proteins like plasminogen (Plg).
- * The specific mechanisms of plasminogen binding by P. aeruginosa require further elucidation.
Purpose of the Study:
- * To confirm the binding affinity of P. aeruginosa to human plasminogen.
- * To identify the bacterial surface protein responsible for plasminogen binding.
- * To investigate the role of this protein in bacterial invasion.
Main Methods:
- * Confirmation of P. aeruginosa binding to human plasminogen.
- * Identification of the plasminogen-binding protein using cell wall analysis.
- * Electron microscopy to visualize protein localization on the bacterial cell surface.
- * Immunoblotting assays to examine plasminogen-binding activity.
Main Results:
- * P. aeruginosa demonstrated a significant binding affinity for human plasminogen.
- * An enolase-like protein was identified on the P. aeruginosa cell wall.
- * Electron microscopy supported the presence of alpha-enolase on the bacterial cell surface.
- * The identified enolase-like protein exhibited plasminogen-binding activity.
Conclusions:
- * P. aeruginosa utilizes an enolase-like protein, likely alpha-enolase, on its cell surface to bind human plasminogen.
- * This interaction is a key factor in P. aeruginosa's ability to invade host tissues.
- * Targeting this bacterial enolase-plasminogen interaction could offer novel therapeutic strategies against P. aeruginosa infections.
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