Abstract
An ideal HIV-1 vaccine would induce broadly neutralising antibodies but such antibodies are rarely induced. Could “holes” in the naive B-cell repertoire account for the lack of antibodies that bind conserved, broadly neutralising epitopes in the HIV-1 envelope? New research does not support this possibility but shows instead that sugars on HIV-1 envelope proteins prevent them binding to the unmutated ancestor antibodies of existing broadly neutralising antibodies to the HIV-1 envelope. Moreover, immunisation of rhesus macaques with deglycosylated HIV-1 gp140 envelope protein enhances the induction of antibodies to a broadly neutralising gp41 epitope.
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