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The preS1 protein is a domain of the large envelope (surface) protein (L-HBsAg) of the hepatitis B virus (HBV). It plays a critical role in viral infectivity, host cell entry, and immune recognition. The N-terminal segment of preS1 contains a myristoylation site at glycine-2 and an essential receptor-binding site (RBS), mediating attachment to human hepatocytes via interaction with sodium taurocholate co-transporting polypeptide (NTCP), which serves as the primary cellular receptor for HBV entry.
preS1 mediates attachment to human hepatocytes via interaction with sodium taurocholate co-transporting polypeptide (NTCP), which serves as the primary cellular receptor for HBV entry. Myristoylated synthetic peptides specific for the N-terminal [pre-S1] domain can bind to hepatocyte plasma membranes and block infection in vitro and in vivo. Mutations within key hydrophobic regions of preS1 abolish both infectivity and membrane fusion capability.
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