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Updated: Jan 10, 2026

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding
Published on: September 15, 2010
Orphan broadly RBD-binding antibodies annotate three remaining conserved RBD epitopes along SARS-CoV-2 evolution.
Minxiang Xie1, Yinong Qiu1, Xiaoyu Zhao2,3
1Key Laboratory of Medical Molecular Virology (MOE/NHC/CAMS), Shanghai Institute of Infectious Disease and Biosecurity, Shanghai Frontiers Science Center of Pathogenic Microorganisms and Infection, Shanghai Fifth People's Hospital, Shanghai Key Laboratory of Medical Epigenetics, Institutes of Biomedical Sciences, School of Basic Medical Sciences, Fudan University, Shanghai, China.
Scientists discovered broadly binding antibodies (bbAbs) that target conserved regions of the SARS-CoV-2 spike protein, offering potential protection against current and future variants. These antibodies show promise for developing broadly protective vaccines.
Area of Science:
- Immunology
- Virology
- Structural Biology
Background:
- The receptor-binding domain (RBD) of SARS-CoV-2 spike protein evolves, leading to antibody evasion.
- The persistence of conserved RBD epitopes and antibody responses against them across variants remain unclear.
Purpose of the Study:
- To identify conserved SARS-CoV-2 RBD epitopes and antibodies that can neutralize emerging variants.
- To investigate the potential of these antibodies for developing broadly protective vaccines.
Main Methods:
- Heterogeneous double-bait single B-cell sorting strategy.
- Identification and characterization of broadly binding antibodies (bbAbs).
- In vivo passive transfer studies in a hamster model and structural analyses.
Main Results:
- A subset of bbAbs demonstrated broad-spectrum RBD binding, including recognition of SARS-CoV-1 and variants like EG.5.1, BA.2.86, JN.1, and KP.2/3.
- bbAbs showed elevated somatic hypermutation but were infrequently derived from clonally expanded B lymphocytes.
- Passive transfer of bbAbs reduced viral infection in hamsters; structural analyses identified three conserved RBD epitopes.
Conclusions:
- Conserved and immunogenic RBD conformations exist and can be targeted by bbAbs.
- These findings suggest potential targets for future mutational pressure and provide a foundation for broadly protective vaccine development.
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