EMD-28910

Single-particle
4.1 Å
EMD-28910 Deposition: 20/11/2022
Map released: 27/09/2023
Last modified: 20/11/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-28910

Glycan-Base ConC Env Trimer

EMD-28910

Single-particle
4.1 Å
EMD-28910 Deposition: 20/11/2022
Map released: 27/09/2023
Last modified: 20/11/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Human immunodeficiency virus 1
Sample: HIV-1 Consensus C Env trimer with glycan covered base
Fitted models: 8f7t (Avg. Q-score: 0.351)

Deposition Authors: Olia AS, Kwong PD
Soluble prefusion-closed HIV-envelope trimers with glycan-covered bases.
PUBMED: 37554450
DOI: doi:10.1016/j.isci.2023.107403
ISSN: 2589-0042
Abstract:
Soluble HIV-1-envelope (Env) trimers elicit immune responses that target their solvent-exposed protein bases, the result of removing these trimers from their native membrane-bound context. To assess whether glycosylation could limit these base responses, we introduced sequons encoding potential N-linked glycosylation sites (PNGSs) into base-proximal regions. Expression and antigenic analyses indicated trimers bearing six-introduced PNGSs to have reduced base recognition. Cryo-EM analysis revealed trimers with introduced PNGSs to be prone to disassembly and introduced PNGS to be disordered. Protein-base and glycan-base trimers induced reciprocally symmetric ELISA responses, in which only a small fraction of the antibody response to glycan-base trimers recognized protein-base trimers and vice versa. EM polyclonal epitope mapping revealed glycan-base trimers -even those that were stable biochemically- to elicit antibodies that recognized disassembled trimers. Introduced glycans can thus mask the protein base but their introduction may yield neo-epitopes that dominate the immune response.