Aotus selected for this study were subjected to liver and kidney functional tests as well as hemoglobin and hematocrit measurements. Reversine clinical and laboratory evaluation was made before immunization and after the end of the study. If loss of appetite or weakness were observed, further clinical testing and evaluation was performed, such hematology and chemical to ensure healthy conditions. An experienced veterinarian and technicians were in charge of animal handling which did not require anesthesia. The endpoints considered for the monkeys were decrease of body weight, lack of appetite, skin`s lesions in the immunization site due to the adjuvant, corporal temperature, dehydration test, low levels of Haematocrit/hemoglobin and changes on the biochemistry parameters. None of the animals died during the course of the research. After the end of the study and healthy conditions verification, monkeys were transferred to a rest or reproduction modules where they are kept alive with food and water supply until their natural death. We report the functional TB activity of a Pvs48/45 recombinant protein produced in E. coli using a harmonized sequence, which leads to high yields of a properly folded protein and conserved conformational epitopes. Epitopes with conformation similar to the native protein were indirectly determined to be WZ4002 side effects present in the recombinant product by protein reactivity with antibodies elicited by both the natural exposure to P. vivax malaria in endemic areas as well as by the recognition of parasite proteins by antibodies produced through experimental animal immunizations with the Pvs48/45 recombinant protein. Even more interesting is the fact that anti-Pvs48/45 antibodies produced by immunized mice and monkeys efficiently blocked parasite transmission to An. albimanus mosquitoes in ex-vivo MFA. Although heterologous protein production in E. coli has become a routine method for proteins of different characteristics, the expression of soluble and functional malaria proteins in bacteria still represents a challenge due to considerations of cost, speed, ease of use and genetic manipulation. Furthermore, it frequently results in a lack of expression, poor protein solubility due to the aggregation of the recombinant product in inclusion bodies, and in cellular toxicity. Several Plasmodium genome features are thought to hinder optimal expression of malarial proteins. These features are: 1) the P. falciparum genome exhibits an unusually high content of adenine and thymine ; 2) P. falciparum proteins are larger than their homologues in others malaria species; and 3) Plasmodium parasites display post-translational modifications that are unique to this parasite species. Although in many aspects the P. vivax genome is similar to that of P. falciparum, P. vivax contains AT-rich chromosome ends and has a telomere-distal regions which consists of GC-rich sequences.