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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...

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Autores principales: Cowan, Graeme J. M., Bockau, Ulrike, Eleni-Muus, Janna, Aldag, Ingo, Samuel, Kay, Creasey, Alison M., Hartmann, Marcus W. W., Cavanagh, David R.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3906136/
https://www.ncbi.nlm.nih.gov/pubmed/24489871
http://dx.doi.org/10.1371/journal.pone.0087198
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author Cowan, Graeme J. M.
Bockau, Ulrike
Eleni-Muus, Janna
Aldag, Ingo
Samuel, Kay
Creasey, Alison M.
Hartmann, Marcus W. W.
Cavanagh, David R.
author_facet Cowan, Graeme J. M.
Bockau, Ulrike
Eleni-Muus, Janna
Aldag, Ingo
Samuel, Kay
Creasey, Alison M.
Hartmann, Marcus W. W.
Cavanagh, David R.
author_sort Cowan, Graeme J. M.
collection PubMed
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.
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spelling pubmed-39061362014-01-31 A Novel Malaria Vaccine Candidate Antigen Expressed in Tetrahymena thermophila Cowan, Graeme J. M. Bockau, Ulrike Eleni-Muus, Janna Aldag, Ingo Samuel, Kay Creasey, Alison M. Hartmann, Marcus W. W. Cavanagh, David R. PLoS One Research Article 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. Public Library of Science 2014-01-29 /pmc/articles/PMC3906136/ /pubmed/24489871 http://dx.doi.org/10.1371/journal.pone.0087198 Text en © 2014 Cowan et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Cowan, Graeme J. M.
Bockau, Ulrike
Eleni-Muus, Janna
Aldag, Ingo
Samuel, Kay
Creasey, Alison M.
Hartmann, Marcus W. W.
Cavanagh, David R.
A Novel Malaria Vaccine Candidate Antigen Expressed in Tetrahymena thermophila
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
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3906136/
https://www.ncbi.nlm.nih.gov/pubmed/24489871
http://dx.doi.org/10.1371/journal.pone.0087198
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