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The host cell receptors for YF-VAX (the 17D strain of the Yellow Fever Virus) are a collection of cell surface molecules that facilitate viral attachment and internalization. The primary receptors and attachment factors identified include AXL receptor tyrosine kinase (AXL), T-cell immunoglobulin and mucin domain-1 (TIM-1), and the C-type lectin DC-SIGN (CD209), which is crucial for the infection of dendritic cells (Lozach et al., 2005; Meertens et al., 2012). These receptors often utilize a mechanism known as apoptotic mimicry, where the virus binds to host proteins like Gas6 that recognize phosphatidylserine on the viral envelope, subsequently engaging TAM receptors like Axl to trigger endocytosis (Jemielity et al., 2013). Additionally, the chaperone protein GRP78 (HSPA5) has been identified as a co-receptor that interacts with the viral envelope protein to mediate entry (Nain et al., 2017). Because YF-VAX is a live-attenuated vaccine, its ability to infect host cells via these receptors is essential for the replication required to elicit a protective immune response. While these proteins are the natural entry points for the virus, they are also investigated as potential therapeutic targets for antiviral strategies aimed at blocking viral entry during acute infection. Heparan sulfate also serves as an initial attachment factor, concentrating the virus on the cell surface before it engages more specific entry receptors. The diversity of these receptors allows the virus to infect a wide range of cell types, contributing to the systemic nature of the immune response generated by the vaccine.
Viral attachment and receptor-mediated endocytosis
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