Babesia bovis : identification of immunodominant merozoite surface proteins in soluble culture-derived exoantigen |
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| Authors: | W. Carl Johnson Lance E. Perryman Will L. Goff |
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| Affiliation: | (1) United States Department of Agriculture/Agricultural Research Service, Washington State University, Pullman, WA, 99164-7030, USA Fax: 509-885-8328; e-mail: wgoff@vetmed.wsu.edu, US;(2) Department of Veterinary Microbiology and Pathology, Washington State University, Pullman, WA 99164–7040, USA, US |
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| Abstract: | Babesia bovis merozoite proteins presenting as exoantigens in in vitro culture supernatants have been characterized. Bovine antisera to B. bovis exoantigens were used to immunoprecipitate [35S]-methionine metabolically labeled or lactoperoxidase-catalyzed radioiodinated B. bovis merozoite proteins. A total of 24 metabolically labeled proteins ranging in molecular weight from 24,000 to 225,000 Da and 9 radioiodinated proteins with molecular weights varying between 24,000 and 225,000 Da were identified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Monoclonal antibodies to B. bovis merozoite surface proteins were also used to immunoprecipitate metabolically labeled exoantigens directly from in vitro culture supernatants. These results demonstrate epitopes from at least nine merozoite surface proteins present in the exoantigen fraction, among which are the recently characterized major surface antigens 1 and 2, rhoptry-associated protein 1, and spherical body protein 2. Received: 1 April 1997 / Accepted: 6 May 1997 |
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