ArticleJournal of virology2011
Yeast-elicited cross-reactive antibodies to HIV Env glycans efficiently neutralize virions expressing exclusively high-mannose N-linked glycans.
Article in Journal of virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 46 citations in OpenAlex.
- Protein and Glycan Mimicry in HIV Vaccine Design.Journal of molecular biology · 2019Review
- Oligomannose Glycopeptide Conjugates Elicit Antibodies Targeting the Glycan Core Rather than Its Extremities.ACS central science · 2019Article
- Glycan Microarrays as Chemical Tools for Identifying Glycan Recognition by Immune Proteins.Frontiers in chemistry · 2019Review
- Antibody responses to the HIV-1 envelope high mannose patch.Advances in immunology · 2019Review
- Vaccine Elicitation of High Mannose-Dependent Neutralizing Antibodies against the V3-Glycan Broadly Neutralizing Epitope in Nonhuman Primates.Cell reports · 2017Article
- Platelet Factor 4 Inhibits and Enhances HIV-1 Infection in a Concentration-Dependent Manner by Modulating Viral Attachment.AIDS research and human retroviruses · 2016Article
- Article
- Designing synthetic vaccines for HIV.Expert review of vaccines · 2015Review
- Crystal structure of the HIV neutralizing antibody 2G12 in complex with a bacterial oligosaccharide analog of mammalian oligomannose.Glycobiology · 2015Article
- Targeting host-derived glycans on enveloped viruses for antibody-based vaccine design.Current opinion in virology · 2015Review
- Recent strategies targeting HIV glycans in vaccine design.Nature chemical biology · 2014Review
- Directed evolution of multivalent glycopeptides tightly recognized by HIV antibody 2G12.Journal of the American Chemical Society · 2014Article
- High temperature SELMA: evolution of DNA-supported oligomannose clusters which are tightly recognized by HIV bnAb 2G12.Journal of the American Chemical Society · 2014Article
- Synthetic carbohydrate antigens for HIV vaccine design.Current opinion in chemical biology · 2013Review
- Recent advances on the use of structural biology for the design of novel envelope immunogens of HIV-1.Current HIV research · 2013Article
- Development of prophylactic vaccines against HIV-1.Retrovirology · 2013Review
- Antibodies expose multiple weaknesses in the glycan shield of HIV.Nature structural & molecular biology · 2013Article
- Prime-boost immunization of rabbits with HIV-1 gp120 elicits potent neutralization activity against a primary viral isolate.PloS one · 2013Article
- Combinations of griffithsin with other carbohydrate-binding agents demonstrate superior activity against HIV Type 1, HIV Type 2, and selected carbohydrate-binding agent-resistant HIV Type 1 strains.AIDS research and human retroviruses · 2012Article
- High-mannose glycan-dependent epitopes are frequently targeted in broad neutralizing antibody responses during human immunodeficiency virus type 1 infection.Journal of virology · 2012Article
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 HIV envelope (Env) protein uses a dense coat of glycans to mask conserved domains and evade host humoral immune responses. The broadly neutralizing antibody 2G12, which binds a specific cluster of high-mannose glycans on HIV Env, shows that the glycan shield can also serve as a target for neutralizing antibodies. We have described a triple mutant Saccharomyces cerevisiae strain that expresses high-mannose glycoproteins that bind to 2G12. When used to immunize rabbits, this yeast elicits antibodies that bind to gp120-associated glycans but fail to neutralize virus. Here we sought to determine the reason for these discordant results. Affinity purification of sera over columns conjugated with three 2G12-reactive yeast glycoproteins showed that these proteins could adsorb 80% of the antibodies that bind to gp120 glycans. Despite binding to monomeric gp120, these mannose-specific antibodies failed to bind cell surface-expressed trimeric Env. However, when Env was expressed in the presence of the mannosidase inhibitor kifunensine to force retention of high-mannose glycans at all sites, the purified antibodies gained the abilities to bind trimeric Env and to strongly and broadly neutralize viruses produced under these conditions. Combined, these data show that the triple mutant yeast strain elicits antibodies that bind to high-mannose glycans presented on the HIV envelope, but only when they are displayed in a manner not found on native Env trimers. This implies that the underlying structure of the protein scaffold used to present the high-mannose glycans may be critical to allow elicitation of antibodies that recognize trimeric Env and neutralize virus.
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Registered trials
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.