Generation, characterization and immunogenicity of a novel chimeric recombinant protein based on Plasmodium vivax AMA-1 and MSP1<inf>19</inf>

dc.contributor.authorMariana Vilela Rochaen_US
dc.contributor.authorKátia Sanches Françosoen_US
dc.contributor.authorLuciana Chagas Limaen_US
dc.contributor.authorTarsila Mendes Camargoen_US
dc.contributor.authorRicardo L.D. Machadoen_US
dc.contributor.authorFabio T.M. Costaen_US
dc.contributor.authorLaurent Réniaen_US
dc.contributor.authorFrancois Nostenen_US
dc.contributor.authorBruce Russellen_US
dc.contributor.authorMauricio M. Rodriguesen_US
dc.contributor.authorIrene S. Soaresen_US
dc.contributor.otherUniversidade de Sao Paulo - USPen_US
dc.contributor.otherInstituto Evandro Chagasen_US
dc.contributor.otherUniversidade Estadual de Campinasen_US
dc.contributor.otherA-Star, Singapore Immunology Networken_US
dc.contributor.otherMahidol Universityen_US
dc.contributor.otherNuffield Department of Clinical Medicineen_US
dc.contributor.otherUniversity of Otagoen_US
dc.contributor.otherUniversidade Federal de Sao Pauloen_US
dc.description.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.en_US
dc.identifier.citationVaccine. Vol.35, No.18 (2017), 2463-2472en_US
dc.rightsMahidol Universityen_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.subjectImmunology and Microbiologyen_US
dc.titleGeneration, characterization and immunogenicity of a novel chimeric recombinant protein based on Plasmodium vivax AMA-1 and MSP1<inf>19</inf>en_US