A 32 kDa surface antigen of Theileria parva: Characterization and immunization studies
Previous studies using monoclonal antibody (mAb) 4C9 specific for a 32 kDa antigen (p32) of Theileria parva demonstrated expression of the antigen on the surface of the sporozoite, making it a potential antigen for sporozoite neutralization. A full-length cDNA encoding the major merozoite/piroplasm...
| Autores principales: | , , , , , , , , , |
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| Formato: | Journal Article |
| Lenguaje: | Inglés |
| Publicado: |
Cambridge University Press
2000
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| Materias: | |
| Acceso en línea: | https://hdl.handle.net/10568/35036 |
| _version_ | 1855520386402222080 |
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| author | Skilton, Robert A. Musoke, A.J. Wells, C.W. Yagi, Y. Nene, Vishvanath M. Spooner, P.R. Gachanja, J. Osaso, J. Bishop, Richard P. Morzaria, S.P. |
| author_browse | Bishop, Richard P. Gachanja, J. Morzaria, S.P. Musoke, A.J. Nene, Vishvanath M. Osaso, J. Skilton, Robert A. Spooner, P.R. Wells, C.W. Yagi, Y. |
| author_facet | Skilton, Robert A. Musoke, A.J. Wells, C.W. Yagi, Y. Nene, Vishvanath M. Spooner, P.R. Gachanja, J. Osaso, J. Bishop, Richard P. Morzaria, S.P. |
| author_sort | Skilton, Robert A. |
| collection | Repository of Agricultural Research Outputs (CGSpace) |
| description | Previous studies using monoclonal antibody (mAb) 4C9 specific for a 32 kDa antigen (p32) of Theileria parva demonstrated expression of the antigen on the surface of the sporozoite, making it a potential antigen for sporozoite neutralization. A full-length cDNA encoding the major merozoite/piroplasm surface antigen (mMPSA) of T. parva was cloned and expressed in bacteria. The expressed product reacted strongly with mAb 4C9, demonstrating identity between the p32 and mMPSA of T. parva. Using immunoblot analysis and immunoelectron microscopy with mAb 4C9 it was shown that the mMPSA is a major antigen of the merozoite and piroplasm at the cell surface, while lower levels of antigen are expressed in the sporozoite and schizont stages. Upregulation of the mMPSA occurs at merogony and can be induced by culturing schizont-infected lymphocytes at 42°C. Recombinant mMPSA of T. parva induced high titres of specific antibodies in cattle but failed to confer protection against a T. parva sporozoite stabilate challenge. The pre-challenge sera also failed to neutralize infectivity of sporozoites in an in vitro assay. Possible reasons for the lack of parasite neutralization in vivo and in vitro are discussed. |
| format | Journal Article |
| id | CGSpace35036 |
| institution | CGIAR Consortium |
| language | Inglés |
| publishDate | 2000 |
| publishDateRange | 2000 |
| publishDateSort | 2000 |
| publisher | Cambridge University Press |
| publisherStr | Cambridge University Press |
| record_format | dspace |
| spelling | CGSpace350362024-11-15T08:52:20Z A 32 kDa surface antigen of Theileria parva: Characterization and immunization studies Skilton, Robert A. Musoke, A.J. Wells, C.W. Yagi, Y. Nene, Vishvanath M. Spooner, P.R. Gachanja, J. Osaso, J. Bishop, Richard P. Morzaria, S.P. disease control animal diseases Previous studies using monoclonal antibody (mAb) 4C9 specific for a 32 kDa antigen (p32) of Theileria parva demonstrated expression of the antigen on the surface of the sporozoite, making it a potential antigen for sporozoite neutralization. A full-length cDNA encoding the major merozoite/piroplasm surface antigen (mMPSA) of T. parva was cloned and expressed in bacteria. The expressed product reacted strongly with mAb 4C9, demonstrating identity between the p32 and mMPSA of T. parva. Using immunoblot analysis and immunoelectron microscopy with mAb 4C9 it was shown that the mMPSA is a major antigen of the merozoite and piroplasm at the cell surface, while lower levels of antigen are expressed in the sporozoite and schizont stages. Upregulation of the mMPSA occurs at merogony and can be induced by culturing schizont-infected lymphocytes at 42°C. Recombinant mMPSA of T. parva induced high titres of specific antibodies in cattle but failed to confer protection against a T. parva sporozoite stabilate challenge. The pre-challenge sera also failed to neutralize infectivity of sporozoites in an in vitro assay. Possible reasons for the lack of parasite neutralization in vivo and in vitro are discussed. 2000-06 2014-02-26T16:15:35Z 2014-02-26T16:15:35Z Journal Article https://hdl.handle.net/10568/35036 en Limited Access Cambridge University Press Skilton, R.A., Musoke, A.J., Wells, C.W., Yagi, Y., Nene, V., Spooner, P.R., Gachanja, J., Osaso, J., Bishop, R.P. and Morzaria, S.P. 2000. A 32 kDa surface antigen of Theileria parva: Characterization and immunization studies. Parasitology 120(6):553-564. |
| spellingShingle | disease control animal diseases Skilton, Robert A. Musoke, A.J. Wells, C.W. Yagi, Y. Nene, Vishvanath M. Spooner, P.R. Gachanja, J. Osaso, J. Bishop, Richard P. Morzaria, S.P. A 32 kDa surface antigen of Theileria parva: Characterization and immunization studies |
| title | A 32 kDa surface antigen of Theileria parva: Characterization and immunization studies |
| title_full | A 32 kDa surface antigen of Theileria parva: Characterization and immunization studies |
| title_fullStr | A 32 kDa surface antigen of Theileria parva: Characterization and immunization studies |
| title_full_unstemmed | A 32 kDa surface antigen of Theileria parva: Characterization and immunization studies |
| title_short | A 32 kDa surface antigen of Theileria parva: Characterization and immunization studies |
| title_sort | 32 kda surface antigen of theileria parva characterization and immunization studies |
| topic | disease control animal diseases |
| url | https://hdl.handle.net/10568/35036 |
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