Abstract

The elicitation of broadly neutralizing antibodies (bnAbs) is a key step for the development of a successful an HIV vaccine. Approximately 10-30% of HIV infected individuals do elicit broadly neutralizing antibodies that have been shown to protect against infection in macaque models. Isolation and epitope characterization of these antibodies reveal conserved regions of the virus envelope that can be targeted through vaccine design. The HIV envelope glycoprotein, gp120, is one of the most heavily glycosylated proteins known. The high density of glycans on gp120 limits their processing during biosynthesis, leading to the formation of a high-mannose patch on gp120. The density and heterogeneity of the glycans impede neutralizing antibody (NAb) recognition of Env but, paradoxically, some of the most potent broadly active bNAbs recognize epitopes involving this glycan shield. Here I will discuss our recent studies on the characterization of the HIV glycan shield and the development of HIV glycan-binding HIV bnAbs in a longitudinal cohort of HIV infected individuals.