ArticleJournal of virology2012
Engineering, expression, purification, and characterization of stable clade A/B recombinant soluble heterotrimeric gp140 proteins.
Article in Journal of virology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 32 citations in OpenAlex.
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- Investigation of Antibody Tolerance in Methanol for Analytical Purposes: Methanol Effect Patterns and Molecular Mechanisms.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Triple tandem trimer immunogens for HIV-1 and influenza nucleic acid-based vaccines.NPJ vaccines · 2024Article
- Characterization of a vaccine-elicited human antibody with sequence homology to VRC01-class antibodies that binds the C1C2 gp120 domain.Science advances · 2022Article
- ARTEMIS: A Novel Mass-Spec Platform for HLA-Restricted Self and Disease-Associated Peptide Discovery.Frontiers in immunology · 2021Article
- B cell clonal lineage alterations upon recombinant HIV-1 envelope immunization of rhesus macaques.PLoS pathogens · 2018Article
- Increased breadth of HIV-1 neutralization achieved by diverse antibody clones each with limited neutralization breadth.PloS one · 2018Article
- Development of an anti-HIV vaccine eliciting broadly neutralizing antibodies.AIDS research and therapy · 2017Review
- A heterologous prime-boosting strategy with replicating Vaccinia virus vectors and plant-produced HIV-1 Gag/dgp41 virus-like particles.Virology · 2017Article
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- A New Glycan-Dependent CD4-Binding Site Neutralizing Antibody Exerts Pressure on HIV-1 In Vivo.PLoS pathogens · 2015Article
- Immunogenic Display of Purified Chemically Cross-Linked HIV-1 Spikes.Journal of virology · 2015Article
- Diverse antibody genetic and recognition properties revealed following HIV-1 envelope glycoprotein immunization.Journal of immunology (Baltimore, Md. : 1950) · 2015Article
- Antigenicity and immunogenicity of a trimeric envelope protein from an Indian clade C HIV-1 isolate.The Journal of biological chemistry · 2015Article
- Diverse recombinant HIV-1 Envs fail to activate B cells expressing the germline B cell receptors of the broadly neutralizing anti-HIV-1 antibodies PG9 and 447-52D.Journal of virology · 2014Article
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- Article
- Characterization of humoral responses to soluble trimeric HIV gp140 from a clade A Ugandan field isolate.Journal of translational medicine · 2013Article
- Purification of recombinant vaccinia virus-expressed monomeric HIV-1 gp120 to apparent homogeneity.Protein expression and purification · 2013Article
- Conformation-dependent recognition of HIV gp120 by designed ankyrin repeat proteins provides access to novel HIV entry inhibitors.Journal of virology · 2013Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The envelope glycoprotein (Env) of human immunodeficiency virus type 1 (HIV-1) is composed of two noncovalently associated subunits: an extracellular subunit (gp120) and a transmembrane subunit (gp41). The functional unit of Env on the surface of infectious virions is a trimer of gp120/gp41 heterodimers. Env is the target of anti-HIV neutralizing antibodies. A considerable effort has been invested in the engineering of recombinant soluble forms of the virion-associated Env trimer as vaccine candidates to elicit anti-HIV neutralizing antibody responses. These soluble constructs contain three gp120 subunits and the extracellular segments of the corresponding gp41 subunits. The individual gp120/gp41 protomers on these soluble trimers are identical in amino acid sequence (homotrimers). Here, we engineered novel soluble trimeric gp140 proteins that are formed by the association of gp140 protomers that differ in amino acid sequence and glycosylation patterns (heterotrimers). Specifically, we engineered soluble heterotrimeric proteins composed of clade A and clade B Env protomers. The clade A gp140 protomers were derived from viruses isolated during acute infection (Q168a2, Q259d2.17, and Q461e2), whereas the clade B gp140 protomers were derived from a virus isolated during chronic infection (SF162). The amino acid sequence divergence between the clade A and the clade B Envs is approximately 24%. Neutralization epitopes in the CD4 binding sites and coreceptor binding sites, as well as the membrane-proximal external region (MPER), were differentially expressed on the heterotrimeric and homotrimeric proteins. The heterotrimeric gp140s elicited broader anti-tier 1 isolate neutralizing antibody responses than did the homotrimeric gp140s.
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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.