ArticleJournal of virology2004
Promoting trimerization of soluble human immunodeficiency virus type 1 (HIV-1) Env through the use of HIV-1/simian immunodeficiency virus chimeras.
Article in Journal of virology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 37 citations in OpenAlex.
- HIV-1-based Virus-like Particles that Morphologically Resemble Mature, Infectious HIV-1 Virions.Viruses · 2019Article
- Conjugation of an scFab domain to the oligomeric HIV envelope protein for use in immune targeting.PloS one · 2019Article
- Stabilization of a soluble, native-like trimeric form of an efficiently cleaved Indian HIV-1 clade C envelope glycoprotein.The Journal of biological chemistry · 2017Article
- Cleavage strongly influences whether soluble HIV-1 envelope glycoprotein trimers adopt a native-like conformation.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Hyperimmune bovine colostrum as a low-cost, large-scale source of antibodies with broad neutralizing activity for HIV-1 envelope with potential use in microbicides.Antimicrobial agents and chemotherapy · 2012Article
- Comparative immunogenicity of subtype a Human Immunodeficiency Virus type 1 envelope exhibiting differential exposure of conserved neutralization epitopes.Journal of virology · 2010Article
- The implications of patterns in HIV diversity for neutralizing antibody induction and susceptibility.Current opinion in HIV and AIDS · 2009Review
- Discordant memory B cell and circulating anti-Env antibody responses in HIV-1 infection.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Optimization of human immunodeficiency virus type 1 envelope glycoproteins with V1/V2 deleted, using virus evolution.Journal of virology · 2009Article
- Characterization of neutralizing antibody responses elicited by clade A envelope immunogens derived from early transmitted viruses.Journal of virology · 2008Article
- N-terminal substitutions in HIV-1 gp41 reduce the expression of non-trimeric envelope glycoproteins on the virus.Virology · 2008Article
- Isolation and characterization of monoclonal antibodies elicited by trimeric HIV-1 Env gp140 protein immunogens.Virology · 2007Article
- Inhibition of HIV-1 entry by antibodies: potential viral and cellular targets.Journal of internal medicine · 2007Review
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- Structure and function of the HIV envelope glycoprotein as entry mediator, vaccine immunogen, and target for inhibitors.Advances in pharmacology (San Diego, Calif.) · 2007Review
- Dynamic evolution of antibody populations in a rhesus macaque infected with attenuated simian immunodeficiency virus identified by surface plasmon resonance.Journal of medical primatology · 2006Article
- Kinetic rates of antibody binding correlate with neutralization sensitivity of variant simian immunodeficiency virus strains.Journal of virology · 2005Article
- Efficient trapping of HIV-1 envelope protein by hetero-oligomerization with an N-helix chimera.Retrovirology · 2005Article
- Soluble mimetics of human immunodeficiency virus type 1 viral spikes produced by replacement of the native trimerization domain with a heterologous trimerization motif: characterization and ligand binding analysis.Journal of virology · 2005Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The envelope proteins (Env) of human immunodeficiency virus type 1 (HIV-1) and simian immunodeficiency virus (SIV) form homo-oligomers in the endoplasmic reticulum. The oligomeric structure of Env is maintained, but is less stable, after cleavage in a Golgi compartment and transport to the surface of infected cells. Functional, virion-associated HIV-1 and SIV Env have an almost exclusively trimeric structure. In addition, a soluble form of SIV Env (gp140) forms a nearly homogeneous population of trimers. Here, we describe the oligomeric structure of soluble, uncleaved HIV-1 gp140 and modifications that promote a stable trimeric structure. Biochemical and biophysical analyses, including sedimentation equilibrium and scanning transmission electron microscopy, revealed that unmodified HIV-1 gp140 purified as a heterogeneous range of oligomeric species, including dimers and aggregates. Deletion of the V2 domain alone or, especially, both the V1 and V2 domains reduced dimer formation but promoted aggregation rather than trimerization. Expressing gp140 with mannose-only oligosaccharides did not eliminate heterogeneity. Replacement of the entire gp41 segment of HIV-1 gp140 or just the N-terminal half (85 amino acids) of this segment with the corresponding region of SIV was sufficient to confer efficient trimerization for gp140 derived from clade B and C isolates. Importantly, the relatively small segment of the HIV Env replaced by SIV sequences contains no known targets of neutralizing antibody. The soluble trimeric form of HIV-1 Env should prove useful for assessment of antigenic structure and immunogenicity.
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