Acta Crystallographica Section D: Structural Biology
Acta Crystallographica Section D: Structural Biology
3 years ago

X-ray and EM structures of a natively glycosylated HIV-1 envelope trimer

X-ray and EM structures of a natively glycosylated HIV-1 envelope trimer
Pamela J. Bjorkman, Harry B. Gristick, Haoqing Wang
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.Heavily glycosylated structures of an HIV-1 envelope trimer derived by X-ray crystallography and cryo-EM are compared.

Publisher URL: http://onlinelibrary.wiley.com/resolve/doi

DOI: 10.1107/S2059798317013353

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