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Bacterially expressed full-length recombinant Plasmodium falciparum RH5 protein binds erythrocytes and elicits potent strain-transcending parasite-neutralizing antibodies.

Plasmodium falciparum reticulocyte binding like homolog protein 5 (PfRH5) is important merozoites receptor ligand binding to erythrocytes, basigin. PfRH5 is an attractive candidate malaria vaccine, as expressed by a number of strains Hamster Recombinant Proteins of P. falciparum, can not be genetically altered, and exhibit limited sequence polymorphism. 

Viral vector-induced potent antibody PfRH5 erythrocyte invasion is inhibited. However, it has been a challenge to produce a full-length recombinant expression systems based PfRH5 in bacterial cells. In this study, we have produced full-length recombinant PfRH5 in Escherichia coli that specifically bind erythrocytes exhibit similar to the original PfRH5 parasite protein and also, importantly, elicits potent inhibitory antibodies invasion against a number of strains of P. falciparum. Antibasigin antibodies block the erythrocyte binding both native and recombinant PfRH5, further asserted that they bind with basigin. 


We have thus succeeded in producing a full-length functional PfRH5 as erythrocyte binding active recombinant protein with conformational integrity that mimics that of native parasite protein and elicits potent antibody-neutralizing parasite strain-exceeded. P. falciparum has the ability to develop immune escape mechanism, and thus, the blood-stage malaria vaccines that target multiple antigens or pathways may prove efficacious. 
Bacterially expressed full-length recombinant Plasmodium falciparum RH5 protein binds erythrocytes and elicits potent strain-transcending parasite-neutralizing antibodies.

In this case, the combination of antibodies targeting antigens PfRH5 and other key merozoites produced an additive inhibitory effective against strains of P. falciparum worldwide a few. PfRH5 are immunogenic when immunized with other Mouse Recombinant Proteins antigens, allowing a strong antibody response inhibition invasion with no immune disorders. Our results strongly support the development of a vaccine PfRH5 as a component of a combination of blood-stage malaria.

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