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Immunogenic properties of the Plasmodium vivax vaccine candidate MSP119 expressed as a secreted non-glycosylated polypeptide from Pichia pastoris

Published online by Cambridge University Press:  30 July 2002

I. S. SOARES
Affiliation:
Departamento de Análises Clínicas e Toxicológicas, Faculdade de Ciências Farmacêuticas, Universidade de São Paulo, Av. Prof. Lineu Prestes, 580, Bloco 17, São Paulo, SP, Brazil, 05508-900 Departamento de Microbiologia, Imunologia e Parasitologia, Escola Paulista de Medicina, Universidade Federal de São Paulo, Rua Botucatu 862, 6th floor, São Paulo, SP, Brazil, 04023-062
M. M. RODRIGUES
Affiliation:
Departamento de Microbiologia, Imunologia e Parasitologia, Escola Paulista de Medicina, Universidade Federal de São Paulo, Rua Botucatu 862, 6th floor, São Paulo, SP, Brazil, 04023-062

Abstract

The 19 kDa C-terminal region of the merozoite surface protein 1 (MSP119) is one of the most promising vaccine candidates against the erythrocytic forms of malaria. In the present study, a gene encoding the Plasmodium vivax MSP119 epitope (PvMSP119) and the Pan-Allelic DR epitope (PADRE) was expressed in the methylotrophic yeast Pichia pastoris. A non-glycosylated form of the recombinant protein rPvMSP119-PADRE was purified from culture supernatants. This recombinant protein maintains its antigenicity, being recognized by a very high percentage (85·6%) of sera from Brazilian individuals naturally exposed to P. vivax. The antibody immune response elicited by rPvMSP119-PADRE was compared in C57BL/6 mice immunized with different adjuvant formulations. After 3 immunizing doses, antibody titres induced in the presence of the adjuvants monophosphoryl lipid A, trehalose dicorynomycolate and cell wall skeleton or alum plus CpG ODN 1826 were as high as titres generated by Complete Freund's Adjuvant. Based on these immunological studies, we concluded that rPvMSP119-PADRE deserves further evaluation in pre-clinical immunizations against P. vivax in non-human primates.

Type
Research Article
Copyright
2002 Cambridge University Press

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