Characterisation of the hepatitis B virus cross-species transmission pattern via Na+/taurocholate co-transporting polypeptides from 11 New World and Old World primate species.
Abstract: An exchange from arginine to glycine (as present in humans and great apes) at this position (R158G) alone was sufficient to achieve full transport-competing HBV myr-preS1-peptide binding and susceptibility for HBV/HDV infection.
Mutation of arginine residues to avoid non-specific cellular uptakes for hepatitis B virus core particles.
Result: The replacement of the R residues at aa 157, 158 and 159 (R157G, R158G and R159G) showed a comparatively higher cell binding ability compared with other HBc mutants.