Abstract
Aim: We analyzed the role of mutations on the conformational structure of hepatitis B surface antigen (HBsAg) among HIV-1 positive patients who were infected with occult hepatitis B. Methods: The effects of the potential impact of amino-acid substitutions on the 3D structures of the HBsAg and molecular ducking were investigated using bioinformatics software. Results: Mutations classified in seven groups in accordance with their positions in occult hepatitis B virus infection patients. Some substitutions of residues could linearize the ‘a’ determinant loops. The affinity of binding in mutant HBsAg structures to MAb 12 was lower compared with the wild ones. T123I and P127L substitutions were undergone decrease in HBsAg antigenicity. Conclusion: These findings could be beneficial for a better understanding of hepatitis B virus antigen/antibody interactions.
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