The isolation of highly potent antibodies that recognize a broad diversity of HIV-1 clades has opened up tremendous opportunities for enhancing our understanding of how to neutralize HIV-1. Crystal structures of antibodies have been determined that recognize different epitopes including the gp41 membrane proximal region, the gp120 receptor binding site and clusters of high mannose glycans on gp120. New human monoclonal antibodies (PG and PGT families) have been discovered recently that potently neutralize 70-90% of HIV-1 isolates across all clades. These exciting new antibodies were derived from direct functional screening of B cells from IAVI protocol G donors (Theraclone/Monogram) and are unusually potent. These antibodies have unique features and bind to novel epitopes that include the glycan shield as well as segments of gp120. Structural characterization of these broadly neutralizing antibodies, as well as identification of their glycan epitopes on HIV-1 Env, provide tremendous insights for neutralization of HIV-1 and can now be used for structure-assisted vaccine design.This work was carried out in collaboration with the Burton lab at TSRI and IAW was supported by NIH GM46192, the International AIDS Vaccine Initiative (IAVI) and NIH AI84817.

Broadly neutralizing antibodies that recognize the HIV-1 Env glycan shield

244th National Meeting (2012)

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