Antigenic variation of Mycoplasma gallisepticum, as detected by use of monoclonal antibodies

Victor S. Panangala From the Department of Pathobiology, College of Veterinary Medicine (Panangala, Morsy, Gresham, Tiovio-Kinnucan) and Alabama Agricultural Experiment Station (Panangala), Auburn University, AL 36849-5516.

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Mohamad A. Morsy From the Department of Pathobiology, College of Veterinary Medicine (Panangala, Morsy, Gresham, Tiovio-Kinnucan) and Alabama Agricultural Experiment Station (Panangala), Auburn University, AL 36849-5516.

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Martha M. Gresham From the Department of Pathobiology, College of Veterinary Medicine (Panangala, Morsy, Gresham, Tiovio-Kinnucan) and Alabama Agricultural Experiment Station (Panangala), Auburn University, AL 36849-5516.

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Maria Toivio-Kinnucan From the Department of Pathobiology, College of Veterinary Medicine (Panangala, Morsy, Gresham, Tiovio-Kinnucan) and Alabama Agricultural Experiment Station (Panangala), Auburn University, AL 36849-5516.

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Summary

A panel of monoclonal antibodies (MAb) developed against Mycoplasma gallisepticum strain PG31 was used to probe the antigenic profiles of 5 recognized strains (PG31, R, S6, F, A5969) and 6 field isolates of M gallisepticum. Monoclonal antibody G9 predominantly recognized antigens at apparent molecular mass positions of 90 to 98 kDA. The MAb reacted with all strains and isolates, but the molecular mass position of the antigens varied among some mycoplasmas. Monoclonal antibody G12 reacted with all strains and isolates of M gallisepticum and had an identical banding pattern. However, MAb G10 and G11 reacted selectively only with a limited number of strains and/or isolates. Surface distribution of the MAb-recognized antigens was revealed by immunoelectron microscopy.

Partial physicochemical characterization of MAb G9-recognized antigens identified glycopeptide characteristics. Monoclonal antibody G9 reacted with surface antigens and, hence, participated in agglutination of M gallisepticum. However, the degree of agglutination varied among the various strains and isolates, indicating a quantitative or conformational limitation or an alteration in the anomeric expression of the epitopes. Antigenic variation in M gallisepticum may be mediated by immunologic selective pressures, or a proclivity for habit niche in the host.

Summary

A panel of monoclonal antibodies (MAb) developed against Mycoplasma gallisepticum strain PG31 was used to probe the antigenic profiles of 5 recognized strains (PG31, R, S6, F, A5969) and 6 field isolates of M gallisepticum. Monoclonal antibody G9 predominantly recognized antigens at apparent molecular mass positions of 90 to 98 kDA. The MAb reacted with all strains and isolates, but the molecular mass position of the antigens varied among some mycoplasmas. Monoclonal antibody G12 reacted with all strains and isolates of M gallisepticum and had an identical banding pattern. However, MAb G10 and G11 reacted selectively only with a limited number of strains and/or isolates. Surface distribution of the MAb-recognized antigens was revealed by immunoelectron microscopy.

Partial physicochemical characterization of MAb G9-recognized antigens identified glycopeptide characteristics. Monoclonal antibody G9 reacted with surface antigens and, hence, participated in agglutination of M gallisepticum. However, the degree of agglutination varied among the various strains and isolates, indicating a quantitative or conformational limitation or an alteration in the anomeric expression of the epitopes. Antigenic variation in M gallisepticum may be mediated by immunologic selective pressures, or a proclivity for habit niche in the host.

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