Publication: Generation, characterization and immunogenicity of a novel chimeric recombinant protein based on Plasmodium vivax AMA-1 and MSP1<inf>19</inf>
Issued Date
2017-04-25
Resource Type
ISSN
18732518
0264410X
0264410X
Other identifier(s)
2-s2.0-85015784504
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Mahidol University
Rights Holder(s)
SCOPUS
Bibliographic Citation
Vaccine. Vol.35, No.18 (2017), 2463-2472
Suggested Citation
Mariana Vilela Rocha, Kátia Sanches Françoso, Luciana Chagas Lima, Tarsila Mendes Camargo, Ricardo L.D. Machado, Fabio T.M. Costa, Laurent Rénia, Francois Nosten, Bruce Russell, Mauricio M. Rodrigues, Irene S. Soares Generation, characterization and immunogenicity of a novel chimeric recombinant protein based on Plasmodium vivax AMA-1 and MSP1<inf>19</inf>. Vaccine. Vol.35, No.18 (2017), 2463-2472. doi:10.1016/j.vaccine.2017.03.023 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/41910
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Title
Generation, characterization and immunogenicity of a novel chimeric recombinant protein based on Plasmodium vivax AMA-1 and MSP1<inf>19</inf>
Abstract
© 2017 Elsevier Ltd Plasmodium vivax is the most widely distributed malaria species and the most prevalent species of malaria in America and Asia. Vaccine development against P. vivax is considered a priority in the global program for the eradication of malaria. Earlier studies have characterized the Apical Membrane Antigen 1 (AMA-1) ectodomain and the C-terminal region (19 kDa) of the Merozoite Surface Protein 1 (MSP-1) of P. vivax as immunodominant antigens. Based on this characterization, we designed a chimeric recombinant protein containing both merozoite immunodominant domains (PvAMA166-MSP119). The recombinant PvAMA166-MSP119 was successfully expressed in Pichia pastoris and used to immunize two different mouse strains (BALB/c and C57BL/6) in the presence of the Poly (I:C) as an adjuvant. Immunization with the chimeric protein induced high antibody titers against both proteins in both strains of mice as detected by ELISA. Antisera also recognized the native proteins expressed on the merozoites of mature P. vivax schizonts. Moreover, this antigen was able to induce IFN-gamma-secreting cells in C57BL/6 mice. These findings indicate that this novel yeast recombinant protein containing PvAMA166 and PvMSP119 is advantageous, because of improved antibody titers and cellular immune response. Therefore, this formulation should be further developed for pre-clinical trials in non-human primates as a potential candidate for a P. vivax vaccine.