Han Gao

TL;DR: Structural analysis of an HIV antibody reveals residues important for neutralization breadth and potency, which indicate that gp120 inner domain and bridging sheet residues should be included in immunogens to elicit CD4bs antibodies.

TL;DR: A new site of vulnerability is defined by solving structures of bNAb 8ANC195 complexed with monomeric gp120 by X-ray crystallography and trimeric Env by electron microscopy, making 8ANC 195 the first donor-derived anti-HIV-1 bNAB with an epitope spanning both Env subunits.

TL;DR: 8ANC195 binding partially closed the CD4-bound trimer, confirming structural plasticity of Env by revealing a previously unseen conformation, and 8ANC195's ability to bind different Env conformations suggests advantages for potential therapeutic applications.

TL;DR: To activate B cells that express precursors of broadly neutralizing antibodies within polyclonal repertoires, an immunogen is developed, RC1, that facilitates the recognition of the variable loop 3 (V3)-glycan patch on the envelope protein of HIV-1 and elicits specific serological responses in mice and macaques.

TL;DR: Mutating anti–HIV-1 broadly neutralizing antibodies increases their breadth and reduces pathways for viral escape through mutation.