ArticleJournal of virology2002
Stabilization of the soluble, cleaved, trimeric form of the envelope glycoprotein complex of human immunodeficiency virus type 1.
Article in Journal of virology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 329 papers.
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Who cites it
329 citing papers in PubMed, 449 citations in OpenAlex.
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- Structure of HIV-1 Env glycoprotein on virions reveals an alternative fusion subunit organization and native membrane coupling.bioRxiv : the preprint server for biology · 2026Article
- Funding Strategies to Foster Enabling Basic Science Research in the Development of an HIV Vaccine.Current HIV research · 2026Review
- Under the Radar: Immune Evasion, Pathogenesis and Control of HIV Infection.International journal of molecular sciences · 2025Review
- Antibody feedback establishes an affinity brake in the germinal center.bioRxiv : the preprint server for biology · 2025Article
- A modification to heptad repeat 1 of gp41 improves yield and/or quality of soluble pre-fusion HIV-1 envelope glycoprotein trimers.Journal of virology · 2025Article
- Accelerated cGMP production of near-native HIV-1 Env trimers following electroporation transfection and immunogenicity analysis.NPJ vaccines · 2025Article
- Immunofocusing on the conserved fusion peptide of HIV envelope glycoprotein in rhesus macaques.NPJ vaccines · 2025Article
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- A potent and broad CD4 binding site neutralizing antibody with strong ADCC activity from a Chinese HIV-1 elite neutralizer.Cell discovery · 2025Article
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- Immunofocusing on the conserved fusion peptide of HIV envelope glycoprotein in rhesus macaques.bioRxiv : the preprint server for biology · 2025Article
- Antigen persistence and TLR stimulation contribute to induction of a durable HIV-1-specific neutralizing antibody response.Nature communications · 2025Article
- Structural development of the HIV-1 apex-directed PGT145-PGDM1400 antibody lineage.Cell reports · 2025Article
- Inducible cell lines producing replication-defective human immunodeficiency virus particles containing envelope glycoproteins stabilized in a pretriggered conformation.Journal of virology · 2024Article
269 more citing papers are in PubMed but not listed here.
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Authors and funding
12 authors at 4 institutions in 2 countries.
Funding
Abstract
The envelope glycoprotein (Env) complex of human immunodeficiency virus type 1 has evolved a structure that is minimally immunogenic while retaining its natural function of receptor-mediated virus-cell fusion. The Env complex is trimeric; its six individual subunits (three gp120 and three gp41 subunits) are associated by relatively weak, noncovalent interactions. The induction of neutralizing antibodies after vaccination with individual Env subunits has proven very difficult, probably because they are inadequate mimics of the native complex. Our hypothesis is that a stable form of the Env complex, perhaps with additional modifications to rationally alter its antigenic structure, may be a better immunogen than the individual subunits. A soluble form of Env, SOS gp140, can be made that has gp120 stably linked to the gp41 ectodomain by an intermolecular disulfide bond. This protein is fully cleaved at the proteolysis site between gp120 and gp41. However, the gp41-gp41 interactions in SOS gp140 are too weak to maintain the protein in a trimeric configuration. Consequently, purified SOS gp140 is a monomer (N. Schülke, M. S. Vesanen, R. W. Sanders, P. Zhu, D. J. Anselma, A. R. Villa, P. W. H. I. Parren, J. M. Binley, K. H. Roux, P. J. Maddon, J. P. Moore, and W. C. Olson, J. Virol. 76:7760-7776, 2002). Here we describe modifications of SOS gp140 that increase its trimer stability. A variant SOS gp140, designated SOSIP gp140, contains an isoleucine-to-proline substitution at position 559 in the N-terminal heptad repeat region of gp41. This protein is fully cleaved, has favorable antigenic properties, and is predominantly trimeric. SOSIP gp140 trimers are noncovalently associated and can be partially purified by gel filtration chromatography. These gp140 trimers are dissociated into monomers by anionic detergents or heat but are relatively resistant to nonionic detergents, high salt concentrations, or exposure to a mildly acidic pH. SOSIP gp140 should be a useful reagent for structural and immunogenicity studies.
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