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ABSTRACT: Background
A major goal for the vaccine field is the elicitation of broadly neutralizing antibodies (bnAbs) against pathogens that exhibit extensive antigenic diversity.Methods
In this study, we designed a rigid divalent immunogen for high avidity binding to the bnAb, VRC01, which targets the CD4 binding site (CD4bs) of the HIV spike protein. This was accomplished by covalently linking two HIV-1 gp120 antigens to a complementary antibody and crosslinking the light chains. Binding kinetics were analyzed using a novel gel shift assay and surface plasmon resonance.Results
The rigid divalent immunogen exhibits a higher affinity for VRC01-class antibodies compared to a flexible control, likely due to antigen pre-organization limiting the entropic penalty for divalent bin
SUBMITTER: Bailey R
PROVIDER: S-EPMC12846365 | biostudies-literature | 2026 Jan
REPOSITORIES: biostudies-literature