Simple jQuery Dropdowns
Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/41910
Title: Generation, characterization and immunogenicity of a novel chimeric recombinant protein based on Plasmodium vivax AMA-1 and MSP1<inf>19</inf>
Authors: 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
Universidade de Sao Paulo - USP
Instituto Evandro Chagas
Universidade Estadual de Campinas
A-Star, Singapore Immunology Network
Mahidol University
Nuffield Department of Clinical Medicine
University of Otago
Universidade Federal de Sao Paulo
Keywords: Biochemistry, Genetics and Molecular Biology;Immunology and Microbiology
Issue Date: 25-Apr-2017
Citation: Vaccine. Vol.35, No.18 (2017), 2463-2472
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.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85015784504&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/41910
ISSN: 18732518
0264410X
Appears in Collections:Scopus 2016-2017

Files in This Item:
There are no files associated with this item.


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.