Nature Hot Topic

Structure of antibody-bound gp120 epitope

The V1/V2 variable region of the gp120 envelope glycoprotein of HIV-1, with its extraordinary sequence diversity and N-linked glycosylation, exemplifies the ability of the virus to evade antibody recognition. It has also resisted structural determination. Now Peter Kwong and colleagues have determined the atomic-level structure of gp120 V1/V2 by using an antibody called PG9, which can neutralize most strains of HIV. Instead of being confounded by the N-linked glycan that shields most of gp120 from immune recognition, PG9 uses N-linked glycan for binding through a mechanism shared by a number of antibodies capable of effective HIV neutralization. The structure shows that the antibody recognizes glycopeptide conjugates and avoids diversity in V1/V2 by making sequence-independent interactions, such as hydrogen bonds.

Nature Volume 480 Issue 7377

Top Ten Highlights

Sign up for Nature Research e-alerts to get the lastest research in your inbox every week.

More Hot Topics

PrivacyMark System