![]() Samples that tested negative are depicted at the detection limit of the PCR (1.3 log 10 RNA copies/mL) ( f) Viral RNA in liver and spleen samples of vaccinated and mock-vaccinated lambs by RT-qPCR. ( e) Monitoring of viral RNA in vaccinated and mock-vaccinated lambs by RT-qPCR. The x-axis is set to the limit of detection of the VNT and wells were considered positive when >50% inhibition of viral growth was observed. ( d) Neutralizing antibody responses in weekly-obtained serum samples. ( c) Gn head-specific antibody responses as determined by ELISA. ( b) Average rectal temperatures of vaccinated and mock-vaccinated lambs post RVFV challenge. ( a) Schematic presentation of the vaccination regimen and vaccines. RVFV vaccination-challenge experiment with Gn head-coupled MPSP particles in lambs. Error bars in panels b, c, d and e represent SDs. No animals succumbed or reached a HEP in this experiment. Samples that tested negative are depicted at the detection limit of the PCR (2.3 log 10 RNA copies/mL). Samples that tested negative are depicted at the detection limit of the PCR (1.3 log 10 RNA copies/mL) ( f) Viral RNA in liver and spleen samples of vaccinated and mock-vaccinated lambs using RT-qPCR. ( e) Monitoring of viral RNA in vaccinated and mock-vaccinated lambs using RT-qPCR. ![]() RVFV vaccination-challenge experiment with Gn head-conjugated LS particles in lambs. Gn head domain Rift Valley fever virus bacterial superglue multimeric protein scaffold particles sheep. Furthermore, the same subunit coupled to two other MPSPs ( Geobacillus stearothermophilus E2 or a modified KDPG Aldolase) provided full protection in lambs as well. The results showed that the Gn head domain, when bound to the lumazine synthase-based MPSP, reduced mortality in a lethal mouse model and protected lambs, the most susceptible RVFV target animals, from viremia and clinical signs after immunization. For this, the head domain of glycoprotein Gn, a known target of neutralizing antibodies, was coupled on various MPSPs to further assess immunogenicity and efficacy in vivo. In the present work, we assessed whether this technology could improve the immunogenicity of a candidate subunit vaccine against the zoonotic Rift Valley fever virus (RVFV). ![]() By combining two emerging technologies-i.e., self-assembling multimeric protein scaffold particles (MPSPs) and bacterial superglue-these shortcomings can be overcome and antigens can be bound on particles in their native conformation. Conventionally, antigens are conjugated to scaffolds through genetic fusion or chemical conjugation, which may result in impaired assembly or heterogeneous binding and orientation of the antigens. Compared to free antigens, antigens immobilized on scaffolds, such as nanoparticles, generally show improved immunogenicity. ![]()
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