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TitleCharacterisation of plasmablast-derived HBsAg-specific antibody and its structural basis for binding to native HBsAg dimer.
Journal, issue, pagesGut, Year 2026
Publish dateFeb 9, 2026
AuthorsBin Ju / Zhouqing Liu / Hu Yan / Yong Liu / Lu Zhang / Xiangyang Ge / Xin Wang / Zhu Si / Bing Zhou / Qing Fan / Miao Wang / Yuxiao Li / Wenlong Lai / Jianhui Gan / Haiyan Wang / Juanjuan Zhao / Yuchen Xia / Maofu Liao / Zheng Zhang /
PubMed AbstractBACKGROUND: Plasmablast-derived HBV surface antigen (HBsAg)-specific monoclonal antibody (mAb) and structural basis for binding to native HBsAg are poorly known.OBJECTIVE: We aimed to identify ...BACKGROUND: Plasmablast-derived HBV surface antigen (HBsAg)-specific monoclonal antibody (mAb) and structural basis for binding to native HBsAg are poorly known.
OBJECTIVE: We aimed to identify plasmablast-derived HBsAg-specific mAbs, evaluate their antiviral activities and resolve their structure for binding to native HBsAg.
DESIGN: A previously vaccinated volunteer was enrolled in this study, who was boosted with a dose of recombinant hepatitis B vaccine and donated the blood sample. Activated plasmablasts were sorted from fresh peripheral blood mononuclear cells and mAbs were expressed. Their gene features, cross-genotypic binding activities and antiviral functions in vitro and in vivo were comprehensively analysed. The cryo-electron microscopy (cryo-EM) was used to determine the structure of representative mAb bound to the native HBsAg.
RESULTS: In this study, we cloned a series of HBsAg-specific mAbs directly from clonally expanded plasmablasts from a vaccinated individual. Most of the mAbs displayed cross-reactivities of binding to different genotype HBsAg proteins and antiviral functions such as neutralisation and antibody-dependent cellular phagocytosis. These human anti-HBsAg mAbs, especially SY-4-class and SY-23-class, could be good candidates for antibody drugs. The cryo-EM structure of SY-23 bound to the dimeric HBsAg was determined, revealing its binding mechanism and unprecedented structural detail of the major antigenic loop (AGL) of HBsAg.
CONCLUSION: Overall, our work has uncovered the diverse gene features and varied anti-HBV activities of plasmablast-derived mAbs, providing a series of antibody drug candidates and the long-sought-after atomic model of AGL has paved the way for a wholistic characterisation of the AGL's dynamic conformation during HBV infection and immune response.
External linksGut / PubMed:41663152
MethodsEM (single particle)
Resolution4.0 Å
Structure data

64142

9ugo

EMDB-64142, PDB-9ugo:
Cryo-EM structure of the HBsAg dimer and Complex with Fab
Method: EM (single particle) / Resolution: 4.0 Å

Source
  • homo sapiens (human)
  • hepatitis b virus genotype a
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / HBV antigen / dimer / Fab / complex / VIRAL PROTEIN-IMMUNE SYSTEM complex

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