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Transmission-blocking vaccines (TBV) target the sexual-stages of the malaria parasite in the mosquito midgut and are widely considered to be an essential tool for malaria elimination. High-titer functional antibodies are required against target antigens to achieve effective transmission-blocking activity. We have fused Pfs25, the leading malaria TBV candidate antigen to IMX313, a molecular adjuvant and expressed it both in ChAd63 and MVA viral vectors and as a secreted protein-nanoparticle. Pfs25-IMX313 expressed from viral vectors or as a protein-nanoparticle is significantly more immunogenic and gives significantly better transmission-reducing activity than monomeric Pfs25. In addition, we demonstrate that the Pfs25-IMX313 protein-nanoparticle leads to a qualitatively improved antibody response in comparison to soluble Pfs25, as well as to significantly higher germinal centre (GC) responses. These results demonstrate that antigen multimerization using IMX313 is a very promising strategy to enhance antibody responses against Pfs25, and that Pfs25-IMX313 is a highly promising TBV candidate vaccine.

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Adenoviridae, Adjuvants, Immunologic, Animals, Antibodies, Protozoan, Antigens, Protozoan, Culicidae, Gene Expression, Genetic Vectors, Germinal Center, Humans, Immunogenicity, Vaccine, Insect Vectors, Life Cycle Stages, Malaria Vaccines, Malaria, Falciparum, Mice, Mice, Inbred BALB C, Pichia, Plasmids, Plasmodium falciparum, Protozoan Proteins, Recombinant Fusion Proteins, Vaccination, Vaccines, Synthetic