Characterization of a novel merozoite surface protein of Plasmodium vivax, Pv41.

Since the genome of Plasmodium vivax was sequenced, few proteins have been characterized as highly immunogenic and candidates for inclusion in a vivax malaria vaccine. The P. vivax 41 (Pv41) protein has a signal peptide, one glutamate-rich domain in its central region, and two sexual stage s48/45 domains, and is characterized as a gametocyte surface protein; however, this protein may be expressed principally on the merozoite surface of parasites. The previous study reported the transcription, blood-stage expression, and subcellular localization of Pv41 within the parasite. In this study, the recombinant Pv41 protein was expressed as a soluble form, of a molecular mass ~44 kDa, by a cell-free expression system and was specifically recognized by animal immune sera and vivax patient sera. Evaluation of the human humoral immune response to Pv41 indicated a high immunogenicity, with 62.5% sensitivity and 95% specificity, by protein array. Immunofluorescence assays (IFA) using polyclonal anti-Pv41 antibodies showed that Pv41 was localized on the merozoite surface. The high immunogenicity of Pv41 indicates its potential as a vivax malaria vaccine candidate antigen, particularly in light of its location on the merozoite surface of the parasite.