Abstract
Background Eliciting effective antibody responses are key to the design of HIV vaccines. While the HIV envelope protein is highly immunogenic and provokes a high-titer antibody response during viral infection and experimental immunization, affinity-matured antibodies capable of neutralizing diverse HIV isolates are rarely elicited. While recent vaccine regimens have focused on DNA, viral vector, VLP, or attenuated virus vaccines, of increasing interest are improved recombinant envelope protein immunogens. Immunizations with trimeric gp140 proteins induce higher-titer neutralizing antibody responses and have structural benefits over monomeric gp120 immunizations. Novel approaches being taken for recombinant trimeric gp140 immunogens include the use of consensus and multi-clade gp140 trimers. A consideration for these synthetic proteins that is key to vaccine efficacy: do these proteins structurally represent a native trimeric envelope?
Highlights
Eliciting effective antibody responses are key to the design of HIV vaccines
While recent vaccine regimens have focused on DNA, viral vector, VLP, or attenuated virus vaccines, of increasing interest are improved recombinant envelope protein immunogens
The binding to other conformational monoclonal antibodies (MAbs), this suggests that while the consensus gp140s contain appropriately conformational monomers and are trimeric, the vast majority of the protein is not in a proper quaternary structure. These data suggest that it is important to fully assess structural differences of immunogens even though obvious phenotypic differences may not be present. These observations demonstrate the need to evaluate immunogens in a manner that allows the measurement of functional epitope exposure and solution conformation to assess the potential to elicit a potent, broadly-neutralizing antibody response
Summary
Eliciting effective antibody responses are key to the design of HIV vaccines. While the HIV envelope protein is highly immunogenic and provokes a high-titer antibody response during viral infection and experimental immunization, affinity-matured antibodies capable of neutralizing diverse HIV isolates are rarely elicited. While recent vaccine regimens have focused on DNA, viral vector, VLP, or attenuated virus vaccines, of increasing interest are improved recombinant envelope protein immunogens. Immunizations with trimeric gp140 proteins induce higher-titer neutralizing antibody responses and have structural benefits over monomeric gp120 immunizations. A consideration for these synthetic proteins that is key to vaccine efficacy: do these proteins structurally represent a native trimeric envelope?. The binding to other conformational MAbs, this suggests that while the consensus gp140s contain appropriately conformational monomers and are trimeric, the vast majority of the protein is not in a proper quaternary structure
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