ArticleNature structural & molecular biology2012
Subunit organization of the membrane-bound HIV-1 envelope glycoprotein trimer.
Article in Nature structural & molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 112 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
112 citing papers in PubMed, 154 citations in OpenAlex.
- Vaccine-induced IgG antibodies to V1V2 regions of multiple HIV-1 subtypes correlate with decreased risk of HIV-1 infection.PloS one · 2014Trial
- Viral escape from HIV-1 neutralizing antibodies drives increased plasma neutralization breadth through sequential recognition of multiple epitopes and immunotypes.PLoS pathogens · 2013Trial
- Review
- Molecular Dynamics Investigation of Lipid-Specific Interactions with a Fusion Peptide.Biomolecules · 2024Article
- New Insights into HIV Life Cycle, Th1/Th2 Shift during HIV Infection and Preferential Virus Infection of Th2 Cells: Implications of Early HIV Treatment Initiation and Care.Life (Basel, Switzerland) · 2024Review
- Structure-function analyses reveal key molecular determinants of HIV-1 CRF01_AE resistance to the entry inhibitor temsavir.Nature communications · 2023Article
- Temsavir Modulates HIV-1 Envelope Conformation by Decreasing Its Proteolytic Cleavage.Viruses · 2023Article
- Asymmetric Structures and Conformational Plasticity of the Uncleaved Full-Length Human Immunodeficiency Virus Envelope Glycoprotein Trimer.Journal of virology · 2021Article
- Impact of temperature on the affinity of SARS-CoV-2 Spike glycoprotein for host ACE2.The Journal of biological chemistry · 2021Article
- HIV-1 Envelope Glycoprotein Cell Surface Localization Is Associated with Antibody-Induced Internalization.Viruses · 2021Article
- Review
- Antigenicity and Immunogenicity of HIV-1 Envelope Trimers Complexed to a Small-Molecule Viral Entry Inhibitor.Journal of virology · 2020Article
- Shedding-Resistant HIV-1 Envelope Glycoproteins Adopt Downstream Conformations That Remain Responsive to Conformation-Preferring Ligands.Journal of virology · 2020Article
- Slow Receptor Binding of the Noncytopathic HIV-2Cell reports · 2020Article
- Article
- The lipid membrane of HIV-1 stabilizes the viral envelope glycoproteins and modulates their sensitivity to antibody neutralization.The Journal of biological chemistry · 2020Article
- In Silico Identification of Novel Aromatic Compounds as Potential HIV-1 Entry Inhibitors Mimicking Cellular Receptor CD4.Viruses · 2019Article
- Multimeric Epitope-Scaffold HIV Vaccines Target V1V2 and Differentially Tune Polyfunctional Antibody Responses.Cell reports · 2019Article
- Vaccine-induced V1V2-specific antibodies control and or protect against infection with HIV, SIV and SHIV.Current opinion in HIV and AIDS · 2019Review
- Conformational Engineering of HIV-1 Env Based on Mutational Tolerance in the CD4 and PG16 Bound States.Journal of virology · 2019Article
52 more citing papers are in PubMed but not listed here.
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
The trimeric human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein (Env) spike is a molecular machine that mediates virus entry into host cells and is the sole target for virus-neutralizing antibodies. The mature Env spike results from cleavage of a trimeric glycoprotein precursor, gp160, into three gp120 and three gp41 subunits. Here, we describe an ~11-Å cryo-EM structure of the trimeric HIV-1 Env precursor in its unliganded state. The three gp120 and three gp41 subunits form a cage-like structure with an interior void surrounding the trimer axis. Interprotomer contacts are limited to the gp41 transmembrane region, the torus-like gp41 ectodomain and a trimer-association domain of gp120 composed of the V1, V2 and V3 variable regions. The cage-like architecture, which is unique among characterized viral envelope proteins, restricts antibody access, reflecting requirements imposed by HIV-1 persistence in the host.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.