Exploring New Methods to Dissect Site-Specific Differences in the N-glycosylation Patterns of HIV-1 Envelope Protein Gp120 in Chronic and Transmitted/Founder Virions
Abstract
The extraordinary genetic diversity of HIV variants and their differences in glycosylation of surface protein gp120 have resulted in 30+ years of research with no universal vaccine. Despite this, most transmission events occur from a single transmitted founder virus (T/F). Glycan-binding proteins (lectins) are also thought to be important for HIV’s transmission. This study set out to analyze differences in gp120 glycosylation between T/F and chronic HIV strains using mass spectrometry, site-specific computational analyses, and lectin microarrays. Current results indicate gp120 glycosylation and lectin binding can differ significantly between strains, which may correlate with the differential transmission fitness of the strains. Ultimately, this study has unveiled site-specific patterns of glycosylation that can be investigated further as novel vaccine targets.