ABSTRACT
Immunization of cattle with a purified Anaplasma marginale major surface protein, AmF36, induced protection against homologous challenge with the Florida isolate. Similarly, immunized cattle were protected from challenge with the antigenically and structurally distinct Washington-O isolate of A. marginale. The degree of protection in AmF36-immunized cattle varied from complete prevention of rickettsemia to significant delay in the onset of rickettsemia compared with control immunized cattle. A single AmF36 vaccinate was not protected against homologous challenge despite development of a strong antibody response. Immunoprecipitation of A. marginale proteins with a monoclonal antibody to AmF36 identified minor molecular size heterogeneity in this protein from different isolates, including the Florida and Washington-O isolates. The apparent molecular size of this surface protein in the Florida isolate was 36 kilodaltons, whereas the analogous proteins in Washington-O and four other isolates of A. marginale from the United States had molecular masses of 33 to 34 kilodaltons. Significantly, the surface-exposed peptides of these proteins appear to be conserved among the different isolates. These results demonstrate the potential of AmF36 as a subunit immunogen for bovine anaplasmosis and indicate a structural basis for its cross-protective ability.
