ArticleJournal of biomedical science2026
Crystal structure of the CD33/Fab-10C8 complex elucidates the mechanism of antibody antagonism in HBV-induced immunosuppression.
Article in Journal of biomedical science, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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Who cites it
1 citing paper in PubMed.
- Research Progress on Mechanisms of Immune Tolerance Induced by Hepatitis B Surface Antigen in Chronic HBV Infection.Journal of immunology research · 2026Review
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Authors and funding
5 authors.
Funding
Abstract
backgroundHepatitis B virus (HBV) infection persists through immune evasion strategies, including engagement of the inhibitory receptor CD33 (Siglec-3) by α2,6-linked sialoglycans on HBsAg. This interaction induces ITIM phosphorylation and SHP-1/2 recruitment, dampening myeloid cell activation. The monoclonal antibody 10C8 has been identified as a potent antagonist of CD33, but the structural basis for its inhibitory activity remains unclear.
methodsWe determined the 3.2 Å crystal structure of the human CD33 extracellular domain (CD33-ECD) in complex with the Fab fragment of 10C8 (Fab-10C8). The stoichiometry and assembly of the complex in solution were validated by size-exclusion chromatography and analytical ultracentrifugation (AUC). Structural comparisons with apo CD33 were performed to assess potential Fab-induced conformational changes, and buried surface area analyses were conducted to characterize binding interfaces.
resultsThe structure reveals a 2:2 stoichiometry complex comprising two CD33-ECD molecules and two Fab-10C8 fragments, consistent with the 157 kDa molecular mass determined by AUC. Each Fab engages the V-set domain through extensive complementarity-determining region (CDR) interactions, burying ~612 Å
conclusionsThis study provides the structural insight into antibody-mediated inhibition of CD33. By locking CD33 into a sterically occluded, signaling-refractory conformation, 10C8 effectively reverses HBV-induced immunosuppression, thereby restoring host antiviral activity. These findings establish a structural framework for rational design of Siglec-targeted immunotherapies against chronic viral infections and other immune regulatory disorders.
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