X‐ray and EM structures of a natively glycosylated HIV‐1 envelope trimer. Issue 10 (10th October 2017)

• Record Type: Journal Article
• Authors: Gristick, Harry B.; Wang, Haoqing; Bjorkman, Pamela J.
• Is Part Of: Acta crystallographica. Volume 73:Issue 10(2017)
• Page Start: 822
• Page End: 828
• Publication Date: 2017-10-10
• Subjects: HIV‐1 envelope -- N‐linked glycans -- X‐ray crystallography -- single‐particle cryo‐EM; X-ray crystallography -- Periodicals; Crystallography -- Periodicals; Molecular biology -- Periodicals; Molecular structure -- Periodicals; Biomolecules -- Structure -- Periodicals; Cytology -- Periodicals; Biomolecules -- Structure; Crystallography; Cytology; Molecular biology; Molecular structure; X-ray crystallography; Periodicals; 548
• DOI: 10.1107/S2059798317013353
• Languages: English
• ISSNs: 2059-7983

Abstract

Abstract : Heavily glycosylated structures of an HIV‐1 envelope trimer derived by X‐ray crystallography and cryo‐EM are compared. 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.