ArticleNature biotechnology2013
Strategic addition of an N-linked glycan to a monoclonal antibody improves its HIV-1-neutralizing activity.
Article in Nature biotechnology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers, 1 of them a synthesis that pooled it.
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Who cites it
38 citing papers in PubMed, 1 synthesis or guideline pooled it, 52 citations in OpenAlex.
- A potential antibody repertoire diversification mechanism through tyrosine sulfation for biotherapeutics engineering and production.Frontiers in immunology · 2022Pooled it
- High-sensitive glycomics using seGRAP-mass spectrometry uncovers a conserved N-glycome in single human oocytes.Nature communications · 2026Article
- Optimizing a human monoclonal antibody for better neutralization of SARS-CoV-2.Nature communications · 2025Article
- Tyrosine Sulfation at Antibody Light Chain CDR-1 Increases Binding Affinity and Neutralization Potency to Interleukine-4.International journal of molecular sciences · 2024Article
- Potent neutralization by a RBD antibody with broad specificity for SARS-CoV-2 JN.1 and other variants.Npj viruses · 2024Article
- Editorial: Mechanisms and strategies of unconventional antibody diversification for greater immune adaptability.Frontiers in immunology · 2023Article
- HIV-1 bispecific antibody iMab-N6 exhibits enhanced breadth but not potency over its parental antibodies iMab and N6.Virology journal · 2022Article
- New Opportunities in Glycan Engineering for Therapeutic Proteins.Antibodies (Basel, Switzerland) · 2022Review
- Strategies for Glycoengineering Therapeutic Proteins.Frontiers in chemistry · 2022Review
- Design of a Bispecific HIV Entry Inhibitor Targeting the Cell Receptor CD4 and Viral Fusion Protein Gp41.Frontiers in cellular and infection microbiology · 2022Article
- Shotgun scanning glycomutagenesis: A simple and efficient strategy for constructing and characterizing neoglycoproteins.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- A cross-neutralizing antibody between HIV-1 and influenza virus.PLoS pathogens · 2021Article
- Improving the Pharmacodynamics and In Vivo Activity of ENPP1-Fc Through Protein and Glycosylation Engineering.Clinical and translational science · 2021Article
- Pharmacokinetics Versus In Vitro Antiproliferative Potency to Design a Novel Hyperglycosylated hIFN-α2 Biobetter.Pharmaceutical research · 2021Article
- Broadly neutralizing antibodies for HIV-1: efficacies, challenges and opportunities.Emerging microbes & infections · 2020Review
- GSK3732394: a Multi-specific Inhibitor of HIV Entry.Journal of virology · 2019Article
- Glycoengineering of Antibodies for Modulating Functions.Annual review of biochemistry · 2019Review
- A glycan shield on chimpanzee CD4 protects against infection by primate lentiviruses (HIV/SIV).Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Breaking the law: unconventional strategies for antibody diversification.Nature reviews. Immunology · 2019Review
- Site-selective chemoenzymatic glycoengineering of Fab and Fc glycans of a therapeutic antibody.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Ibalizumab is a humanized monoclonal antibody that binds human CD4--a key receptor for HIV--and blocks HIV-1 infection. However, HIV-1 strains with mutations resulting in loss of an N-linked glycan from the V5 loop of the envelope glycoprotein gp120 are resistant to ibalizumab. Previous structural analysis suggests that this glycan fills a void between the gp120 V5 loop and the ibalizumab light chain, perhaps causing steric hindrance that disrupts viral entry. If this void contributes to HIV-1 resistance to ibalizumab, we reasoned that 'refilling' it by engineering an N-linked glycan into the ibalizumab light chain at a position spatially proximal to gp120 V5 may restore susceptibility to ibalizumab. Indeed, one such ibalizumab variant neutralized 100% of 118 diverse HIV-1 strains tested in vitro, including 10 strains resistant to parental ibalizumab. These findings demonstrate that the strategic placement of a glycan in the variable region of a monoclonal antibody can substantially enhance its activity.
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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.