Improving immunogenicity of HIV-1 envelope gp120 by glycan removal and immune complex formation

Background HIV-1 envelope (Env) gp120 is an important target for neutralizing antibody (Ab) responses against the virus. However, developing gp120 vaccines that elicit potent and broad neutralizing Abs has proven to be a formidable challenge. The envelope gp120 is highly glycosylated and carbohydrate moieties play an important role in modulation of immunobiological property of HIV-1 Env gp120. Previously, removal of a specific N-linked glycan at residue 448 by N to Q mutation (N448Q) has been found to enhance in vitro antigenicity of neutralizing epitopes in the V3 loop. In the present study we examined immunogenicity of mutant gp120 in mice.