Sistemas de expresión de proteínas recombinantes para el análisis funcional de antígenos de Plasmodium falciparum y Plasmodium vivax: una revisión

Introduction. Understanding the function of Plasmodium spp. Antigens involved in invasion of host cells is necessary to design vaccines. Different studies have generated recombinant proteins using heterologous expression systems, obtaining molecules similar to native ones. These advances are essential to develop strategies that block the infection of these pathogens.Objective. Describe the most important characteristics and methodological aspects of recombinant protein expression systems in functional studies of Plasmodium spp.Methodology. Descriptive review of studies published in PubMed, Science Direct, Embase and MedLine. Inclusion criteria: works published between 2010 and 2020 that included recombinant systems in Escherichia coli cells, mammalian and cell-free, for functional studies of Plasmodium falciparum and Plasmodium vivax antigens. 70 original articles were reviewed, 58 met the established criteria and 12 used other heterologous systems than those analyzed in this study.Results. Obtaining recombinant proteins by means of a prokaryotic system, with higher performance and low cost, has allowed functional studies of a significant number of antigens. Mammalian cell and cell free systems, which allow for post-translational modifications and adequate folding of molecules, are used to produce antigen libraries with native-like conformational structure.Conclusion. Plasmodium spp. antigen study involved in infection and development in target cells, requires adequate selection of the recombinant production method. The refinement of expression processes in prokaryotic, eukaryotic and in vitro systems, through genetic engineering and cell culture, will allow better yields and lower cost