Abstract
Background The generation of globally relevant HIV-1 immunogens mimicking native, trimeric Envelope (Env) structure, remains a major challenge for HIV-1 vaccine development. We identified a mosaic Env sequence, originally designed to optimize cellular immunologic coverage of global HIV-1 sequence diversity, which was capable of forming biochemically stable trimers. We assessed this mosaic Env gp140 trimer in guinea pig immunogenicity studies compared to our previously reported biochemically stable C97ZA012 (clade C) trimer. Methods
Highlights
The generation of globally relevant HIV-1 immunogens mimicking native, trimeric Envelope (Env) structure, remains a major challenge for HIV-1 vaccine development
We identified a mosaic Env sequence, originally designed to optimize cellular immunologic coverage of global HIV-1 sequence diversity, which was capable of forming biochemically stable trimers
Stabilized mosaic gp140 trimer exhibited a single band by Western blotting, single peak by size-exclusion chromatography both after production, a freeze-thaw cycle and 7day incubation at 4oC
Summary
The generation of globally relevant HIV-1 immunogens mimicking native, trimeric Envelope (Env) structure, remains a major challenge for HIV-1 vaccine development. We identified a mosaic Env sequence, originally designed to optimize cellular immunologic coverage of global HIV-1 sequence diversity, which was capable of forming biochemically stable trimers. We assessed this mosaic Env gp140 trimer in guinea pig immunogenicity studies compared to our previously reported biochemically stable C97ZA012 (clade C) trimer
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