ArticleThe Journal of biological chemistry2010
Design of a non-glycosylated outer domain-derived HIV-1 gp120 immunogen that binds to CD4 and induces neutralizing antibodies.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 36 citations in OpenAlex.
- Strategies for inducing effective neutralizing antibody responses against HIV-1.Expert review of vaccines · 2019Review
- Antigenicity and Immunogenicity of Differentially Glycosylated Hepatitis C Virus E2 Envelope Proteins Expressed in Mammalian and Insect Cells.Journal of virology · 2019Article
- Design, display and immunogenicity of HIV1 gp120 fragment immunogens on virus-like particles.Vaccine · 2018Article
- Bacterially expressed HIV-1 gp120 outer-domain fragment immunogens with improved stability and affinity for CD4-binding site neutralizing antibodies.The Journal of biological chemistry · 2018Article
- Evolution of Neutralization Response in HIV-1 Subtype C-Infected Individuals Exhibiting Broad Cross-Clade Neutralization of HIV-1 Strains.Frontiers in immunology · 2018Article
- Glycosylation of the core of the HIV-1 envelope subunit protein gp120 is not required for native trimer formation or viral infectivity.The Journal of biological chemistry · 2017Article
- Structure-based Design of Cyclically Permuted HIV-1 gp120 Trimers That Elicit Neutralizing Antibodies.The Journal of biological chemistry · 2017Article
- Antigenicity and immunogenicity of a trimeric envelope protein from an Indian clade C HIV-1 isolate.The Journal of biological chemistry · 2015Article
- Article
- Eliciting neutralizing antibodies with gp120 outer domain constructs based on M-group consensus sequence.Virology · 2014Article
- Immune focusing and enhanced neutralization induced by HIV-1 gp140 chemical cross-linking.Journal of virology · 2013Article
- Advances in structure-based vaccine design.Current opinion in virology · 2013Review
- Design of an Escherichia coli expressed HIV-1 gp120 fragment immunogen that binds to b12 and induces broad and potent neutralizing antibodies.The Journal of biological chemistry · 2013Article
- Isolation of a high affinity neutralizing monoclonal antibody against 2009 pandemic H1N1 virus that binds at the 'Sa' antigenic site.PloS one · 2013Article
- Structural insights into key sites of vulnerability on HIV-1 Env and influenza HA.Immunological reviews · 2012Review
- Article
- Existence of different structural intermediates and aggregates on the folding pathway of ovalbumin.Journal of fluorescence · 2012Article
- Antigenicity and Immunogenicity in HIV-1 Antibody-Based Vaccine Design.Journal of AIDS & clinical research · 2012Article
- Article
- Envelope deglycosylation enhances antigenicity of HIV-1 gp41 epitopes for both broad neutralizing antibodies and their unmutated ancestor antibodies.PLoS pathogens · 2011Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The outer domain (OD) of the HIV-1 envelope glycoprotein gp120 is an important target for vaccine design as it contains a number of conserved epitopes, including a large fraction of the CD4 binding site. Attempts to design OD-based immunogens in the past have met with little success. We report the design and characterization of an Escherichia coli-expressed OD-based immunogen (OD(EC)), based on the sequence of the HxBc2 strain. The OD(EC)-designed immunogen lacks the variable loops V1V2 and V3 and incorporates 11 designed mutations at the interface of the inner and the outer domains of gp120. Biophysical studies showed that OD(EC) is folded and protease-resistant, whereas OD(EC) lacking the designed mutations is highly aggregation-prone. In contrast to previously characterized OD constructs, OD(EC) bound CD4 and the broadly neutralizing antibody b12 but not the non-neutralizing antibodies b6 and F105. Upon immunization in rabbits, OD(EC) was highly immunogenic, and the sera showed measurable neutralization for four subtype B and one subtype C virus including two b12-resistant viruses. In contrast, sera from rabbits immunized with gp120 did not neutralize any of the viruses. OD(EC) is the first example of a gp120 fragment-based immunogen that yields significant neutralizing antibodies.
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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.