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Identification and characterization of a Mycoplasma synoviae 55,000-molecular-weight antigen associated with
M A Morsy1, V S Panangala, P C Hu
1Department of Pathobiology, College of Veterinary Medicine, Auburn University, Alabama 36849-5516.
Abstract:
Serological studies have shown that some antigenic determinants are conserved among several pathogenic Mycoplasma species, including Mycoplasma pneumoniae, M. genitalium, and M. gallisepticum. M. synoviae, an avian pathogen that shares certain morphological and biological features with the above-mentioned mycoplasmas, was examined by the protein immunoblot procedure for its reactivity with hyperimmune rabbit antiserum specific for the major (190,000 molecular-weight [MW]) adhesion P1 protein of M. pneumoniae. A single polypeptide of M. synoviae of approximately 55,000 MW was recognized by the anti-P1 antiserum. The 55,000-MW antigen was electroeluted following electrophoretic separation of M. synoviae polypeptides, and the eluted protein was used for immunization of mice for the production of monoclonal antibodies (MAbs) and polyclonal antiserum. Immunoelectron microscopy with MAbs and gold-conjugated secondary antibodies showed that the 55,000-MW antigen was located at the cell surface and was more densely clustered around the bleb-like protuberance of the cell. Immuno-affinity-purified 55,000-MW antigen, as well as the antibodies produced against it, blocked the hemagglutination by M. synoviae.
Insights
Researchers identified a conserved 55,000 MW cell surface antigen in Mycoplasma synoviae, an avian pathogen. This antigen, recognized by antibodies against Mycoplasma pneumoniae P1 protein, plays a role in hemagglutination.
Area of Science:
- Microbiology
- Immunology
- Veterinary Science
Background:
- Pathogenic Mycoplasma species share conserved antigenic determinants.
- Mycoplasma synoviae is an avian pathogen with similarities to human Mycoplasma pathogens.
Purpose of the Study:
- To investigate antigenic similarities between Mycoplasma synoviae and other pathogenic Mycoplasma species.
- To characterize a potential cell surface antigen in M. synoviae.
Main Methods:
- Protein immunoblot using anti-P1 antiserum from Mycoplasma pneumoniae.
- Electrophoretic separation and electroelution of M. synoviae polypeptides.
- Production of monoclonal antibodies (MAbs) and polyclonal antiserum against the M. synoviae antigen.
- Immunoelectron microscopy to determine antigen localization.
- Hemagglutination inhibition assays.
Main Results:
- A 55,000 MW polypeptide from M. synoviae reacted with anti-P1 antiserum.
- The 55,000 MW antigen was localized to the cell surface, particularly around protuberances.
- The purified 55,000 MW antigen and antibodies against it inhibited M. synoviae hemagglutination.
Conclusions:
- M. synoviae possesses a 55,000 MW cell surface antigen antigenically related to the M. pneumoniae P1 protein.
- This antigen is involved in the hemagglutination activity of M. synoviae.
- The findings suggest conserved surface structures among pathogenic Mycoplasma species.