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Ferritin is a ubiquitous protein primarily known for its role in intracellular iron storage, but it has emerged as a premier self-assembling nanoparticle scaffold for vaccine development (Zhang et al., 2020) [1]. In the context of Nipah virus (NiV) prevention, the ferritin scaffold is engineered to display the attachment glycoprotein (G) from both Malaysia (NiV-M) and Bangladesh (NiV-B) strains, often utilizing an Fc-fusion strategy to enhance protein stability and simplify manufacturing (Joyce et al., 2022; Czajkowsky et al., 2012) [2, 4]. This multivalent presentation mimics the repetitive antigenic structure of viral particles, thereby significantly increasing the potency of the immune response compared to monomeric antigens (Zhang et al., 2020) [1]. Nipah virus is a highly lethal zoonotic pathogen that causes severe respiratory illness and encephalitis, making the development of such platforms a global health priority (Bossart et al., 2012) [3]. The manufacturing interaction specifically refers to the biochemical and biophysical processes required to successfully conjugate or fuse the NiV-G-Fc proteins onto the ferritin nanocage while maintaining structural integrity and epitope accessibility (Joyce et al., 2022) [2]. This approach aims to provide a broad-spectrum vaccine candidate capable of protecting against diverse NiV outbreaks (Bossart et al., 2012) [3].
The ferritin nanoparticle scaffold enables the multivalent display of viral antigens, specifically the Nipah virus G protein, which promotes B-cell receptor clustering and the induction of high-titer neutralizing antibodies (Zhang et al., 2020; Joyce et al., 2022) [1, 2].
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