Crystal structure of the CD33/Fab-10C8 complex elucidates the mechanism of antibody antagonism in HBV-induced immunosuppression
Yi-Hung Yeh, Min-Guan Lin, Pei-Shan Sung, Shie-Liang Hsieh, Chwan-Deng Hsiao · 2026
Read Crystal structure of the CD33/Fab-10C8 complex elucidates the mechanism of antibody antagonism in HBV-induced immunosuppression by Yi-Hung Yeh, Min-Guan Lin, Pei-Shan Sung, Shie-Liang Hsieh, Chwan-Deng Hsiao (2026) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-13220637.txt.
Description
Yi-Hung Yeh and colleagues solve the structure of an antibody locked onto the brake CD33 in a 2026 study. Hepatitis B virus persists partly by engaging CD33, a receptor on myeloid immune cells whose sugar-binding surface, grabbed by viral proteins, triggers an off signal. The monoclonal antibody 10C8 blocks that suppression, but nobody knew how.
The structure, at 3.2 angstroms, shows two receptor molecules clasped by two antibody fragments, an assembly whose weight matched measurements. The antibody grips the receptor's outer domain next to, not inside, the sugar-binding pocket, covering surface to bar the virus protein from docking. Binding squeezes the receptor pair into a tighter angle than its relaxed state, a geometry preventing the clustering the off signal needs. The authors frame 10C8 as a clamp that holds the brake in a signaling-dead pose, restoring antiviral activity, and offer the structure as a template for designing antagonists.
Catalog record
| CREATOR | Yi-Hung Yeh, Min-Guan Lin, Pei-Shan Sung, Shie-Liang Hsieh, Chwan-Deng Hsiao |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 49 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |