Young Do Kwon

TL;DR: The identification of three broadly neutralizing antibodies, isolated from an HIV-1–infected individual, that exhibited great breadth and potency of neutralization and were specific for the co-receptor CD4-binding site of the glycoprotein 120 (gp120), part of the viral Env spike.

TL;DR: The structure of V1/V2 in complex with PG9 is reported, identifying a paradigm of antibody recognition for highly glycosylated antigens, which—with PG9—involves a site of vulnerability comprising just two glycans and a strand.

TL;DR: Crystallized fully glycosylated Env trimers from clades A, B, and G reveal a diversity in oligosaccharide affinity and a requirement for accommodating glycans among known broadly neutralizing antibodies that target the glycan-shielded trimer.

TL;DR: The crystal structure of an HIV-1 gp120 core with intact gp41-interactive region in its CD4-bound state is determined, compared to unliganded and antibody-bound forms to identify structurally invariant and plastic components, and ligand-oriented cryoelectron tomograms are used to define component mobility in the viral spike context.

TL;DR: Antigenicity-guided structural design can be used both to delineate mechanism and to fix conformation, with DS-Env trimers in virus-like-particle and soluble formats providing a new generation of vaccine antigens.