ArticleBriefings in bioinformatics2026
Intelligent antigen design combined with yeast display enhances targeted immune responses.
Article in Briefings in bioinformatics, 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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Abstract
Inducing strong and targeted humoral immune responses, a central goal of next-generation vaccine development, involves a complex series of interconnected steps. However, a comprehensive study that addresses and integrates all steps is still missing. Here, we present a study that addresses these steps to elicit precise neutralizing antibody (nAb) responses targeting focused epitope motifs. We present a new protein design model called EpiTopoFold for constructing a topology that precisely accommodates and stabilizes the epitope motif. After ten thousand in silico simulations, we designed a de novo antigen L9, which structurally incorporated three epitope motifs from the receptor-binding domain (RBD) of the coronavirus spike protein. To enhance antigen immunogenicity, we displayed L9 on the surface of yeast (Saccharomyces cerevisiae). In mice, the yeast-displayed L9 induced stronger and broader neutralizing responses than the alum-adjuvanted L9 or commercial RBD protein. Together, this work establishes a proof-of-concept framework that integrates intelligent antigen design with yeast surface display to enable robust and targeted nAb responses for next-generation vaccine development.
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