ArticleBMC veterinary research2014
Mycoplasma synoviae enolase is a plasminogen/fibronectin binding protein.
Article in BMC veterinary research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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34 citing papers in PubMed, 63 citations in OpenAlex.
- When less is more: cell size reduction as a metabolic lifeline inFrontiers in microbiology · 2026Article
- The chaperone GrpE mediates adhesion in Mycoplasma bovis and interactions with host extracellular matrix components and plasminogen.Veterinary research · 2025Article
- Indirect ELISA developed to detect antibodies against Mycoplasma synoviae P50 protein via immunoproteomic screening.Applied microbiology and biotechnology · 2025Article
- Mycoplasma synoviae elongation factor thermo stable is an adhesion-associated protein that enters cells by endocytosis and stimulates DF-1 cell proliferation.BMC veterinary research · 2024Article
- Research Progress in the Development of Vaccines against MycoplasmaMicroorganisms · 2024Article
- Identification of plasminogen-binding sites inFrontiers in cellular and infection microbiology · 2024Article
- Target antigen screening and development of a multi-component subunit vaccine againstFrontiers in cellular and infection microbiology · 2024Article
- Screening of immunogenic proteins and evaluation of vaccine candidates against Mycoplasma synoviae.NPJ vaccines · 2023Article
- Hijacking of Host Plasminogen byMicrobiology spectrum · 2023Article
- Article
- Evaluation of the protective efficacy of six major immunogenic proteins ofFrontiers in veterinary science · 2023Article
- NADH oxidase of Mycoplasma synoviae is a potential diagnostic antigen, plasminogen/fibronectin binding protein and a putative adhesin.BMC veterinary research · 2022Article
- Host cell interactions of novel antigenic membrane proteins of Mycoplasma agalactiae.BMC microbiology · 2022Article
- A multifunctional enolase mediates cytoadhesion and interaction with host plasminogen and fibronectin in Mycoplasma hyorhinis.Veterinary research · 2022Article
- Review
- Comparative Genomics ofFrontiers in veterinary science · 2021Article
- Binding of Plasminogen toFrontiers in microbiology · 2021Article
- Evidence for the Rapid and Divergent Evolution of Mycoplasmas: Structural and Phylogenetic Analysis of Enolases.Frontiers in molecular biosciences · 2021Article
- Mycoplasma hyorhinis as a possible cause of fibrinopurulent meningitis in pigs? - a case series.Porcine health management · 2020Article
- Structural Insights into the Interactions of Candidal Enolase with Human Vitronectin, Fibronectin and Plasminogen.International journal of molecular sciences · 2020Article
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Authors and funding
10 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundMycoplasma 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.
resultsWe 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.
conclusionThese 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.
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