Autologous Antibody Responses to an HIV Envelope Glycan Hole Are Not Easily Broadened in Rabbits
Copyright policy )Autologous Antibody Responses to an HIV Envelope Glycan Hole Are Not Easily Broadened in Rabbits
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.
- Harvard University United States
- Amsterdam UMC Netherlands
- Cornell University United States
- Massachusetts Institute of Technology United States
- University College London United Kingdom
Glycosylation, Immunodominant Epitopes, Protein Conformation, Cryoelectron Microscopy, env Gene Products, Human Immunodeficiency Virus, Glycan hole, HIV Antibodies, Antibodies, Neutralizing, SOSIP, HEK293 Cells, Interferometry, Rabbit immunization, Neutralization Tests, Polysaccharides, Vaccines and Antiviral Agents, HIV-1, Animals, Humans, Autologous neutralization, Epitope, Monoclonal antibodies, Rabbits
Glycosylation, Immunodominant Epitopes, Protein Conformation, Cryoelectron Microscopy, env Gene Products, Human Immunodeficiency Virus, Glycan hole, HIV Antibodies, Antibodies, Neutralizing, SOSIP, HEK293 Cells, Interferometry, Rabbit immunization, Neutralization Tests, Polysaccharides, Vaccines and Antiviral Agents, HIV-1, Animals, Humans, Autologous neutralization, Epitope, Monoclonal antibodies, Rabbits
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