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On the prereceptor-engaged HIV-1 envelope glycoprotein (Env) spike, epitope access by the membrane-proximal external region (MPER)-directed broadly neutralizing antibodies 2F5 and 4E10 remains unresolved. Data on binding to cell surface Env and entry data using primary isolates suggest inaccessibility of the 2F5 and 4E10 epitopes on the viral spike prior to(More)
Background It is widely accepted that the elicitation of a broadly neutralizing antibody (bNAb) response will be crucial for an effective vaccine against HIV-1. Although a handful of bNAbs have been isolated, these antibodies recognize epitopes on the virus that have failed to elicit bNAb responses when incorporated into a diverse range of immunogens.(More)
Background The ability to elicit broadly cross-reactive neutralizing antibodies is a major challenge in the development of an HIV-1 vaccine capable of neutralizing broad array of viruses in circulation. Nevertheless, a number of HIV-1 infected donors have broadly neutralizing sera and a handful of broadly neutralizing monoclonal antibodies have been(More)
Conclusion Structural characterization and biochemical analysis of these antibodies have uncovered novel specificities to new glycan-dependent epitopes and reveal further mechanisms for viral neutralization. These new epitopes provide additional insights for neutralization of HIV-1 and how antibodies can bind and penetrate the glycan shield, a novel(More)
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