Autologous Antibody Responses to an HIV Envelope Glycan Hole Are Not Easily Broadened in Rabbits
Yuhe R. Yang, Laura E. McCoy, Marit J. van Gils, Raiees Andrabi, Hannah L. Turner, Meng Yuan, Christopher A. Cottrell, Gabriel Ozorowski, James E. Voss, Matthias Pauthner, Thomas M. Polveroni, Terrence Messmer, Ian A. Wilson, Rogier W. Sanders, Dennis R. Burton, Andrew B. Ward
Abstract
A glycan hole is one of the most dominant autologous neutralizing epitopes targeted on BG505 and B41 SOSIP trimer-immunized rabbits. Our high-resolution cryo-electron microscopy (cryoEM) studies of B41 in complex with a B41-specific antibody complex elucidate the molecular basis of this strain-specific glycan hole response. We conclude that even for the immunodominant glycan hole shared between BG505 and B41, the prospect of designing prime-boost immunogens remains difficult.