Literature DB >> 28279830

Effects of partially dismantling the CD4 binding site glycan fence of HIV-1 Envelope glycoprotein trimers on neutralizing antibody induction.

Ema T Crooks1, Keiko Osawa1, Tommy Tong1, Samantha L Grimley1, Yang D Dai2, Robert G Whalen3, Daniel W Kulp4, Sergey Menis4, William R Schief5, James M Binley6.   

Abstract

Previously, VLPs bearing JR-FL strain HIV-1 Envelope trimers elicited potent neutralizing antibodies (nAbs) in 2/8 rabbits (PLoS Pathog 11(5): e1004932) by taking advantage of a naturally absent glycan at position 197 that borders the CD4 binding site (CD4bs). In new immunizations, we attempted to improve nAb responses by removing the N362 glycan that also lines the CD4bs. All 4 rabbits developed nAbs. One targeted the N197 glycan hole like our previous sera. Two sera depended on the N463 glycan, again suggesting CD4bs overlap. Heterologous boosts appeared to reduce nAb clashes with the N362 glycan. The fourth serum targeted a N362 glycan-sensitive epitope. VLP manufacture challenges prevented us from immunizing larger rabbit numbers to empower a robust statistical analysis. Nevertheless, trends suggest that targeted glycan removal may improve nAb induction by exposing new epitopes and that it may be possible to modify nAb specificity using rational heterologous boosts.
Copyright © 2017 Elsevier Inc. All rights reserved.

Entities:  

Keywords:  Antibody; Env, trimer; Glycan; Gp120, neutralization; HIV-1; VLP; Vaccine

Mesh：

Substances：

Year:  2017        PMID： 28279830      PMCID： PMC5895097          DOI： 10.1016/j.virol.2017.02.024

Source DB:  PubMed          Journal:  Virology        ISSN： 0042-6822            Impact factor:   3.616


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