ArticleJournal of molecular biology2020
Cryo-EM Structure of Full-length HIV-1 Env Bound With the Fab of Antibody PG16.
Article in Journal of molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 64 citations in OpenAlex.
- Bispecific antibodies for cancer therapy: evolution of structural formats and co-targeting strategies from wet-lab to AI-driven in silico modeling.Cancer letters · 2026Review
- Crystal structure of HERV-K envelope glycoprotein surface subunit.Journal of virology · 2026Article
- Investigating the role of a conserved hydrophobic pocket of gp41 in the anti-HIV activity of fusion inhibitors.Protein science : a publication of the Protein Society · 2026Article
- EMoMiS: A pipeline for epitope-based molecular mimicry search in protein structures with potential applications to SARS-CoV-2.Computational and structural biotechnology journal · 2026Article
- Structural Heterogeneity of the Membrane-Interacting Region of the HIV-1 Envelope Glycoprotein.Journal of the American Chemical Society · 2025Article
- Structural Heterogeneity of the Membrane-Interacting Region of the HIV-1 Envelope Glycoprotein.bioRxiv : the preprint server for biology · 2025Article
- The membrane-proximal external region of human immunodeficiency virus (HIV-1) envelope glycoprotein trimers in A18-lipid nanodiscs.Communications biology · 2025Article
- Structural development of the HIV-1 apex-directed PGT145-PGDM1400 antibody lineage.Cell reports · 2025Article
- Conformations of membrane human immunodeficiency virus (HIV-1) envelope glycoproteins solubilized in Amphipol A18 lipid-nanodiscs.Journal of virology · 2024Article
- Design of soluble HIV-1 envelope trimers free of covalent gp120-gp41 bonds with prevalent native-like conformation.Cell reports · 2024Article
- Microsecond dynamics control the HIV-1 Envelope conformation.Science advances · 2024Article
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- Conformations of Human Immunodeficiency Virus Envelope Glycoproteins in Detergents and Styrene-Maleic Acid Lipid Particles.Journal of virology · 2023Article
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- Asymmetric conformations of cleaved HIV-1 envelope glycoprotein trimers in styrene-maleic acid lipid nanoparticles.Communications biology · 2023Article
- Cryo-electron tomography of Birbeck granules reveals the molecular mechanism of langerin lattice formation.eLife · 2022Article
- Structural dynamics reveal isolate-specific differences at neutralization epitopes on HIV Env.iScience · 2022Article
- Functional and Highly Cross-Linkable HIV-1 Envelope Glycoproteins Enriched in a Pretriggered Conformation.Journal of virology · 2022Article
- Global Increases in Human Immunodeficiency Virus Neutralization Sensitivity Due to Alterations in the Membrane-Proximal External Region of the Envelope Glycoprotein Can Be Minimized by Distant State 1-Stabilizing Changes.Journal of virology · 2022Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The HIV-1 envelope protein (Env) is the target of neutralizing antibodies and the template for vaccine immunogen design. The dynamic conformational equilibrium of trimeric Env influences its antigenicity and potential immunogenicity. Antibodies that bind at the trimer apex stabilize a "closed" conformation characteristic of the most difficult to neutralize isolates. A goal of vaccine development is therefore to mimic the closed conformation in a designed immunogen. A disulfide-stabilized, trimeric Env ectodomain-the "SOSIP" construct-has many of the relevant properties; it is also particularly suitable for structure determination. Some single-molecule studies have, however, suggested that the SOSIP trimer is not a good representation of Env on the surface of a virion or an infected cell. We isolated Env (fully cleaved to gp120 and gp41) from the surface of expressing cells using tagged, apex-binding Fab PG16 and determined the structure of the PG16-Env complex by cryo-EM to an overall resolution of 4.6 Å. Placing the only purification tag on the Fab ensured that the isolated Env was continuously stabilized in its closed, native conformation. The Env structure in this complex corresponds closely to the SOSIP structures determined by both x-ray crystallography and cryo-EM. Although the membrane-interacting elements are not resolved in our reconstruction, we can make inferences about the connection between ectodomain and membrane-proximal external region (MPER) by reference to the published cryo-tomography structure of an Env "spike" and the NMR structure of the MPER-transmembrane segment. We discuss these results in view of the conflicting interpretations in the literature.
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