A novel malaria vaccine candidate antigen expressed in Tetrahymena thermophila.
Development of effective malaria vaccines is hampered by the problem of producing correctly folded Plasmodium proteins for use as vaccine components. We have investigated the use of a novel ciliate expression system, Tetrahymena thermophila, as a P. falciparum vaccine antigen platform. A synthetic v...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2014-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3906136?pdf=render |
| _version_ | 1818217972946173952 |
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| author | Graeme J M Cowan Ulrike Bockau Janna Eleni-Muus Ingo Aldag Kay Samuel Alison M Creasey Marcus W W Hartmann David R Cavanagh |
| author_facet | Graeme J M Cowan Ulrike Bockau Janna Eleni-Muus Ingo Aldag Kay Samuel Alison M Creasey Marcus W W Hartmann David R Cavanagh |
| author_sort | Graeme J M Cowan |
| collection | DOAJ |
| description | Development of effective malaria vaccines is hampered by the problem of producing correctly folded Plasmodium proteins for use as vaccine components. We have investigated the use of a novel ciliate expression system, Tetrahymena thermophila, as a P. falciparum vaccine antigen platform. A synthetic vaccine antigen composed of N-terminal and C-terminal regions of merozoite surface protein-1 (MSP-1) was expressed in Tetrahymena thermophila. The recombinant antigen was secreted into the culture medium and purified by monoclonal antibody (mAb) affinity chromatography. The vaccine was immunogenic in MF1 mice, eliciting high antibody titers against both N- and C-terminal components. Sera from immunized animals reacted strongly with P. falciparum parasites from three antigenically different strains by immunofluorescence assays, confirming that the antibodies produced are able to recognize parasite antigens in their native form. Epitope mapping of serum reactivity with a peptide library derived from all three MSP-1 Block 2 serotypes confirmed that the MSP-1 Block 2 hybrid component of the vaccine had effectively targeted all three serotypes of this polymorphic region of MSP-1. This study has successfully demonstrated the use of Tetrahymena thermophila as a recombinant protein expression platform for the production of malaria vaccine antigens. |
| first_indexed | 2024-12-12T07:16:22Z |
| format | Article |
| id | doaj.art-76f6dc7e0bcc40768418ad13ebdc7062 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-12T07:16:22Z |
| publishDate | 2014-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-76f6dc7e0bcc40768418ad13ebdc70622022-12-22T00:33:31ZengPublic Library of Science (PLoS)PLoS ONE1932-62032014-01-0191e8719810.1371/journal.pone.0087198A novel malaria vaccine candidate antigen expressed in Tetrahymena thermophila.Graeme J M CowanUlrike BockauJanna Eleni-MuusIngo AldagKay SamuelAlison M CreaseyMarcus W W HartmannDavid R CavanaghDevelopment of effective malaria vaccines is hampered by the problem of producing correctly folded Plasmodium proteins for use as vaccine components. We have investigated the use of a novel ciliate expression system, Tetrahymena thermophila, as a P. falciparum vaccine antigen platform. A synthetic vaccine antigen composed of N-terminal and C-terminal regions of merozoite surface protein-1 (MSP-1) was expressed in Tetrahymena thermophila. The recombinant antigen was secreted into the culture medium and purified by monoclonal antibody (mAb) affinity chromatography. The vaccine was immunogenic in MF1 mice, eliciting high antibody titers against both N- and C-terminal components. Sera from immunized animals reacted strongly with P. falciparum parasites from three antigenically different strains by immunofluorescence assays, confirming that the antibodies produced are able to recognize parasite antigens in their native form. Epitope mapping of serum reactivity with a peptide library derived from all three MSP-1 Block 2 serotypes confirmed that the MSP-1 Block 2 hybrid component of the vaccine had effectively targeted all three serotypes of this polymorphic region of MSP-1. This study has successfully demonstrated the use of Tetrahymena thermophila as a recombinant protein expression platform for the production of malaria vaccine antigens.http://europepmc.org/articles/PMC3906136?pdf=render |
| spellingShingle | Graeme J M Cowan Ulrike Bockau Janna Eleni-Muus Ingo Aldag Kay Samuel Alison M Creasey Marcus W W Hartmann David R Cavanagh A novel malaria vaccine candidate antigen expressed in Tetrahymena thermophila. PLoS ONE |
| title | A novel malaria vaccine candidate antigen expressed in Tetrahymena thermophila. |
| title_full | A novel malaria vaccine candidate antigen expressed in Tetrahymena thermophila. |
| title_fullStr | A novel malaria vaccine candidate antigen expressed in Tetrahymena thermophila. |
| title_full_unstemmed | A novel malaria vaccine candidate antigen expressed in Tetrahymena thermophila. |
| title_short | A novel malaria vaccine candidate antigen expressed in Tetrahymena thermophila. |
| title_sort | novel malaria vaccine candidate antigen expressed in tetrahymena thermophila |
| url | http://europepmc.org/articles/PMC3906136?pdf=render |
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