Abstract
The highly variable and heavily glycosylated surface of the HIV-1 Envelope (Env) trimer present formidable challenges for eliciting broad and potent responses to the virus. While the overwhelming majority of broadly neutralizing antibodies described to date target the pre-fusion closed form of Env, a few neutralizing antibodies, including the broadly neutralizing antibody b12, target an open state of the trimer known as occluded-open. In the occluded-open state, glycans are splayed outwards and conserved residues that are inaccessible on the closed state are revealed. Here, I present a strategy for stabilizing this otherwise transient state of the trimer with the goal of eliciting antibodies that target the unexplored landscape of cryptic epitopes present on the occluded-open state of HIV-Env.
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