Structures of Natively-Glycosylated HIV-1 Envelope Trimers Define Antibody-Mediated Neutralization of HIV-1
- Creators
- Barnes, Christopher O.
Abstract
Broadly neutralizing antibodies (bNAbs) isolated from HIV-1 infected individuals inform vaccine design and are potential therapeutic agents. However, developing bNAbs with increased efficacy requires understanding how antibodies interact with the native oligomannose and complex-type N-glycan shield that hides most protein epitopes on HIV-1 envelope (Env). We present single-particle cryoEM structures of natively-glycosylated Env trimers complexed with newly identified bNAbs that target distinct epitopes on the surface of Env. A 3.3Å cryoEM structure of Env bound to SF12, an antibody that recognizes a glycan-dominated epitope on Env's silent face, revealed distinct N-glycan conformations across Env protomers, demonstrating intra-Env glycan heterogeneity. Insights from these antibody-Env complex structures have facilitated our understanding of bNAb-glycan interactions critical for their potential use in HIV-1 prevention, therapy, and vaccine development.
Additional Information
© 2020 Biophysical Society. Available online 7 February 2020.Additional details
- Eprint ID
- 101989
- DOI
- 10.1016/j.bpj.2019.11.211
- Resolver ID
- CaltechAUTHORS:20200319-084323389
- Created
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2020-03-19Created from EPrint's datestamp field
- Updated
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2021-11-16Created from EPrint's last_modified field