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Abstract Background Serological tests to detect antibodies specific to <it>Plasmodium vivax </it>could be a valuable tool for epidemiological studies, for screening blood donors in areas where the malaria is not endemic and for diagnosis of infected individuals. Because <it>P. vivax </it>cannot be easily obtained <it>in vitro</it>, ELISA assays using total or semi-purified antigens are rarely used. Based on this limitation, we tested whether recombinant proteins representing the 19 kDa C-terminal region of the merozoite surface protein-1 of <it>P. vivax </it>(MSP119) could be useful for serological detection of malaria infection. Methods Three purified recombinant proteins produced in <it>Escherichia coli </it>(GST-MSP119, His6-MSP119 and His6-MSP119-PADRE) and one in <it>Pichia pastoris </it>(yMSP119-PADRE) were compared for their ability to bind to IgG antibodies of individuals with patent <it>P. vivax </it>infection. The method was tested with 200 serum samples collected from individuals living in the north of Brazil in areas endemic for malaria, 53 serum samples from individuals exposed to <it>Plasmodium falciparum </it>infection and 177 serum samples from individuals never exposed to malaria. Results Overall, the sensitivity of the ELISA assessed with sera from naturally infected individuals was 95%. The proportion of serum samples that reacted with recombinant proteins GST-MSP119, His6-MSP119, His6-MSP119-PADRE and yMSP119-PADRE was 90%, 93.5%, 93.5% and 93.5%, respectively. The specificity values of the ELISA determined with sera from healthy individuals and from individuals with other infectious diseases were 98.3% (GST-MSP119), 97.7% (His6-MSP119 and His6-MSP119-PADRE) or 100% (yMSP119-PADRE). Conclusions Our study demonstrated that for the Brazilian population, an ELISA using a recombinant protein of the MSP119 can be used as the basis for the development of a valuable serological assay for the detection of <it>P. vivax </it>malaria.</p

malaria journal

Serological detection of Plasmodium vivax malaria using recombinant proteins corresponding to the 19-kDa C-terminal region of the merozoite surface protein-1