ArticleCurrent issues in molecular biology2026
A Multi-Model Strategy for Optimizing Hepatitis B Virus preS1 Epitope Recognition by the Antibody HzKR127.
Article in Current issues in molecular biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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7 authors.
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Abstract
Functional cure of chronic hepatitis B virus (HBV) infection remains a significant challenge, making viral-entry-blocking antibodies a promising antiviral strategy. Here, we developed a structure-guided computational workflow for affinity-enhancing candidate mutations at the interface between the humanized neutralizing antibody HzKR127 and the HBV preS1 peptide epitope. Based on the crystal structure of the HzKR127-preS1 complex, we performed single-site saturation mutagenesis across the paratope, evaluating variants with a consensus effect score integrated from seven computational models. Benchmarking against published alanine scanning data showed that our consensus score effectively identified major-affinity-loss residues, achieving ROC AUC values of 0.81 and 0.84 for residue-level and site-level predictions, respectively. Mutational profiling revealed distinct asymmetric mutational responses, with broad intolerance on the preS1 side and localized favorable substitutions within antibody CDRs. Multilevel prioritization identified 26 antibody-side candidates, 17 of which showed improved HADDOCK refinement scores compared to the wild type. In particular, the H:D97W/F/Y substitutions presented the strongest structural rationale for enhancing improved interfacial packing through aromatic hydrophobic contacts with preS1 Phe10. These findings provide a prioritized list of candidates for experimental validation and a practical framework for the rational optimization of antibodies targeting functionally constrained viral epitopes.
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