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Conformational Analysis of Hepatitis B Virus Surface Antigen Mutations Among Hiv-Positive Patients Diagnosed With Occult Hepatitis B Virus Publisher



Poortahmasebi V1, 2, 3 ; Poorebrahim M4 ; Sadeghi A5 ; Abazari MF6 ; Sadredinamin M7 ; Hasanpoor E8 ; Jazayeri SM6, 9
Authors
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Authors Affiliations
  1. 1. Infectious and Tropical Diseases Research Center, Tabriz University of Medical Sciences, Tabriz, Iran
  2. 2. Liver and Gastrointestinal Disease Research Center, Tabriz University of Medical Sciences, Tabriz, Iran
  3. 3. Department of Virology, Faculty of Medicine, Tabriz University of Medical Sciences, Tabriz, Iran
  4. 4. Department of Medical Biotechnology, School of Advanced Technologies in Medicine, Tehran University of Medical Sciences, Tehran, Iran
  5. 5. Iranian Tissue Bank and Research Center, Tehran University of Medical Sciences, Tehran, Iran
  6. 6. Research Center for Clinical Virology, Tehran University of Medical Sciences, Tehran, Iran
  7. 7. Department of Microbiology, School of Medicine, Shahid Beheshti University of Medical Sciences, Tehran, Iran
  8. 8. School of Electrical and Computer Engineering, University College of Engineering, University of Tehran, Tehran, Iran
  9. 9. Hepatitis B Molecular Laboratory, Department of Virology, Tehran University of Medical Sciences, Tehran, Iran

Source: Future Virology Published:2020


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. © 2020 Future Medicine Ltd.
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