Residues critical for duck hepatitis B virus neutralization are involved in host cell interaction.

摘要: To date, no detailed analysis of the neutralization properties duck hepatitis B virus (DHBV) has been reported, and it is not clear whether any known epitopes correspond to viral receptor binding site or sequences involved in cell entry pathway. We demonstrate here that antibodies directed against two overlapping peptides (amino acids 83 97 93 107), covering most DHBV pre-S neutralizing epitopes, both inhibit primary hepatocytes neutralize infectivity. An extensive mutagenesis motif 88WTP90, which shortest sequence epitope recognized by virus-neutralizing monoclonal antibody (MAb) 900 was performed order define amino these interactions. Single point mutations within this affected neither replication nor infectivity but abolished MAb completely. Interestingly, mutants with three consecutive residue replacements (SIP SIH) retained competence were longer infectious. The loss SIH SIP mutant particles associated significantly reduced could be rescued trans complementation wild-type protein. Taken together, results indicate each acid 88WTP90 critical for recognition replacement first all residues strongly reduces interaction abrogates These data imply contains key are host cell.