Abstract
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.
Highlights
HIV-1 envelope (Env) gp120 is an important target for neutralizing antibody (Ab) responses against the virus
In the present study we examined immunogenicity of mutant gp120 in mice
Neutralizing activity was directed to V3 and other undefined neutralizing epitopes
Summary
HIV-1 envelope (Env) gp120 is an important target for neutralizing antibody (Ab) responses against the virus. 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. 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
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