ArticleJournal of acquired immune deficiency syndromes (1999)2016
Distinct HIV-1 Neutralization Potency Profiles of Ibalizumab-Based Bispecific Antibodies.
Article in Journal of acquired immune deficiency syndromes (1999), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 11 citations in OpenAlex.
- Design of a Bispecific HIV Entry Inhibitor Targeting the Cell Receptor CD4 and Viral Fusion Protein Gp41.Frontiers in cellular and infection microbiology · 2022Article
- Combinations of Single Chain Variable Fragments From HIV Broadly Neutralizing Antibodies Demonstrate High Potency and Breadth.Frontiers in immunology · 2021Article
- Conditionally Replicating Vectors Mobilize Chimeric Antigen Receptors against HIV.Molecular therapy. Methods & clinical development · 2020Article
- An update on antiviral antibody-based biopharmaceuticals.International immunopharmacology · 2020Review
- Engineering and characterising a novel, highly potent bispecific antibody iMab-CAP256 that targets HIV-1.Retrovirology · 2019Article
- GSK3732394: a Multi-specific Inhibitor of HIV Entry.Journal of virology · 2019Article
- Ibalizumab, a Novel Monoclonal Antibody for the Management of Multidrug-Resistant HIV-1 Infection.Antimicrobial agents and chemotherapy · 2019Review
- Engineering multi-specific antibodies against HIV-1.Retrovirology · 2018Review
- Ibalizumab Targeting CD4 Receptors, An Emerging Molecule in HIV Therapy.Frontiers in microbiology · 2017Review
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
backgroundPreexposure prophylaxis using antiretroviral agents has been shown to effectively prevent human immunodeficiency virus type 1 (HIV-1) acquisition in high-risk populations. However, the efficacy of these regimens is highly variable, which is thought to be largely due to the varying degrees of adherence to a daily intervention in the populations. Passive immunization using broadly neutralizing antibodies (bNAbs) against HIV-1, with their relatively long half-life and favorable safety profile, could provide an alternative to daily preexposure prophylaxis. However, most bNAbs have a limited breadth, only neutralizing 70%-90% of all HIV-1 strains.
methodsTo overcome the problem of limited antiviral breadth, we proposed that targeting human CD4 and HIV-1 envelope proteins simultaneously may improve virus-neutralization breadth and potency. Therefore, we constructed bispecific antibodies (biAbs) using single-chain variable fragments of anti-gp120 bNAbs fused to ibalizumab (iMab), a humanized monoclonal antibody that binds human CD4, the primary receptor for HIV-1.
resultsSome of our biAbs neutralized 100% of HIV-1 strains tested in vitro at clinically achievable concentrations. Distinct neutralization patterns were observed in this panel of biAbs. Those biAbs with specificity for the CD4-binding site on gp120 demonstrated 100% breadth, as well as slightly improved potency compared with iMab. In contrast, biAbs with specificity for the V1-V2 apex epitope or the V3-glycan epitope on gp120 demonstrated dramatically improved potency; some showed limited gain in neutralization breadth, whereas others (eg, PGT128-LM52 and 123-iMab) improved to 100% breadth.
conclusionOur data suggest that this panel of iMab-based biAbs could be used to probe the parameters for potent HIV-1 neutralization. Moreover, a few of these biAbs warrant further studies and possibly clinical development.
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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.