Navegando por Palavras-chave "Recombinant vaccine"

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    Generation, characterization and immunogenicity of a novel chimeric recombinant protein based on Plasmodium vivax AMA-1 and MSP1(19)
    (Elsevier Sci Ltd, 2017) Rocha, Mariana Vilela; Francoso, Katia Sanches; Lima, Luciana Chagas; Camargo, Tarsila Mendes; Machado, Ricardo L. D.; Costa, Fabio T. M.; Renia, Laurent; Nosten, Francois; Russell, Bruce; Rodrigues, Mauricio M. [UNIFESP]; Soares, Irene S.
    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 (PvAMA1(66)-MSP1(19)). 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 PvAMA1(66) and PvMSP1(19) 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. (C) 2017 Elsevier Ltd. All rights reserved.
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    A recombinant multi-antigen vaccine formulation containing Babesia bovis merozoite surface antigens MSA-2a(1), MSA-2b and MSA-2c elicits invasion-inhibitory antibodies and IFN-gamma producing cells
    (Biomed Central Ltd, 2016) Gimenez, Alba Marina [UNIFESP]; Francoso, Katia S.; Ersching, Jonatan [UNIFESP]; Icimoto, Marcelo Yudi [UNIFESP]; Oliveira, Vitor [UNIFESP]; Rodriguez, Anabel E.; Schnittger, Leonhard; Florin-Christensen, Monica; Rodrigues, Mauricio Martins [UNIFESP]; Soares, Irene S.
    Background: Babesia bovis is a tick transmitted protozoan hemoparasite and the causative agent of bovine babesiosis, a potential risk to more than 500 million cattle worldwide. The vaccines currently available are based on attenuated parasites, which are difficult to produce, and are only recommended for use in bovines under one year of age. When used in older animals, these vaccines may cause life-threatening clinical symptoms and eventually death. The development of a multi-subunit recombinant vaccine against B. bovis would be attractive from an economic standpoint and, most importantly, could be recommended for animals of any age. In the present study, recombinant ectodomains of MSA-2a(1), MSA-2b and MSA-2c antigens were expressed in Pichia pastoris yeast as secreted soluble peptides. Results: The antigens were purified to homogeneity, and biochemically and immunologically characterized. A vaccine formulation was obtained by emulsifying a mixture of the three peptides with the adjuvant Montanide ISA 720, which elicited high IgG antibody titers against each of the above antigens. IgG antibodies generated against each MSA-antigen recognized merozoites and significantly inhibited the invasion of bovine erythrocytes. Cellular immune responses were also detected, which were characterized by splenic and lymph node CD4(+) T cells producing IFN-gamma and TNF-alpha upon stimulation with the antigens MSA-2a(1) or MSA-2c. Conclusions: These data strongly suggest the high protective potential of the presented formulation, and we propose that it could be tested in vaccination trials of bovines challenged with B. bovis.
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    A recombinant vaccine based on domain II of Plasmodium vivax Apical Membrane Antigen 1 induces high antibody titres in mice
    (Elsevier B.V., 2010-08-31) Gentil, Fernanda; Bargieri, Daniel Y. [UNIFESP]; Leite, Juliana A.; Francoso, Katia S.; Patricio, Mariana B. M.; Espindola, Noeli M.; Vaz, Adelaide J.; Palatnik-de-Sousa, Clarisa B.; Rodrigues, Mauricio M. [UNIFESP]; Costa, Fabio Trindade Maranhão [UNIFESP]; Soares, Irene S.; Universidade de São Paulo (USP); Universidade Federal de São Paulo (UNIFESP); Universidade Estadual de Campinas (UNICAMP); Universidade Federal do Rio de Janeiro (UFRJ)
    The Apical Membrane Antigen 1 (AMA-1) is considered a promising candidate for development of a malaria vaccine against asexual stages of Plasmodium. We recently identified domain II (DII) of Plasmodium vivax AMA-1 (PvAMA-1) as a highly immunogenic region recognised by IgG antibodies present in many individuals during patent infection with P. vivax. the present study was designed to evaluate the immunogenic properties of a bacterial recombinant protein containing PvAMA-1 DII. To accomplish this, the recombinant protein was administered to mice in the presence of each of the following six adjuvants: Complete/Incomplete Freund's Adjuvant (CFA/IFA), aluminium hydroxide (Alum), Quil A, QS21 saponin, CpG-ODN 1826 and TiterMax. We found that recombinant DII was highly immunogenic in BALB/c mice when administered in the presence of any of the tested adjuvants. Importantly, we show that DII-specific antibodies recognised the native AMA-1 protein expressed on the surface of P. vivax merozoites isolated from the blood of infected patients. These results demonstrate that a recombinant protein containing PvAMA-1 DII is immunogenic when administered in different adjuvant formulations, and indicate that this region of the AMA-1 protein should continue to be evaluated as part of a subunit vaccine against vivax malaria. (C) 2010 Elsevier B.V. All rights reserved.