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Background We have previously engineered computationally-designed ‘epitope-scaffold’ constructs for the broadly neutralizing, MPER-specific antibody 4E10, consisting of the epitope grafted as a structural unit onto non-HIV scaffold proteins for optimal presentation during immunization. 4E10 epitope-scaffolds display dissociation constants for mature 4E10 ranging down to picomolar values and can elicit epitope-specific responses during immunization. Sera from immunized animals failed to potently neutralize HIV, at least partially due to differences between human and nonhuman germline repertoires. Successful use of epitopescaffolds as vaccine immunogens will require optimizing interactions with both the mature antibody target and appropriate precursors, while preserving or generating neutralization potency during maturation.

Functional properties of an ensemble of candidate germline-encoded precursors of the anti-MPER antibody 4E10