![]() ![]() The coupling of antigens to the surface of these so-called nanoparticles enhances uptake by phagocytic cells, stimulating innate-, humoral-, and cellular immune responses. Protein-, lipid-, mineral-, and polymer-based scaffolds can be used to increase the immunogenicity of antigens. 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. ![]()
0 Comments
Leave a Reply. |