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Background   Mycoplasma synoviae  is an avian pathogen that can lead to respiratory tract infections and arthritis in chickens and turkeys, resulting in serious economic losses to the poultry industry. Enolase reportedly plays important roles in several bacterial pathogens, but its role in  M. synoviae  has not been established. Therefore, in this study, the enolase encoding gene ( eno ) of  M. synoviae  was amplified from strain WVU1853 and expressed in  E. coli  BL21 cells. Then the enzymatic activity, immunogenicity and binding activity with chicken plasminogen (Plg) and human fibronectin (Fn) was evaluated.    Results  We demonstrated that the recombinant  M. synoviae  enolase protein (rMsEno) can catalyze the conversion of 2-phosphoglycerate (2-PGA) to phosphoenolpyruvate (PEP), the Km and Vmax values of rMsEno were 1.1 × 10 −3  M and 0.739 μmol/L/min, respectively. Western blot and immuno-electron microscopy analyses confirmed that enolase was distributed on the surface and within the cytoplasm of  M. synoviae  cells. The binding assays demonstrated that rMsEno was able to bind to chicken Plg and human Fn proteins. A complement-dependent mycoplasmacidal assay demonstrated that rabbit anti–rMsEno serum had distinct mycoplasmacidal efficacy in the presence of complement, which also confirmed that enolase was distributed on the surface of  M. synoviae . An inhibition assay showed that the adherence of  M. synoviae  to DF-1 cells pre-treated with Plg could be effectively inhibited by treatment with rabbit anti-rMsEno serum.    Conclusion  These results reveal that  M. synoviae  enolase has good catalytic activity for conversion of 2-PGA to PEP, and binding activity with chicken Plg and human Fn. Rabbit anti–rMsEno serum displayed an obvious complement-dependent mycoplasmacidal effect and adherent inhibition effect. These results suggested that the  M. synoviae  enolase plays an important role in  M. synoviae  metabolism, and could potentially impact  M. synoviae  infection and immunity.    Electronic supplementary material  The online version of this article (doi:10.1186/s12917-014-0223-6) contains supplementary material, which is available to authorized users.

Mycoplasma synoviaeenolase is a plasminogen/fibronectin binding protein