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

摘要: Plasmodium falciparum reticulocyte binding-like homologous protein 5 (PfRH5) is an essential merozoite ligand that binds with its erythrocyte receptor, basigin. PfRH5 attractive malaria vaccine candidate, as it expressed by a wide number of P. strains, cannot be genetically disrupted, and exhibits limited sequence polymorphisms. Viral vector-induced antibodies potently inhibited invasion. However, has been challenge to generate full-length recombinant in bacterial-cell-based expression system. In this study, we have produced Escherichia coli specific binding similar the native parasite also, importantly, elicits potent invasion-inhibitory against strains. Antibasigin blocked both PfRH5, further confirming they bind We thus successfully functionally active conformational integrity mimics strain-transcending parasite-neutralizing antibodies. capability develop immune escape mechanisms, thus, blood-stage vaccines target multiple antigens or pathways may prove highly efficacious. regard, antibody combinations targeting other key additive inhibition worldwide was immunogenic when immunized antigens, eliciting responses no interference. Our results strongly support development component combination vaccine.