ArticlebioRxiv : the preprint server for biology2025
Divalent HIV-1 gp120 Immunogen Exhibits Selective Avidity for Broadly Neutralizing Antibody VRC01 Precursors.
Article in bioRxiv : the preprint server for biology, 2025. 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
A major goal for the vaccine field is elicitation of broadly neutralizing antibodies (bnAbs) against pathogens that exhibit extensive antigenic diversity. 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 HIV spike protein. This was accomplished by covalently linking two HIV-1 gp120 antigens to a complementary antibody and crosslinking the light chains. The divalent immunogen exhibits a higher affinity for VRC01-class antibodies compared to a non-Fab-Fab-crosslinked control, likely due to antigen pre-organization limiting the entropic penalty for divalent binding. Importantly, this immunogen exhibited divalent binding to VRC01 and monovalent binding to a non-CD4bs Ab, A32 - a characteristic we refer to as "selective avidity." This report supports future Highlights: We designed a rigid divalent immunogen containing two copies of gp120 antigenThe gp120s are positioned to bind divalently to both Fabs of a target B cell receptorThe immunogen binds monovalently to non-target B cell receptorsThis "selective avidity" effect may be used for immune focusing.
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