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The Mycoplasma gallisepticum α-enolase is cell surface-exposed and mediates adherence by binding to chicken

Hongjun Chen1, Shengqing Yu, Xinyue Shen

  • 1Shanghai Veterinary Research Institute, The Chinese Academy of Agricultural Sciences, 518 Ziyue Road, Shanghai 200241, PR China.

Microbial Pathogenesis
|June 14, 2011
PubMed

Insights

Mycoplasma gallisepticum alpha-enolase acts as an adhesin, facilitating bacterial attachment to chicken cells. This finding, confirmed through various assays, reveals a key virulence factor for this pathogen.

Area of Science:

  • Microbiology
  • Bacterial Pathogenesis
  • Protein Function

Background:

  • Alpha-enolase is a known adhesin in other pathogenic bacteria.
  • The function of alpha-enolase in Mycoplasma gallisepticum adhesion was previously uncharacterized.

Purpose of the Study:

  • To investigate the role of alpha-enolase in Mycoplasma gallisepticum adhesion to host cells.
  • To characterize the biochemical and immunological properties of M. gallisepticum alpha-enolase.

Main Methods:

  • Heterologous expression of mutated M. gallisepticum alpha-enolase in E. coli.
  • Protein purification and activity assays (NADH to NAD+ conversion).
  • Antibody generation, immunoblotting, immunofluorescence, ELISA, and adherence inhibition assays.

Main Results:

  • Recombinant M. gallisepticum alpha-enolase (rMGEno) was successfully expressed and purified, retaining enzymatic activity.
  • Alpha-enolase was localized to the surface of M. gallisepticum cells.
  • rMGEno binds chicken plasminogen, and antibodies against alpha-enolase significantly inhibit bacterial adhesion to chicken fibroblasts (DF-1 cells).

Conclusions:

  • Mycoplasma gallisepticum alpha-enolase functions as a surface adhesin.
  • Alpha-enolase contributes to the adhesion of M. gallisepticum to chicken host cells, likely through plasminogen binding.

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