作者: Bartek Nogal , Laura E. McCoy , Marit J. van Gils , Christopher A. Cottrell , James E. Voss
DOI: 10.1101/831008
关键词:
摘要: To date, immunization studies of rabbits with the BG505 SOSIP.664 HIV envelope glycoprotein trimers have revealed 241/289 glycan hole as dominant neutralizing antibody epitope. Here, we isolated monoclonal antibodies from a rabbit that did not exhibit hole-dependent autologous serum neutralization. The compete previously hole-specific but N332 supersite broadly antibodies. A high resolution cryoEM structure one in complex trimer demonstrated that, while epitope recognized overlapped by contacting GDIR motif at base V3, primary contacts were located variable V1 loop. These data suggest strain-specific responses to may interfere and vaccine immunogens require engineering minimize these off-target or steer them toward more desirable pathway.