ArticleProceedings of the National Academy of Sciences of the United States of America2000
Cooperative subunit interactions within the oligomeric envelope glycoprotein of HIV-1: functional complementation of specific defects in gp120 and gp41.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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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
35 citing papers in PubMed.
- Natural variations at the E433 site in Env-gp120 β20-β21 cooperate with V2 and gp41 mutations to modulate HIV-1 infectivity.Frontiers in microbiology · 2026Article
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- The membrane-proximal external region of human immunodeficiency virus (HIV-1) envelope glycoprotein trimers in A18-lipid nanodiscs.Communications biology · 2025Article
- Article
- Asymmetric conformations of cleaved HIV-1 envelope glycoprotein trimers in styrene-maleic acid lipid nanoparticles.Communications biology · 2023Article
- Challenging the Existing Model of the Hexameric HIV-1 Gag Lattice and MA Shell Superstructure: Implications for Viral Entry.Viruses · 2021Article
- HIV-1 Entry and Membrane Fusion Inhibitors.Viruses · 2021Review
- Molecular Mechanism of HIV-1 Entry.Trends in microbiology · 2019Review
- Sequential trafficking of Env and Gag to HIV-1 T cell virological synapses revealed by live imaging.Retrovirology · 2019Article
- CD4 occupancy triggers sequential pre-fusion conformational states of the HIV-1 envelope trimer with relevance for broadly neutralizing antibody activity.PLoS biology · 2019Article
- Receptor Activation of HIV-1 Env Leads to Asymmetric Exposure of the gp41 Trimer.PLoS pathogens · 2016Article
- Different infectivity of HIV-1 strains is linked to number of envelope trimers required for entry.PLoS pathogens · 2015Article
- Modular assembly of dimeric HIV fusion inhibitor peptides with enhanced antiviral potency.Bioorganic & medicinal chemistry letters · 2013Article
- HIV-1 neutralizing antibodies: understanding nature's pathways.Immunological reviews · 2013Review
- Inhibition of the HIV-1 spike by single-PG9/16-antibody binding suggests a coordinated-activation model for its three protomeric units.Journal of virology · 2013Article
- Human antibodies that neutralize HIV-1: identification, structures, and B cell ontogenies.Immunity · 2012Review
- Analysis of the subunit stoichiometries in viral entry.PloS one · 2012Article
- Engineering, expression, purification, and characterization of stable clade A/B recombinant soluble heterotrimeric gp140 proteins.Journal of virology · 2012Article
- Intraprotomer masking of third variable loop (V3) epitopes by the first and second variable loops (V1V2) within the native HIV-1 envelope glycoprotein trimer.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
The envelope glycoprotein (Env) of HIV-1 is displayed on the surface of the virion or infected cell as an oligomer of multiple gp120/gp41 complexes. We sought to unravel the relationships between this oligomeric structure and the requirements for sequential interactions with CD4 and coreceptor (CCR5 or CXCR4). We used a quantitative cell fusion assay to examine the effects of coexpressing pairs of Envs, each nonfunctional because of a specific defect in one of the essential properties. We observed efficient fusion activity upon coexpression of two Env variants, one containing a gp41 subunit with a mutated fusion peptide and the other containing a gp120 subunit with a mutated CD4 binding site or a mismatched coreceptor specificity. We also observed fusion upon coexpression of two Env variants with distinct gp120 defects, i.e., a CD4 binding site mutation and the incorrect coreceptor specificity determinants. Coimmunoprecipitation experiments verified the efficient formation of mixed oligomers, suggesting that the observed fusion reflected subunit complementation within the oligomeric complex. These results support a model in which cooperative subunit interactions within the Env oligomer result in concerted conformational changes upon receptor binding, resulting in activation for fusion. The implications of these findings for Env function and virus neutralization are discussed.
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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.