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Significance Broadly neutralizing antibodies (bNAbs) can prevent new HIV-1 infections, but most are insufficiently broad or potent to protect from the diverse pool of circulating viruses. V2-glycan/apex bNAbs are exceptionally potent, but their breadth is limited. Their neutralizing activity requires tyrosine sulfation, a posttranslational modification that precludes their improvement with phage or yeast display. Here, we demonstrate the utility of a mammalian display approach whereby the heavy- and light-chain loci of a B cell line are CRISPR edited to encode the apex bNAb CAP256-VRC26.25. These loci were iteratively diversified through homology-directed repair with a library of DNA templates and through in vitro somatic hypermutation and selected with diverse envelope glycoprotein trimers. This approach can identify broader and more-potent apex bNAbs.

In vitro affinity maturation of broader and more-potent variants of the HIV-1–neutralizing antibody CAP256-VRC26.25