ArticleJournal of virology2012
Amino acid substitutions at positions 122 and 145 of hepatitis B virus surface antigen (HBsAg) determine the antigenicity and immunogenicity of HBsAg and influence in vivo HBsAg clearance.
Article in Journal of virology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 80 citations in OpenAlex.
- First identification of occult hepatitis B infection among ethnic minority students in Thai Nguyen, Vietnam.BMC infectious diseases · 2025Article
- Dual defects in HBsAg antigenicity and secretion caused by the C138R mutation in the S gene trigger occult hepatitis B virus infection.Journal of translational medicine · 2025Article
- Mechanisms underlying delayed loss of HBeAg and HBV DNA following HBsAg seroclearance in PEG-IFNα treated patients of chronic hepatitis B.Emerging microbes & infections · 2025Article
- Parenteral viral hepatitis among students in Da Nang, Vietnam, and insights into new hepatitis B virus genotype B classification.Scientific reports · 2025Article
- The Characteristic of HBV Quasispecies Is Related to Occult HBV Infection of Infants Born to Highly Viremic Mothers.Viruses · 2024Article
- Effect of S-region mutations on HBsAg in HBsAg-negative HBV-infected patients.Virology journal · 2024Article
- Role of S protein transmembrane domain mutations in the development of occult hepatitis B virus infection.Emerging microbes & infections · 2022Article
- HBV sL13H mutation impairs its surface antigen expression and ability to induce autophagy.Genes & diseases · 2022Article
- Efficient cellular and humoral immune response and production of virus-neutralizing antibodies by the Hepatitis B Virus S/preS1Frontiers in immunology · 2022Article
- In silico analysis of mutations associated with occult hepatitis B virus (HBV) infection in South Africa.Archives of virology · 2021Article
- Molecular Mechanisms during Hepatitis B Infection and the Effects of the Virus Variability.Viruses · 2021Review
- Detection of S-HBsAg Mutations in Patients with Hematologic Malignancies.Diagnostics (Basel, Switzerland) · 2021Article
- A putative amphipathic alpha helix in hepatitis B virus small envelope protein plays a critical role in the morphogenesis of subviral particles.Journal of virology · 2021Article
- Identification of Two Critical Neutralizing Epitopes in the Receptor Binding Domain of Hepatitis B Virus preS1.Journal of virology · 2021Article
- E2 Site Mutations in S Protein Strongly Affect Hepatitis B Surface Antigen Detection in the Occult Hepatitis B Virus.Frontiers in microbiology · 2021Article
- TLR5 activation in hepatocytes alleviates the functional suppression of intrahepatic CD8Immunology · 2020Article
- Review
- Article
- Hepatitis B and Pregnancy: Virologic and Immunologic Characteristics.Hepatology communications · 2020Review
- New Markers in Monitoring the Reactivation of Hepatitis B Virus Infection in Immunocompromised Hosts.Viruses · 2019Review
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Authors and funding
11 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A variety of amino acid substitutions, such as K122I and G145R, have been identified around or within the a determinant of hepatitis B surface antigen (HBsAg), impair HBsAg secretion and antibody binding, and may be responsible for immune escape in patients. In this study, we examined how different substitutions at amino acid positions 122 and 145 of HBsAg influence HBsAg expression, secretion, and recognition by anti-HBs antibodies. The results showed that the hydrophobicity, the presence of the phenyl group, and the charges in the side chain of the amino acid residues at position 145 reduced HBsAg secretion and impaired reactivity with anti-HBs antibodies. Only the substitution K122I at position 122 affected HBsAg secretion and recognition by anti-HBs antibodies. Genetic immunization in mice demonstrated that the priming of anti-HBs antibody response was strongly impaired by the substitutions K122I, G145R, and others, like G145I, G145W, and G145E. Mice preimmunized with wild-type HBsAg (wtHBsAg) or variant HBsAg (vtHBsAg) were challenged by hydrodynamic injection (HI) with a replication-competent hepatitis B virus (HBV) clone. HBsAg persisted in peripheral blood for at least 3 days after HI in mice preimmunized with vtHBsAg but was undetectable in mice preimmunized with wtHBsAg, indicating that vtHBsAgs fail to induce proper immune responses for efficient HBsAg clearance. In conclusion, the biochemical properties of amino acid residues at positions 122 and 145 of HBsAg have a major effect on antigenicity and immunogenicity. In addition, the presence of proper anti-HBs antibodies is indispensable for the neutralization and clearance of HBsAg during HBV infection.
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