ArticlePloS one2012
α-Enolase, an adhesion-related factor of Mycoplasma bovis.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed, 93 citations in OpenAlex.
- FtsZ contributes to cytoadhesion and interaction with host extracellular matrix components and plasminogen in Mycoplasma bovis.Veterinary research · 2025Article
- The chaperone GrpE mediates adhesion in Mycoplasma bovis and interactions with host extracellular matrix components and plasminogen.Veterinary research · 2025Article
- Identification of a heparin-binding protein encoded byJournal of bacteriology · 2025Article
- Enolase AmEno15, a Promising Candidate for Understanding the Infectious Process ofInternational journal of molecular sciences · 2025Article
- ENO1 fromBiomolecules · 2025Article
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- Integrated Information for Pathogenicity and Treatment of Spiroplasma.Current microbiology · 2024Review
- Target antigen screening and development of a multi-component subunit vaccine againstFrontiers in cellular and infection microbiology · 2024Article
- LppA is a novel plasminogen receptor of Mycoplasma bovis that contributes to adhesion by binding the host extracellular matrix and Annexin A2.Veterinary research · 2023Article
- NADH oxidase of Mycoplasma synoviae is a potential diagnostic antigen, plasminogen/fibronectin binding protein and a putative adhesin.BMC veterinary research · 2022Article
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- A multifunctional enolase mediates cytoadhesion and interaction with host plasminogen and fibronectin in Mycoplasma hyorhinis.Veterinary research · 2022Article
- Annexin A2 regulatesFrontiers in immunology · 2022Article
- Review
- TheFrontiers in microbiology · 2022Review
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- AApplied and environmental microbiology · 2021Article
- Immune Evasion ofPathogens (Basel, Switzerland) · 2021Review
- Evidence for the Rapid and Divergent Evolution of Mycoplasmas: Structural and Phylogenetic Analysis of Enolases.Frontiers in molecular biosciences · 2021Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mycoplasma bovis is the causative agent of Mycoplasma bovis-associated disease (MbAD). Although the mechanisms underlying M. bovis adherence to host cells is not clear, recent studies have shown that the cell surface protein α-enolase facilitates bacterial invasion and dissemination in the infected host. In this study, we cloned, expressed and purified recombinant M. bovis α-enolase and induced polyclonal anti-α-enolase antibodies in rabbits. M. bovis α-enolase was detected in the cytoplasmic and membrane protein fractions by these antibodies. Triple immunofluorescence labeling combined with confocal laser scanning microscopy (CLSM) revealed that the plasminogen (Plg) enhanced the adherence of M. bovis to embryonic bovine lung (EBL) cells; the values obtained for adherence and inhibition are consistent with this finding. Interestingly, we found that trace amounts of trypsin acted as a more effective enhancer of cell adherence than Plg. Hence, our data indicate that surface-associated M. bovis α-enolase is an adhesion-related factor of M. bovis that contributes to adherence by binding Plg.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.