X-ray and EM structures of a natively glycosylated HIV-1 envelope trimer
Abstract
The structural and biochemical characterization of broadly neutralizing anti-HIV-1 antibodies (bNAbs) has been essential in guiding the design of potential vaccines to prevent infection by HIV-1. While these studies have revealed critical mechanisms by which bNAbs recognize and/or accommodate N-glycans on the trimeric envelope glycoprotein (Env), they have been limited to the visualization of high-mannose glycan forms only, since heterogeneity introduced from the presence of complex glycans makes it difficult to obtain high-resolution structures. 3.5 and 3.9 Å resolution crystal structures of the HIV-1 Env trimer with fully processed and native glycosylation were solved, revealing a glycan shield of high-mannose and complex-type N-glycans that were used to define the complete epitopes of two bNAbs. Here, the refinement of the N-glycans in the crystal structures is discussed and comparisons are made with glycan densities in glycosylated Env structures derived by single-particle cryo-electron microscopy.
Additional Information
© 2017 International Union of Crystallography. Received 4 August 2017; Accepted 19 September 2017. We thank Christopher O. Barnes for careful proofreading and useful discussions while writing the manuscript. We also thank the beamline staff at Stanford Synchrotron Radiation Lightsource (SSRL) and Jens Kaiser and the Molecular Observatory at Caltech for assistance with data processing, Zhiheng Yu, Chuan Hong and Rick Huang (Janelia Farm) for assistance with cryo-EM data collection and motion correction, and Alasdair McDowall and Songye Chen for training in cryo-EM techniques and data processing. This research was supported by National Institutes of Health Grant 2 P50 GM082545-06 (to PJB) and National Institute Of Allergy and Infectious Diseases of the National Institutes of Health Grant HIVRAD P01 AI100148 (to PJB).Attached Files
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Additional details
- PMCID
- PMC5633907
- Eprint ID
- 82395
- Resolver ID
- CaltechAUTHORS:20171016-160803487
- NIH
- 2 P50 GM082545-06
- NIH
- P01 AI100148
- Created
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2017-10-17Created from EPrint's datestamp field
- Updated
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2022-03-22Created from EPrint's last_modified field