Mycoplasma synoviae enolase is a plasminogen/fibronectin binding protein

Area of Science:

• Veterinary Microbiology
• Avian Pathology
• Molecular Biology

Background:

• Mycoplasma synoviae causes significant economic losses in poultry due to respiratory infections and arthritis.
• The role of enolase, a known virulence factor in other pathogens, in M. synoviae remains uncharacterized.

Purpose of the Study:

• To investigate the enzymatic activity, immunogenicity, and host-binding properties of Mycoplasma synoviae enolase.
• To assess the potential of M. synoviae enolase as a target for immune-based interventions.

Main Methods:

• Amplification and expression of the M. synoviae enolase gene (eno) in E. coli.
• Enzymatic activity assays, Western blot, immuno-electron microscopy, and binding assays with chicken plasminogen (Plg) and human fibronectin (Fn).
• Complement-dependent mycoplasmacidal assays and adherence inhibition assays using anti-enolase serum.

Main Results:

• Recombinant M. synoviae enolase (rMsEno) demonstrated catalytic activity in converting 2-phosphoglycerate to phosphoenolpyruvate.
• Enolase was localized to the surface and cytoplasm of M. synoviae cells.
• rMsEno bound to chicken Plg and human Fn, and antibodies against rMsEno exhibited mycoplasmacidal activity and inhibited M. synoviae adherence.

Conclusions:

• M. synoviae enolase possesses significant enzymatic and binding activities, interacting with host proteins Plg and Fn.
• The surface localization and immunogenicity of M. synoviae enolase suggest its involvement in M. synoviae pathogenesis.
• Anti-enolase antibodies demonstrate therapeutic potential by inducing mycoplasmacidal effects and inhibiting bacterial adherence.