An integrative structural and biophysical workflow indicates engagement of VRC01 germline antibodies can occur with a gp120 426c core construct containing all wild-type N-linked glycosylation sites, including the Asn276 glycan.

Structural and computational analyses of germline antibody/HIV-1 gp120 complexes provide both general principles relevant to the unusual evolution of potent CD4-binding site antibodies and guidelines for structure-based immunogen design.

Signal-peptide cleavage of HIV-1 envelope glycoprotein is delayed because of alpha-helical structure covering the cleavage site, effecting early cleavage alters the folding pathway and resulting in localized misfolding and reduced viral fitness.

Lymph node gp120 specific B cells extract locally injected HIV-1 gp120 from SIGN-R1 positive macrophages that line the subcapsular sinus overlying the lymph node interfollicular channels.

Rhesus macaques can develop broadly neutralizing antibodies (bNAbs) against the V3-glycan patch of Env that resembles human V3/N332 bNABs.

HIV escapes human immune pressure through a single mutation in V2 domain of envelope protein leading to emergence of mutant-specific broadly reactive antibodies, a phenomenon recapitulated in combinatorial vaccine design.

Targeted SOCS3 null mice reveal that maturation of cortical bone comprises both pore closure and accumulation of high density bone, requiring local suppression of gp130-STAT3 in osteocytes and subsequent osteoclastogenesis.

Strategies to enhance Tfh cells for HIV-vaccine antibody persistence and protection is pivotal for vaccine success.

Single particle cryoEM structure of antibody complex with HIV-1 envelope trimer reveals new mode of asymmetric recognition of trimer apex.

Using single-cell CITE-seq to implicate monocytes as the cellular origin of a protective HIV vaccine gene signature.